Cultivation of kidney mesangial cells (MC) is easily established and widely used. MCs produce several complementary regulatory proteins (C). We studied whether MC synthesized components C (C3, C5, C8). MC culture was established from the normal portion of nephrectomy for kidney cancer. After growing to a close meeting in RPMI / 17% FBS and resting 24 hours in RPMI / 0.5% FBS, MC stimulated up to 72 hours with IL-1β or IL-6 (10, 100, 1000 U / mL).
Both C5 and C8 detection by ELISA. While C3 is present in supernatant in basal conditions (15.5-107.6 ng / 10 (6) cells / 24 hours) in different MC lines. IL-1β regulates synthesis with 2.4-4.5 folds, while IL-6 does not show any effect. The c3 synthetic rate is cell 1.76 ng / 10 (6) under IL-1 stimulation versus basal level 0.37 ng / hour / 10 (6) cells. MC C3 production, especially induced by IL-1 may have pathogenetic relevance in glomerulonephritis.
Rooperol, cytokine synthesis inhibitors, reduces breathing explosions on leukocytes and human macrophies and mice.
Chemiluminescence enhanced by Luminol is measured in all fresh human blood, or human neutrophils are isolated from the blood of heparation, macrophages of alveolar humans and macrophages of alveolar rats which are stimulated with endotoxin bacteria (LPS). Esther TetraAceTate from Rooperol, a recatechol that shows anticoytokine activity, added to the cell simultaneously with LPS inhibiting the breathing explosion. The effective concentration of Rooperol is in the range of 1-10 mothers depending on the type of cell and in accordance with the inhibition of the production of nitrate oxide by macrophages of mice alveolar. Thus Roerol can reduce some effects of excessive phagocytic activity and inflammatory reactions but by extinguishing free radical production can also reduce resistance to bacterial infections.
Leptin increases survival and induces migration, degranulation, and synthesis of cytokines from human basophyl.
Basophils are the rarest leukocytes in human blood, but are now recognized as one of the most important immunomodulatory cells and the effector in allergic inflammation. Leptin, a member of the Cytokine IL-6 family, has a metabolic effect as an adipocine, and is also known to participate in the pathogenesis of inflammatory reactions. Because there is an epidemiological relationship between obesity and allergies, we examine whether the basophyl function is modified by leptin.
We found that the human basophyl expressed Leptin receptor (LEPR) at MRNA and surface protein levels, which was regulated by IL-33. Leptin exerts strong effects on several basophyl functions. This causes a strong migration response to human basophyl, potentially similar to the basophil-active kemokine. Also, Leptin increases the survival of human basophyl, even though its potential is less than IL-3. In addition, CD63, the marker of basophil activation is stated on the cell surface, regulated by leptin, the effect is neutralized by blocking LEPR.
Basophyl degranulation assessment and cytokine synthesis found that leptin shows a strong priming effect on human basophyl degranulation in response to FCεRI aggregation and induces Th2, but not the production of cytokines by cells. In short, these findings indicate that leptin may be the main molecule that mediates the effects of adipocytes in inflammatory cells such as basophiles by binding LEPR and activating cellular functions, which may worsen allergic inflammation.
Learn at the synthesis of complement components by human kidney mesangial cells in culture. Assessment of cytokine effects.
Cultivation of kidney mesangial cells (MC) is easily established and widely used. MCs produce several complementary regulatory proteins (C). We studied whether MC synthesized components C (C3, C5, C8). MC culture was established from the normal portion of nephrectomy for kidney cancer. After growing to a close meeting in RPMI / 17% FBS and resting 24 hours in RPMI / 0.5% FBS, MC stimulated up to 72 hours with IL-1β or IL-6 (10, 100, 1000 U / mL). Both C5 and C8 detection by ELISA.
While C3 is present in supernatant in basal conditions (15.5-107.6 ng / 10 (6) cells / 24 hours) in different MC lines. IL-1β regulates synthesis with 2.4-4.5 folds, while IL-6 does not show any effect. The c3 synthetic rate is cell 1.76 ng / 10 (6) under IL-1 stimulation versus basal level 0.37 ng / hour / 10 (6) cells. MC C3 production, especially induced by IL-1 may have pathogenetic relevance in glomerulonephritis.
Rooperol, cytokine synthesis inhibitors, reduces breathing explosions on leukocytes and human macrophies and mice.
Chemiluminescence enhanced by Luminol is measured in all fresh human blood, or human neutrophils are isolated from the blood of heparation, macrophages of alveolar humans and macrophages of alveolar rats which are stimulated with endotoxin bacteria (LPS). Esther TetraAceTate from Rooperol, a recatechol that shows anticoytokine activity, added to the cell simultaneously with LPS inhibiting the breathing explosion. The effective concentration of Rooperol is in the range of 1-10 mothers depending on the type of cell and in accordance with the inhibition of the production of nitrate oxide by macrophages of mice alveolar. Thus Roerol can reduce some effects of excessive phagocytic activity and inflammatory reactions but by extinguishing free radical production can also reduce resistance to bacterial infections.
Leptin increases survival and induces migration, degranulation, and synthesis of cytokines from human basophyl.
Basophils are the rarest leukocytes in human blood, but are now recognized as one of the most important immunomodulatory cells and the effector in allergic inflammation. Leptin, a member of the Cytokine IL-6 family, has a metabolic effect as an adipocine, and is also known to participate in the pathogenesis of inflammatory reactions. Because there is an epidemiological relationship between obesity and allergies, we examine whether the basophyl function is modified by leptin. We found that the human basophyl expressed Leptin receptor (LEPR) at MRNA and surface protein levels, which was regulated by IL-33.
Leptin exerts strong effects on several basophyl functions. This causes a strong migration response to human basophyl, potentially similar to the basophil-active kemokine. Also, Leptin increases the survival of human basophyl, even though its potential is less than IL-3. In addition, CD63, the marker of basophil activation is stated on the cell surface, regulated by leptin, the effect is neutralized by blocking LEPR. Basophyl degranulation assessment and cytokine synthesis found that leptin shows a strong priming effect on human basophyl degranulation in response to FCεRI aggregation and induces Th2, but not the production of cytokines by cells.
TWEAK, recombinant / TNFSF12, recombinant (Human) |
054-85 |
PHOENIX PEPTIDE |
10 μg |
EUR 261.36 |
Recombinant Human PGⅡ |
E21-RA29-1 |
EnoGene |
- |
Ask for price |
Recombinant Human GC |
MBS7616369-005mg |
MyBiosource |
0.05mg |
EUR 405 |
Recombinant Human GC |
MBS7616369-02mg |
MyBiosource |
0.2mg |
EUR 760 |
Recombinant Human GC |
MBS7616369-1mg |
MyBiosource |
1mg |
EUR 2175 |
Recombinant Human GC |
MBS7616369-5x1mg |
MyBiosource |
5x1mg |
EUR 8410 |
Recombinant Human GH |
MBS7608417-005mg |
MyBiosource |
0.05mg |
EUR 405 |
Recombinant Human GH |
MBS7608417-02mg |
MyBiosource |
0.2mg |
EUR 760 |
Recombinant Human GH |
MBS7608417-1mg |
MyBiosource |
1mg |
EUR 2175 |
Recombinant Human GH |
MBS7608417-5x1mg |
MyBiosource |
5x1mg |
EUR 8410 |
Recombinant Human GS |
MBS7608504-005mg |
MyBiosource |
0.05mg |
EUR 345 |
Recombinant Human GS |
MBS7608504-02mg |
MyBiosource |
0.2mg |
EUR 635 |
Recombinant Human GS |
MBS7608504-1mg |
MyBiosource |
1mg |
EUR 1800 |
Recombinant Human GS |
MBS7608504-5x1mg |
MyBiosource |
5x1mg |
EUR 6955 |
Recombinant Human C6 |
MBS7608602-005mg |
MyBiosource |
0.05mg |
EUR 345 |
Recombinant Human C6 |
MBS7608602-02mg |
MyBiosource |
0.2mg |
EUR 635 |
Recombinant Human C6 |
MBS7608602-1mg |
MyBiosource |
1mg |
EUR 1800 |
Recombinant Human C6 |
MBS7608602-5x1mg |
MyBiosource |
5x1mg |
EUR 6955 |
Recombinant Human AR |
MBS7612815-005mg |
MyBiosource |
0.05mg |
EUR 405 |
Recombinant Human AR |
MBS7612815-02mg |
MyBiosource |
0.2mg |
EUR 760 |
Recombinant Human AR |
MBS7612815-1mg |
MyBiosource |
1mg |
EUR 2175 |
Recombinant Human FH |
MBS7613325-005mg |
MyBiosource |
0.05mg |
EUR 405 |
Recombinant Human FH |
MBS7613325-02mg |
MyBiosource |
0.2mg |
EUR 760 |
Recombinant Human FH |
MBS7613325-1mg |
MyBiosource |
1mg |
EUR 2175 |
Recombinant Human FH |
MBS7613325-5x1mg |
MyBiosource |
5x1mg |
EUR 8410 |
Recombinant Human HP |
MBS7614251-005mg |
MyBiosource |
0.05mg |
EUR 405 |
Recombinant Human HP |
MBS7614251-02mg |
MyBiosource |
0.2mg |
EUR 760 |
Recombinant Human HP |
MBS7614251-1mg |
MyBiosource |
1mg |
EUR 2175 |
Recombinant Human HP |
MBS7614251-5x1mg |
MyBiosource |
5x1mg |
EUR 8410 |
Recombinant Human AR |
MBS7612815-5x1mg |
MyBiosource |
5x1mg |
EUR 8410 |
Recombinant Human CP |
MBS7613562-005mg |
MyBiosource |
0.05mg |
EUR 405 |
Recombinant Human CP |
MBS7613562-02mg |
MyBiosource |
0.2mg |
EUR 760 |
Recombinant Human CP |
MBS7613562-1mg |
MyBiosource |
1mg |
EUR 2175 |
Recombinant Human CP |
MBS7613562-5x1mg |
MyBiosource |
5x1mg |
EUR 8410 |
Recombinant Human TH |
MBS7613924-005mg |
MyBiosource |
0.05mg |
EUR 345 |
Recombinant Human TH |
MBS7613924-02mg |
MyBiosource |
0.2mg |
EUR 635 |
Recombinant Human TH |
MBS7613924-1mg |
MyBiosource |
1mg |
EUR 1800 |
Recombinant Human TH |
MBS7613924-5x1mg |
MyBiosource |
5x1mg |
EUR 6955 |
Recombinant Human C5 |
MBS7609068-005mg |
MyBiosource |
0.05mg |
EUR 345 |
Recombinant Human C5 |
MBS7609068-02mg |
MyBiosource |
0.2mg |
EUR 635 |
Recombinant Human C5 |
MBS7609068-1mg |
MyBiosource |
1mg |
EUR 1800 |
Recombinant Human C5 |
MBS7609068-5x1mg |
MyBiosource |
5x1mg |
EUR 6955 |
Recombinant Human Rb |
MBS7609212-005mg |
MyBiosource |
0.05mg |
EUR 470 |
Recombinant Human Rb |
MBS7609212-02mg |
MyBiosource |
0.2mg |
EUR 885 |
Recombinant Human Rb |
MBS7609212-1mg |
MyBiosource |
1mg |
EUR 2540 |
Recombinant Human Rb |
MBS7609212-5x1mg |
MyBiosource |
5x1mg |
EUR 9820 |
Recombinant Human FH |
MBS7609262-005mg |
MyBiosource |
0.05mg |
EUR 560 |
Recombinant Human FH |
MBS7609262-02mg |
MyBiosource |
0.2mg |
EUR 1060 |
Recombinant Human FH |
MBS7609262-1mg |
MyBiosource |
1mg |
EUR 3065 |
Recombinant Human FH |
MBS7609262-5x1mg |
MyBiosource |
5x1mg |
EUR 11850 |
Recombinant Human C4 |
MBS7609327-005mg |
MyBiosource |
0.05mg |
EUR 405 |
Recombinant Human C4 |
MBS7609327-02mg |
MyBiosource |
0.2mg |
EUR 760 |
Recombinant Human C4 |
MBS7609327-1mg |
MyBiosource |
1mg |
EUR 2175 |
Recombinant Human C4 |
MBS7609327-5x1mg |
MyBiosource |
5x1mg |
EUR 8410 |
Recombinant Human C4 |
MBS7609328-005mg |
MyBiosource |
0.05mg |
EUR 405 |
Recombinant Human C4 |
MBS7609328-02mg |
MyBiosource |
0.2mg |
EUR 760 |
Recombinant Human C4 |
MBS7609328-1mg |
MyBiosource |
1mg |
EUR 2175 |
Recombinant Human C4 |
MBS7609328-5x1mg |
MyBiosource |
5x1mg |
EUR 8410 |
Recombinant Human GH |
P1223-.1 |
ApexBio |
10X10ug |
EUR 240 |
Description: Peptides & Proteins|Recombinant Proteins |
Recombinant Human GH |
P1223-.5 |
ApexBio |
50X10ug |
EUR 538.4 |
Description: Peptides & Proteins|Recombinant Proteins |
DR3 (human):Fc (human), (recombinant) |
MBS566215-005mg |
MyBiosource |
0.05mg |
EUR 585 |
DR3 (human):Fc (human), (recombinant) |
MBS566215-5x005mg |
MyBiosource |
5x0.05mg |
EUR 2585 |
Recombinant Human REC8 |
MBS7613173-005mg |
MyBiosource |
0.05mg |
EUR 405 |
Recombinant Human REC8 |
MBS7613173-02mg |
MyBiosource |
0.2mg |
EUR 760 |
Recombinant Human REC8 |
MBS7613173-1mg |
MyBiosource |
1mg |
EUR 2175 |
Recombinant Human REC8 |
MBS7613173-5x1mg |
MyBiosource |
5x1mg |
EUR 8410 |
Recombinant Human PRL |
AP76222 |
SAB |
1mg |
EUR 2369 |
|
Recombinant Human PRL |
CM10-10ug |
Novoprotein |
10ug |
EUR 169.2 |
Description: Lyophilized from a 0.2 μm filtered solution of 20mM PB,150mM NaCl,pH7.4. |
Recombinant Human PRL |
CM10-1mg |
Novoprotein |
1mg |
EUR 2008.8 |
Description: Lyophilized from a 0.2 μm filtered solution of 20mM PB,150mM NaCl,pH7.4. |
Recombinant Human PRL |
CM10-500ug |
Novoprotein |
500ug |
EUR 1423.2 |
Description: Lyophilized from a 0.2 μm filtered solution of 20mM PB,150mM NaCl,pH7.4. |
Recombinant Human PRL |
CM10-50ug |
Novoprotein |
50ug |
EUR 363.6 |
Description: Lyophilized from a 0.2 μm filtered solution of 20mM PB,150mM NaCl,pH7.4. |
Recombinant Human CSK |
Z500098 |
ABM |
10 µg |
EUR 370 |
Description: CSK is a cytoplasmic tyrosine kinase that has been shown to downregulate the tyrosine kinase activity of the c-src through tyrosine phosphorylation of the c-src carboxy terminus . A yeast 2-hybrid system has been used to identify proteins associated with CSK. The Src homology-3 (SH3) domain of CSK associates with a proline-rich region of PEP, a protein-tyrosine phosphatase expressed in hemopoietic cells . This association is highly specific and it is speculated that PEP may be an effector and/or regulator of CSK in T cells and other hemopoietic cells. |
Recombinant Human BMX |
Z500413 |
ABM |
10 µg |
EUR 370 |
Description: Recombinant full-length human BMX was expressed by baculovirus in Sf9 insect cells using an N-terminal GST tag. The BMX gene encodes a non-receptor tyrosine kinase, which may play a role in the growth and differentiation of hematopoietic cells. The BMX gene is located on chromosomal band Xp22.2 between the DXS197 and DXS207 loci. Interestingly, chromosome X also contains the closest relative of BMX, the BTK gene, implicated in X-linked agammaglobulinemia. BMX is found to induce activation of the Stat signalling pathway. |
Recombinant Human EGF |
Z100139 |
ABM |
1.0 mg |
EUR 205 |
Description: Epidermal growth factor (EGF) is a small mitogenic protein that is thought to be involved in mechanisms such as normal cell growth, oncogenesis, and wound healing. This protein shows both strong sequential and functional homology with human type-alpha transforming growth factor (hTGF alpha), which is a competitor for EGF receptor sites. EGF receptors are expressed in almost all types of tissues. Parietal endoderm, mature skeletal muscles, and hematopoietic tissues do not express the receptor. The EGF receptor, designated HER1, is a 170 kDa transmembrane glycoprotein with a length of 1186 amino acids. It is identical with a previously described glycoprotein called SA-7 (species antigen 7). The extracellular receptor domain has a length of 621 amino acids, including 11 glycosylated asparagine residues and 51 cysteine residues. This domain contains the EGF binding site and also binds mammalian TGF-alpha. |
Recombinant Human GH1 |
Z100265 |
ABM |
500 µg |
EUR 85 |
Description: The physiological activity for which growth hormone is best known is the promotion of growth of bone, cartilage, and soft tissues. Detectable levels of growth hormone are found throughout the remainder of adulthood, suggesting other functions in addition to promotion of growth. Growth hormone may be important for the maintenance of lean body mass; most growth-promoting effects of growth hormone are mediated by IGF-1 the synthesis of which is regulated by growth hormone. The biological activities of growth hormone are mediated by receptors belonging to one of the cytokine receptor families. Growth hormone has been shown to be produced by T cells, B cells, and macrophages. In human lymphocytes growth hormone appears to up-regulate its own expression. Growth hormone appears to act as an enhancer of immune responses and is produced in considerable amounts by T helper cells. |
Recombinant Human GH1 |
Z100269 |
ABM |
1.0 mg |
EUR 150 |
Description: The physiological activity for which growth hormone is best known is the promotion of growth of bone, cartilage, and soft tissues. Detectable levels of growth hormone are found throughout the remainder of adulthood, suggesting other functions in addition to promotion of growth. Growth hormone may be important for the maintenance of lean body mass; most growth-promoting effects of growth hormone are mediated by IGF-1 the synthesis of which is regulated by growth hormone. The biological activities of growth hormone are mediated by receptors belonging to one of the cytokine receptor families. Growth hormone has been shown to be produced by T cells, B cells, and macrophages. In human lymphocytes growth hormone appears to up-regulate its own expression. Growth hormone appears to act as an enhancer of immune responses and is produced in considerable amounts by T helper cells. |
Recombinant Human IL2 |
Z100485 |
ABM |
50 µg |
EUR 85 |
Description: A helical bundle of 4 α-helices, IL2 is an immunoregulatory cytokine that is expressed by CD4+/CD8+ T cells, γδ T cells, B cells, eosinophils and dendritic cells. IL2 stimulates growth and differentiation of B-cells, NK cells, lymphokine-activated killer cells, monocytes, macrophages and oligodendrocytes. While Human IL2 shares 56% and 66% amino acid sequence identity with mouse and rat IL2, respectively only human and mouse IL2 exhibit cross-species activity. Characteristically, IL2 exerts both autocrine and paracrine activity on T cells. In a regulatory role, IL2 is important for the development, survival, and function of regulatory T cells, it enhances Fas-mediated activation-induced cell death, and it inhibits the development of inflammatory Th17 cells. Recombinant Human IL2 is a non-glycosylated polypeptide that contains one intrachain disulfide bond. |
Recombinant Human IL2 |
Z100487 |
ABM |
100 µg |
EUR 145 |
Description: A helical bundle of 4 α-helices, IL2 is an immunoregulatory cytokine that is expressed by CD4+/CD8+ T cells, γδ T cells, B cells, eosinophils and dendritic cells. IL2 stimulates growth and differentiation of B-cells, NK cells, lymphokine-activated killer cells, monocytes, macrophages and oligodendrocytes. While Human IL2 shares 56% and 66% amino acid sequence identity with mouse and rat IL2, respectively only human and mouse IL2 exhibit cross-species activity. Characteristically, IL2 exerts both autocrine and paracrine activity on T cells. In a regulatory role, IL2 is important for the development, survival, and function of regulatory T cells, it enhances Fas-mediated activation-induced cell death, and it inhibits the development of inflammatory Th17 cells. Recombinant Human IL2 is a non-glycosylated polypeptide that contains one intrachain disulfide bond. |
Recombinant Human IL2 |
Z100489 |
ABM |
1.0 mg |
EUR 615 |
Description: A helical bundle of 4 α-helices, IL2 is an immunoregulatory cytokine that is expressed by CD4+/CD8+ T cells, γδ T cells, B cells, eosinophils and dendritic cells. IL2 stimulates growth and differentiation of B-cells, NK cells, lymphokine-activated killer cells, monocytes, macrophages and oligodendrocytes. While Human IL2 shares 56% and 66% amino acid sequence identity with mouse and rat IL2, respectively only human and mouse IL2 exhibit cross-species activity. Characteristically, IL2 exerts both autocrine and paracrine activity on T cells. In a regulatory role, IL2 is important for the development, survival, and function of regulatory T cells, it enhances Fas-mediated activation-induced cell death, and it inhibits the development of inflammatory Th17 cells. Recombinant Human IL2 is a non-glycosylated polypeptide that contains one intrachain disulfide bond. |
Recombinant Human IL3 |
Z100515 |
ABM |
10 µg |
EUR 85 |
Description: IL3 is produced mainly by T cells following cell activation by antigens and mitogens, but also by keratinocytes, natural killer cells, mast cells, endothelial cells, and monocytes. The analysis of bacterial- derived recombinant IL3 shows that glycosylation is not required for activity. IL3 sequences are evolutionarily less well conserved with human and murine IL3 sharing approximately 29% homology (at the protein level) and murine and rat IL3 sharing approximately 54% homology. IL3 receptors are expressed on macrophages, mast cells, eosinophils, megakaryocytes, basophils, bone marrow progenitor cells and various myeloid leukemia cells. Binding of IL3 to its receptor causes specific phosphorylation of a 150 kDa membrane glycoprotein. Recombinant human IL3 is a non-glycosylated globular protein. |
Recombinant Human IL3 |
Z100517 |
ABM |
50 µg |
EUR 155 |
Description: IL3 is produced mainly by T cells following cell activation by antigens and mitogens, but also by keratinocytes, natural killer cells, mast cells, endothelial cells, and monocytes. The analysis of bacterial- derived recombinant IL3 shows that glycosylation is not required for activity. IL3 sequences are evolutionarily less well conserved with human and murine IL3 sharing approximately 29% homology (at the protein level) and murine and rat IL3 sharing approximately 54% homology. IL3 receptors are expressed on macrophages, mast cells, eosinophils, megakaryocytes, basophils, bone marrow progenitor cells and various myeloid leukemia cells. Binding of IL3 to its receptor causes specific phosphorylation of a 150 kDa membrane glycoprotein. Recombinant human IL3 is a non-glycosylated globular protein. |
Recombinant Human IL3 |
Z100519 |
ABM |
1.0 mg |
EUR 2260 |
Description: IL3 is produced mainly by T cells following cell activation by antigens and mitogens, but also by keratinocytes, natural killer cells, mast cells, endothelial cells, and monocytes. The analysis of bacterial- derived recombinant IL3 shows that glycosylation is not required for activity. IL3 sequences are evolutionarily less well conserved with human and murine IL3 sharing approximately 29% homology (at the protein level) and murine and rat IL3 sharing approximately 54% homology. IL3 receptors are expressed on macrophages, mast cells, eosinophils, megakaryocytes, basophils, bone marrow progenitor cells and various myeloid leukemia cells. Binding of IL3 to its receptor causes specific phosphorylation of a 150 kDa membrane glycoprotein. Recombinant human IL3 is a non-glycosylated globular protein. |
Recombinant Human IL4 |
Z100545 |
ABM |
10 µg |
EUR 60 |
Description: IL4 is produced mainly by a sub-population of activated T helper cells which also secrete IL5 and IL6. The biological activities of IL4 are mediated by a specific receptor, the extracellular domain of which is related to the receptors for EPO, IL6, and the beta chain of the IL-2 receptor. IL4 participates in several B-cell activation processes as well as of other cell types. A co-stimulator of DNA-synthesis, IL4 induces the expression of class II MHC molecules on resting B-cells, enhances both secretion and cell surface expression of IgE and IgG1, and also regulates the expression of the low affinity Fc receptor for IgE on both lymphocytes and monocytes. Pre-treatment of macrophages with IL4 prevents the production of IL1, TNF-alpha and prostaglandins in response to activation of the cells by bacterial endotoxins or IFN-gamma. |
Recombinant Human IL4 |
Z100547 |
ABM |
100 µg |
EUR 470 |
Description: IL4 is produced mainly by a sub-population of activated T helper cells which also secrete IL5 and IL6. The biological activities of IL4 are mediated by a specific receptor, the extracellular domain of which is related to the receptors for EPO, IL6, and the beta chain of the IL-2 receptor. IL4 participates in several B-cell activation processes as well as of other cell types. A co-stimulator of DNA-synthesis, IL4 induces the expression of class II MHC molecules on resting B-cells, enhances both secretion and cell surface expression of IgE and IgG1, and also regulates the expression of the low affinity Fc receptor for IgE on both lymphocytes and monocytes. Pre-treatment of macrophages with IL4 prevents the production of IL1, TNF-alpha and prostaglandins in response to activation of the cells by bacterial endotoxins or IFN-gamma. |
Recombinant Human IL4 |
Z100549 |
ABM |
1.0 mg |
EUR 3450 |
Description: IL4 is produced mainly by a sub-population of activated T helper cells which also secrete IL5 and IL6. The biological activities of IL4 are mediated by a specific receptor, the extracellular domain of which is related to the receptors for EPO, IL6, and the beta chain of the IL-2 receptor. IL4 participates in several B-cell activation processes as well as of other cell types. A co-stimulator of DNA-synthesis, IL4 induces the expression of class II MHC molecules on resting B-cells, enhances both secretion and cell surface expression of IgE and IgG1, and also regulates the expression of the low affinity Fc receptor for IgE on both lymphocytes and monocytes. Pre-treatment of macrophages with IL4 prevents the production of IL1, TNF-alpha and prostaglandins in response to activation of the cells by bacterial endotoxins or IFN-gamma. |
Recombinant Human IL6 |
Z100555 |
ABM |
20 µg |
EUR 235 |
Description: IL6 is a pleiotropic cytokine that participates in a wide variety of biological functions such as acute phase response, inflammation, hematopoiesis, bone metabolism and cancer. While produced mainly by stimulated monocytes, fibroblasts and endothelial cells, IL6 is also known to be produced by macrophages, T cells, B lymphocytes, granulocytes, smooth muscle cells, eosinophils, chondrocytes, osteoblasts, mast cells, glial cells and keratinocytes, upon stimulation. Unlike murine IL6 which is inactive on human cells, both human and murine IL6 are equally active on murine cells. The IL6 receptor is a strongly glycosylated protein of 80 kDa and a length of 449 amino acids (designated CD126). Recombinant human IL6 is a 21 kDa, non-glycosylated protein that contains two disulfide bridges. |
Recombinant Human IL6 |
Z100557 |
ABM |
100 µg |
EUR 960 |
Description: IL6 is a pleiotropic cytokine that participates in a wide variety of biological functions such as acute phase response, inflammation, hematopoiesis, bone metabolism and cancer. While produced mainly by stimulated monocytes, fibroblasts and endothelial cells, IL6 is also known to be produced by macrophages, T cells, B lymphocytes, granulocytes, smooth muscle cells, eosinophils, chondrocytes, osteoblasts, mast cells, glial cells and keratinocytes, upon stimulation. Unlike murine IL6 which is inactive on human cells, both human and murine IL6 are equally active on murine cells. The IL6 receptor is a strongly glycosylated protein of 80 kDa and a length of 449 amino acids (designated CD126). Recombinant human IL6 is a 21 kDa, non-glycosylated protein that contains two disulfide bridges. |
Recombinant Human IL6 |
Z100559 |
ABM |
10 x 100 µg (Z100557 x 10) |
EUR 4215 |
Description: IL6 is a pleiotropic cytokine that participates in a wide variety of biological functions such as acute phase response, inflammation, hematopoiesis, bone metabolism and cancer. While produced mainly by stimulated monocytes, fibroblasts and endothelial cells, IL6 is also known to be produced by macrophages, T cells, B lymphocytes, granulocytes, smooth muscle cells, eosinophils, chondrocytes, osteoblasts, mast cells, glial cells and keratinocytes, upon stimulation. Unlike murine IL6 which is inactive on human cells, both human and murine IL6 are equally active on murine cells. The IL6 receptor is a strongly glycosylated protein of 80 kDa and a length of 449 amino acids (designated CD126). Recombinant human IL6 is a 21 kDa, non-glycosylated protein that contains two disulfide bridges. |
Recombinant Human LIF |
Z100605 |
ABM |
10 µg |
EUR 85 |
Description: LIF is a multifunctional secreted glycoprotein that exists in both soluble and matrix bound forms. It displays biologic activities ranging from the differentiation of myeloid leukemic cells into macrophage lineage to effects on bone metabolism, inflammation, neural development, embryogenesis, and the maintenance of implantation. It is now clear that LIF is related in both structure and mechanism of action to the interleukin IL-6 family of cytokines, which also includes IL-11, ciliary neurotrophic factor, oncostatin M, and cardiotrophin 1. The actions of these cytokines are mediated through specific cell-surface receptors that consist of a unique chain and the shared signal transducing subunit gp130. |
Recombinant Human LIF |
Z100607 |
ABM |
100 µg |
EUR 360 |
Description: LIF is a multifunctional secreted glycoprotein that exists in both soluble and matrix bound forms. It displays biologic activities ranging from the differentiation of myeloid leukemic cells into macrophage lineage to effects on bone metabolism, inflammation, neural development, embryogenesis, and the maintenance of implantation. It is now clear that LIF is related in both structure and mechanism of action to the interleukin IL-6 family of cytokines, which also includes IL-11, ciliary neurotrophic factor, oncostatin M, and cardiotrophin 1. The actions of these cytokines are mediated through specific cell-surface receptors that consist of a unique chain and the shared signal transducing subunit gp130. |
Recombinant Human LIF |
Z100609 |
ABM |
1.0 mg |
EUR 1500 |
Description: LIF is a multifunctional secreted glycoprotein that exists in both soluble and matrix bound forms. It displays biologic activities ranging from the differentiation of myeloid leukemic cells into macrophage lineage to effects on bone metabolism, inflammation, neural development, embryogenesis, and the maintenance of implantation. It is now clear that LIF is related in both structure and mechanism of action to the interleukin IL-6 family of cytokines, which also includes IL-11, ciliary neurotrophic factor, oncostatin M, and cardiotrophin 1. The actions of these cytokines are mediated through specific cell-surface receptors that consist of a unique chain and the shared signal transducing subunit gp130. |
Recombinant Human OSM |
Z100755 |
ABM |
10 µg |
EUR 85 |
Description: Oncostatin M is produced by monocytes and T cells after cell activation, adherent macrophages, and various T cell lines. Oncostatin M is a member of the IL-6-related cytokine subfamily that includes IL-6, IL-11, LIF, CNTF and CT-1. Oncostatin M mediates its bioactivities through two different heterodimer receptors. They both involve gp130 as a signal transducing moiety, which is found also in receptors for a number of other cytokines. When gp130 dimerizes with LIF receptor beta subunit this generates the high affinity type 1 OSM receptor. When gp130 dimerizes with a protein known as OSM receptor beta this generates the type 2 OSM receptor. Both OSM receptors activate the receptor-associated Janus kinases JAK1, JAK2, and TYK2. Signaling also involves the transcriptional activators STAT3 and STAT5b (see also: STAT proteins) were specifically activated through the gp130-OSM-R-beta type II heterocomplex. The signaling pathway differences observed between the common type I LIF/OSM receptor and the specific type II OSM receptor might explain some of the bioactivities specifically displayed by OSM. Oncostatin M inhibits the growth of several tumor cell lines (A375 melanoma, lung carcinomas). The antiproliferative activity of oncostatin M for some cell lines is synergised by TGF-beta and IFN-gamma. It promotes the growth of human fibroblasts, vascular smooth muscle cells, and some normal cell lines. Oncostatin can inhibit the proliferation of murine M1 myeloid leukemic cells and induces their differentiation into macrophage-like cells, a function shared by LIF, G- CSF, and IL-6. |
Recombinant Human OSM |
Z100757 |
ABM |
200 µg |
EUR 925 |
Description: Oncostatin M is produced by monocytes and T cells after cell activation, adherent macrophages, and various T cell lines. Oncostatin M is a member of the IL-6-related cytokine subfamily that includes IL-6, IL-11, LIF, CNTF and CT-1. Oncostatin M mediates its bioactivities through two different heterodimer receptors. They both involve gp130 as a signal transducing moiety, which is found also in receptors for a number of other cytokines. When gp130 dimerizes with LIF receptor beta subunit this generates the high affinity type 1 OSM receptor. When gp130 dimerizes with a protein known as OSM receptor beta this generates the type 2 OSM receptor. Both OSM receptors activate the receptor-associated Janus kinases JAK1, JAK2, and TYK2. Signaling also involves the transcriptional activators STAT3 and STAT5b (see also: STAT proteins) were specifically activated through the gp130-OSM-R-beta type II heterocomplex. The signaling pathway differences observed between the common type I LIF/OSM receptor and the specific type II OSM receptor might explain some of the bioactivities specifically displayed by OSM. Oncostatin M inhibits the growth of several tumor cell lines (A375 melanoma, lung carcinomas). The antiproliferative activity of oncostatin M for some cell lines is synergised by TGF-beta and IFN-gamma. It promotes the growth of human fibroblasts, vascular smooth muscle cells, and some normal cell lines. Oncostatin can inhibit the proliferation of murine M1 myeloid leukemic cells and induces their differentiation into macrophage-like cells, a function shared by LIF, G- CSF, and IL-6. |
Recombinant Human OSM |
Z100759 |
ABM |
1.0 mg |
EUR 2015 |
Description: Oncostatin M is produced by monocytes and T cells after cell activation, adherent macrophages, and various T cell lines. Oncostatin M is a member of the IL-6-related cytokine subfamily that includes IL-6, IL-11, LIF, CNTF and CT-1. Oncostatin M mediates its bioactivities through two different heterodimer receptors. They both involve gp130 as a signal transducing moiety, which is found also in receptors for a number of other cytokines. When gp130 dimerizes with LIF receptor beta subunit this generates the high affinity type 1 OSM receptor. When gp130 dimerizes with a protein known as OSM receptor beta this generates the type 2 OSM receptor. Both OSM receptors activate the receptor-associated Janus kinases JAK1, JAK2, and TYK2. Signaling also involves the transcriptional activators STAT3 and STAT5b (see also: STAT proteins) were specifically activated through the gp130-OSM-R-beta type II heterocomplex. The signaling pathway differences observed between the common type I LIF/OSM receptor and the specific type II OSM receptor might explain some of the bioactivities specifically displayed by OSM. Oncostatin M inhibits the growth of several tumor cell lines (A375 melanoma, lung carcinomas). The antiproliferative activity of oncostatin M for some cell lines is synergised by TGF-beta and IFN-gamma. It promotes the growth of human fibroblasts, vascular smooth muscle cells, and some normal cell lines. Oncostatin can inhibit the proliferation of murine M1 myeloid leukemic cells and induces their differentiation into macrophage-like cells, a function shared by LIF, G- CSF, and IL-6. |
Recombinant Human PTH |
Z100775 |
ABM |
100 µg |
EUR 85 |
Description: Parathyroid hormone is a circulating hormone that acts as the central regulator of calcium metabolism by directly targeting bone, kidney, and intestine. The classical concept of PTH action is that it regulates serum calcium levels by stimulating bone resorption. However, intermittent administration of PTH selectively stimulates bone formation. It is now known that PTH binds to its receptor PTH1R, and activates the G protein alpha subunits. Besides PKA and PKC activation, PTH also regulates MAPKs including p42/p44 ERKs, p38, and c-Jun N-terminal kinase subtypes. |
Recombinant Human PTH |
Z100777 |
ABM |
1.0 mg |
EUR 705 |
Description: Parathyroid hormone is a circulating hormone that acts as the central regulator of calcium metabolism by directly targeting bone, kidney, and intestine. The classical concept of PTH action is that it regulates serum calcium levels by stimulating bone resorption. However, intermittent administration of PTH selectively stimulates bone formation. It is now known that PTH binds to its receptor PTH1R, and activates the G protein alpha subunits. Besides PKA and PKC activation, PTH also regulates MAPKs including p42/p44 ERKs, p38, and c-Jun N-terminal kinase subtypes. |
Recombinant Human PTH |
Z100779 |
ABM |
2.0 mg |
EUR 1140 |
Description: Parathyroid hormone is a circulating hormone that acts as the central regulator of calcium metabolism by directly targeting bone, kidney, and intestine. The classical concept of PTH action is that it regulates serum calcium levels by stimulating bone resorption. However, intermittent administration of PTH selectively stimulates bone formation. It is now known that PTH binds to its receptor PTH1R, and activates the G protein alpha subunits. Besides PKA and PKC activation, PTH also regulates MAPKs including p42/p44 ERKs, p38, and c-Jun N-terminal kinase subtypes. |
Recombinant Human SCF |
Z100815 |
ABM |
10 µg |
EUR 115 |
Description: SCF is a stromal cell-derived cytokine synthesized by fibroblasts and other cell types. SCF promotes proliferation and early differentiation of cells at the level of multipotent stem cells. It has been suggested that SCF is essential for optimal production of various hematopoietic lineages, mainly because of its ability to prevent apoptosis when co-stimulated with other cytokines. The receptor for SCF, designated SCFR (CD117) is the oncogene designated as KIT. The biological activities of SCF are considerably synergised by colony stimulating factors; GM-CSF and G-CSF, and by IL7, EPO and some other growth and differentiation factors. In combination with IL7, SCF stimulates the proliferation of pre-B cells. SCF is also a potent chemoattractant for cells expressing the kit receptor. Recombinant Human SCF is a monomeric protein that contains intra-chain disulfide bonds. |
Recombinant Human SCF |
Z100817 |
ABM |
100 µg |
EUR 480 |
Description: SCF is a stromal cell-derived cytokine synthesized by fibroblasts and other cell types. SCF promotes proliferation and early differentiation of cells at the level of multipotent stem cells. It has been suggested that SCF is essential for optimal production of various hematopoietic lineages, mainly because of its ability to prevent apoptosis when co-stimulated with other cytokines. The receptor for SCF, designated SCFR (CD117) is the oncogene designated as KIT. The biological activities of SCF are considerably synergised by colony stimulating factors; GM-CSF and G-CSF, and by IL7, EPO and some other growth and differentiation factors. In combination with IL7, SCF stimulates the proliferation of pre-B cells. SCF is also a potent chemoattractant for cells expressing the kit receptor. Recombinant Human SCF is a monomeric protein that contains intra-chain disulfide bonds. |
Recombinant Human SCF |
Z100819 |
ABM |
10 x 100 µg (Z100817 x 10) |
EUR 2350 |
Description: SCF is a stromal cell-derived cytokine synthesized by fibroblasts and other cell types. SCF promotes proliferation and early differentiation of cells at the level of multipotential stem cells. It has been suggested that SCF is essential for optimal production of various hematopoietic lineages, mainly because of its ability to prevent apoptosis when it co-stimulates with other cytokines. The receptor for SCF, designated SCFR(CD117), is the oncogene designated as KIT. The biological activities of SCF are synergised considerably by colony stimulating factors GM-CSF and G-CSF, and also by IL-7, Epo and some other growth and differentiation factors. In combination with IL-7, SCF stimulates the proliferation of pre-B cells. SCF is also a potent chemoattractant for cells (see also: Chemotaxis), for example, mast cells expressing the kit receptor. One response to SCF in these cells is a characteristic rearrangement of the actin filaments of the cytoskeleton. |
Recombinant Human TNF |
Z100855 |
ABM |
50 µg |
EUR 85 |
Description: Tumor Necrosis Factor is secreted by macrophages, monocytes, neutrophils, T cells, natural killer cells following their stimulation by bacterial lipopolysaccharides although cells expressing CD8(+) secrete little or no TNF-alpha. In addition, TNF is secreted by peripheral neutrophilic granulocytes and by a number of transformed cell lines that include those of astrocytes, microglial cells, smooth muscle cells and fibroblasts. Human milk also contains this factor. The synthesis of TNF-alpha is induced by many different stimuli including interferons, IL2, GM-CSF, SP, Bradykinin, Immune complexes, inhibitors of cyclooxygenase and platelet activating factor. TNF-alpha shares approximately 30% homology with TNF-beta. Human TNF-alpha is a non-glycosylated protein of 17.6 kDa. |
Recombinant Human TNF |
Z100857 |
ABM |
100 µg |
EUR 135 |
Description: Tumor Necrosis Factor is secreted by macrophages, monocytes, neutrophils, T cells, natural killer cells following their stimulation by bacterial lipopolysaccharides although cells expressing CD8(+) secrete little or no TNF-alpha. In addition, TNF is secreted by peripheral neutrophilic granulocytes and by a number of transformed cell lines that include those of astrocytes, microglial cells, smooth muscle cells and fibroblasts. Human milk also contains this factor. The synthesis of TNF-alpha is induced by many different stimuli including interferons, IL2, GM-CSF, SP, Bradykinin, Immune complexes, inhibitors of cyclooxygenase and platelet activating factor. TNF-alpha shares approximately 30% homology with TNF-beta. Human TNF-alpha is a non-glycosylated protein of 17.6 kDa. |
Recombinant Human TNF |
Z100859 |
ABM |
1.0 mg |
EUR 630 |
Description: Tumor Necrosis Factor is secreted by macrophages, monocytes, neutrophils, T cells, natural killer cells following their stimulation by bacterial lipopolysaccharides. Cells expressing CD4 secrete TNF-alpha while CD8(+) cells secrete little or no TNF-alpha. Stimulated peripheral neutrophilic granulocytes but also unstimulated cells and also a number of transformed cell lines, astrocytes, microglial cells, smooth muscle cells, and fibroblasts also secrete TNF. Human milk also contains this factor. The synthesis of TNF-alpha is induced by many different stimuli including interferons, IL-2, GM-CSF, SP, Bradykinin, Immune complexes, inhibitors of cyclooxygenase and PAF (platelet activating factor). Human TNF-alpha is a non-glycosylated protein of 17 kDa and a length of 157 amino acids. Murine TNF-alpha is N-glycosylated. Homology with TNF-beta is approximately 30%. TNF-alpha forms dimers and trimers. |
Recombinant Human LTA |
Z100865 |
ABM |
20 µg |
EUR 85 |
Description: TNF-beta is a potent mediator of inflammatory and immune responses. It belongs to the TNF family of ligands and signals through TNFR1 and TNFR2. TNF-beta is produced by activated T and B lymphocytes, and has similar activities to TNF-alpha. Like TNF-alpha, TNF-beta is involved in the regulation of various biological processes including cell proliferation, differentiation, apoptosis, lipid metabolism, coagulation, and neurotransmission. TNF-beta is secreted as a soluble polypeptide, but can form heterotrimers with lymphotoxin-beta, which effectively anchors the TNF-beta to the cell surface. TNF-beta is cytotoxic to a wide range of tumor cells. |
Recombinant Human LTA |
Z100867 |
ABM |
100 µg |
EUR 345 |
Description: TNF-beta is a potent mediator of inflammatory and immune responses. It belongs to the TNF family of ligands and signals through TNFR1 and TNFR2. TNF-beta is produced by activated T and B lymphocytes, and has similar activities to TNF-alpha. Like TNF-alpha, TNF-beta is involved in the regulation of various biological processes including cell proliferation, differentiation, apoptosis, lipid metabolism, coagulation, and neurotransmission. TNF-beta is secreted as a soluble polypeptide, but can form heterotrimers with lymphotoxin-beta, which effectively anchors the TNF-beta to the cell surface. TNF-beta is cytotoxic to a wide range of tumor cells. |
Recombinant Human LTA |
Z100869 |
ABM |
1.0 mg |
EUR 1500 |
Description: TNF-beta is a potent mediator of inflammatory and immune responses. It belongs to the TNF family of ligands and signals through TNFR1 and TNFR2. TNF-beta is produced by activated T and B lymphocytes, and has similar activities to TNF-alpha. Like TNF-alpha, TNF-beta is involved in the regulation of various biological processes including cell proliferation, differentiation, apoptosis, lipid metabolism, coagulation, and neurotransmission. TNF-beta is secreted as a soluble polypeptide, but can form heterotrimers with lymphotoxin-beta, which effectively anchors the TNF-beta to the cell surface. TNF-beta is cytotoxic to a wide range of tumor cells. |
Recombinant Human MIF |
Z100915 |
ABM |
25 µg |
EUR 75 |
Description: Macrophage Migration Inhibitory Factor (MIF) is a proinflammatory cytokine. MIF is involved in the innate immune response to bacterial pathogens. The expression of MIF at sites of inflammation suggests a role as mediator in regulating the function of macrophages in host defense. Counteracts the anti-inflammatory activity of glucocorticoids. Has phenylpyruvate tautomerase and dopachrome tautomerase activity (in vitro), but the physiological substrate is not known. It is not clear whether the tautomerase activity has any physiological relevance, and whether it is important for cytokine activity. |
Recombinant Human MIF |
Z100917 |
ABM |
100 µg |
EUR 255 |
Description: Macrophage Migration Inhibitory Factor (MIF) is a proinflammatory cytokine. MIF is involved in the innate immune response to bacterial pathogens. The expression of MIF at sites of inflammation suggests a role as mediator in regulating the function of macrophages in host defense. Counteracts the anti-inflammatory activity of glucocorticoids. Has phenylpyruvate tautomerase and dopachrome tautomerase activity (in vitro), but the physiological substrate is not known. It is not clear whether the tautomerase activity has any physiological relevance, and whether it is important for cytokine activity. |
Recombinant Human MIF |
Z100919 |
ABM |
1.0 mg |
EUR 1150 |
Description: Macrophage Migration Inhibitory Factor (MIF) is a proinflammatory cytokine. MIF is involved in the innate immune response to bacterial pathogens. The expression of MIF at sites of inflammation suggests a role as mediator in regulating the function of macrophages in host defense. Counteracts the anti-inflammatory activity of glucocorticoids. Has phenylpyruvate tautomerase and dopachrome tautomerase activity (in vitro), but the physiological substrate is not known. It is not clear whether the tautomerase activity has any physiological relevance, and whether it is important for cytokine activity. |
Recombinant Human IL7 |
Z100975 |
ABM |
10 µg |
EUR 85 |
Description: IL7 is a secreted cytokine of the hemopoietin family that primarily affects early B and T cells and plays an important role in stimulating the proliferation of lymphoid progenitors. IL7 is produced by stromal epithelial cells of the thymus, bone marrow, and intestines. Human and murine IL7 share 60% sequence homology at the primary level and known to exhibit cross species activity. Designated CD127, the human IL7 receptor is a strongly glycosylated membrane protein of 76 kDa. Recombinant Human IL7 is a 17.7 kDa, non-glycosylated protein. |
Recombinant Human IL7 |
Z100977 |
ABM |
100 µg |
EUR 470 |
Description: IL7 is a secreted cytokine of the hemopoietin family that primarily affects early B and T cells and plays an important role in stimulating the proliferation of lymphoid progenitors. IL7 is produced by stromal epithelial cells of the thymus, bone marrow, and intestines. Human and murine IL7 share 60% sequence homology at the primary level and known to exhibit cross species activity. Designated CD127, the human IL7 receptor is a strongly glycosylated membrane protein of 76 kDa. Recombinant Human IL7 is a 17.7 kDa, non-glycosylated protein. |
Recombinant Human IL7 |
Z100979 |
ABM |
1.0 mg |
EUR 6900 |
Description: IL7 is secreted constitutively into the conditioned medium of adherent bone marrow stromal cells and thymic cells. Mouse and human keratinocytes have been shown also to express and secrete IL7.Human (152 amino acids; 17.4 kDa) and murine IL7 (129 amino acids) show 60 % sequence homology at the protein level. The human IL7 receptor is an integral strongly glycosylated membrane proteins of 76 kDa expressed on activated T-cells. This receptor has been designated as CD127. IL7 receptors are expressed on pre-B-cells and their progenitors. They are not expressed on mature B-cells. IL7 receptors are expressed also on bone marrow macrophages. Functional IL7 receptors are found on the cell surface of multiphenotypic, biphenotypic, and immature lymphoid progenitors of B- cells with the gene arrangement of the heavy immunoglobulin chain such as those observed in the germ line |
Recombinant Human IL2 |
Z101235 |
ABM |
50 µg |
EUR 235 |
Description: IL-2 is produced mainly by T cells expressing the surface antigen CD4 following cell activation by mitogens or allogen. Interleukin-2 (IL-2) has multiple, sometimes opposing, functions during an inflammatory response. It is a potent inducer of T cell proliferation. Th1 and Th2 effector T cell differentiation and provides T cells with a long-lasting competitive advantage resulting in the optimal survival and function of memory cells. In a regulatory role, IL-2 is important for the development, survival, and function of regulatory T cells, it enhances Fas- mediated activation-induced cell death, and it inhibits the development of inflammatory Th17 cells. Thus, in its dual and contrasting functions, IL-2 contributes to both the induction and the termination of inflammatory immune responses. |
Recombinant Human TNF |
Z101385 |
ABM |
50 µg |
EUR 510 |
Description: Tumor Necrosis Factor is secreted by macrophages, monocytes, neutrophils, T cells, natural killer cells following their stimulation by bacterial lipopolysaccharides. Cells expressing CD4 secrete TNF-alpha while CD8(+) cells secrete little or no TNF-alpha. Stimulated peripheral neutrophilic granulocytes but also unstimulated cells and also a number of transformed cell lines, astrocytes, microglial cells, smooth muscle cells, and fibroblasts also secrete TNF. Human milk also contains this factor. The synthesis of TNF-alpha is induced by many different stimuli including interferons, IL-2, GM-CSF, SP, Bradykinin, immune complexes, inhibitors of cyclooxygenase, and PAF (platelet activating factor). Human TNF-alpha is a non-glycosylated protein of 17 kDa and a length of 157 amino acids. Murine TNF-alpha is N-glycosylated. Homology with TNF-beta is approximately 30%. TNF-alpha forms dimers and trimers. |
Recombinant Human EPO |
Z101435 |
ABM |
50 µg |
EUR 75 |
Description: EPO is predominantly synthesized and secreted by tubular and juxtatubular capillary, endothelial, and interstitial cells of the kidney. Approximately 10-15% of the total amount of EPO comes from extrarenal sources and is predominantly produced by hepatocytes and Kupffer cells of the liver. Approximately 40% of the molecular mass of EPO is due to its glycosylation. Glycosylation is an important factor determining the pharmacokinetic behaviour of EPO in vivo. Non-glycosylated Epo has an extremely short biological half life. Recombinant Human EPO is a glycosylated protein that runs at approximately 35 kDa owing to its glycosylation. |
Recombinant Human EPO |
Z101437 |
ABM |
500 µg |
EUR 360 |
Description: EPO is predominantly synthesized and secreted by tubular and juxtatubular capillary, endothelial, and interstitial cells of the kidney. Approximately 10-15% of the total amount of Epo comes from extrarenal sources and is predominantly produced by hepatocytes and Kupffer cells of the liver. Approximately 40% of the molecular mass of Epo is due to its glycosylation. Glycosylation is an important factor determining the pharmacokinetic behavior of Epo in vivo. Non-glycosylated Epo has an extremely short biological half life. It still binds to its receptor and may even have a higher specific activity in vitro. |
Recombinant Human EPO |
Z101439 |
ABM |
1.0 mg |
EUR 660 |
Description: EPO is predominantly synthesized and secreted by tubular and juxtatubular capillary, endothelial, and interstitial cells of the kidney. Approximately 10-15% of the total amount of Epo comes from extrarenal sources and is predominantly produced by hepatocytes and Kupffer cells of the liver. Approximately 40% of the molecular mass of Epo is due to its glycosylation. Glycosylation is an important factor determining the pharmacokinetic behavior of Epo in vivo. Non-glycosylated Epo has an extremely short biological half life. It still binds to its receptor and may even have a higher specific activity in vitro. |
Recombinant Human SHH |
Z101675 |
ABM |
30 µg |
EUR 105 |
Description: Highly conserved proteins, members of the Hedgehog family are widely represented throughout the animal kingdom. The three known mammalian Hedgehog proteins; Sonic (SHH), Desert (DHH) and Indian (IHH) hedgehog share a high degree of sequence and structural identity. SHH is specifically known to be expressed in fetal intestine, liver, lung and kidney. Recombinant Human SHH represents the N-product (N-terminal domain with Cys24 substituted by an Ile-Val-Ile sequence) which retains all the known signalling capabilities. |
Recombinant Human SHH |
Z101677 |
ABM |
100 µg |
EUR 215 |
Description: Highly conserved proteins, members of the Hedgehog family are widely represented throughout the animal kingdom. The three known mammalian Hedgehog proteins; Sonic (SHH), Desert (DHH) and Indian (IHH) hedgehog share a high degree of sequence and structural identity. SHH is specifically known to be expressed in fetal intestine, liver, lung and kidney. Recombinant Human SHH represents the N-product (N-terminal domain with Cys24 substituted by an Ile-Val-Ile sequence) which retains all the known signalling capabilities. |
Recombinant Human SHH |
Z101679 |
ABM |
1.0 mg |
EUR 1150 |
Description: Highly conserved proteins, members of the Hedgehog family are widely represented throughout the animal kingdom. The three known mammalian Hedgehog proteins; Sonic (SHH), Desert (DHH) and Indian (IHH) hedgehog share a high degree of sequence and structural identity. SHH is specifically known to be expressed in fetal intestine, liver, lung and kidney. Recombinant Human SHH represents the N-product (N-terminal domain with Cys24 substituted by an Ile-Val-Ile sequence) which retains all the known signalling capabilities. |
Recombinant Human DHH |
Z101695 |
ABM |
50 µg |
EUR 85 |
Description: The Desert Hedgehog protein is one of the three Hedgehog family proteins that is highly conserved and plays a role in many developmental processes in animals. DHH become biologically active following its autocatalytic cleavage. There is a high degree of residue homology between Sonic Hedgehog (SHH), Indian Hedgehog (IHH), and DHH. Despite their individual levels of expression and unique biological roles, the Hedgehog family members all use the same signalling pathway, and therefore, may be used interchangeably for some experimental purposes. |
Recombinant Human DHH |
Z101697 |
ABM |
250 µg |
EUR 375 |
Description: The Desert Hedgehog protein is one of the three Hedgehog family proteins that is highly conserved and plays a role in many developmental processes in animals. DHH become biologically active following its autocatalytic cleavage. There is a high degree of residue homology between Sonic Hedgehog (SHH), Indian Hedgehog (IHH), and DHH. Despite their individual levels of expression and unique biological roles, the Hedgehog family members all use the same signalling pathway, and therefore, may be used interchangeably for some experimental purposes. |
Recombinant Human DHH |
Z101699 |
ABM |
1.0 mg |
EUR 1320 |
Description: The Desert Hedgehog protein is one of the three Hedgehog family proteins that is highly conserved and plays a role in many developmental processes in animals. DHH become biologically active following its autocatalytic cleavage. There is a high degree of residue homology between Sonic Hedgehog (SHH), Indian Hedgehog (IHH), and DHH. Despite their individual levels of expression and unique biological roles, the Hedgehog family members all use the same signalling pathway, and therefore, may be used interchangeably for some experimental purposes. |
Recombinant Human MIA |
Z102045 |
ABM |
20 µg |
EUR 85 |
Description: MIA is a secreted, regulatory protein produced mainly by chondrocytes and malignant melanoma cells. This protein induces the metastasis of cancer cells by indirectly causing the detachment of melanoma cells from the surrounding extracellular matrix. MIA levels are now measured and used as a diagnostic tool for melanoma metastasis and rheumatoid arthritis. |
Recombinant Human MIA |
Z102049 |
ABM |
1.0 mg |
EUR 3195 |
Description: MIA is a secreted, regulatory protein produced mainly by chondrocytes and malignant melanoma cells. This protein induces the metastasis of cancer cells by indirectly causing the detachment of melanoma cells from the surrounding extracellular matrix. MIA levels are now measured and used as a diagnostic tool for melanoma metastasis and rheumatoid arthritis. |
Recombinant Human IL9 |
Z102475 |
ABM |
10 µg |
EUR 195 |
Description: Interleukin 9 (IL9) is an immunoregulatory cytokine belonging to the IL-7/IL-9 cytokine family. Commonly produced by TH17 cells, IL9 acts as a hematopoietic cell regulator by preventing apoptosis and stimulates cell proliferation of T lymphocytes, erythroid cells, and mast cells. It binds to the IL9 receptor (IL9R) to activate different signal transducer and activator (STAT) proteins. It also supports IL2 and IL4 independent growth of helper T-cells and affects TH17 and Tregs through STAT3 and STAT5 signalling activation. Furthermore, IL9 has been found to be a candidate gene for asthma as its presence determines the pathogenesis of bronchial hyper-responsiveness. Although human and mouse IL9 share a 56% amino acid identity, human IL9 is not active on mouse cells and can be found to inhibit melanoma growth in mice. |
Recombinant Human IL9 |
Z102479 |
ABM |
1.0 mg |
EUR 6900 |
Description: Interleukin 9 (IL9) is an immunoregulatory cytokine belonging to the IL-7/IL-9 cytokine family. Commonly produced by TH17 cells, IL9 acts as a hematopoietic cell regulator by preventing apoptosis and stimulates cell proliferation of T lymphocytes, erythroid cells, and mast cells. It binds to the IL9 receptor (IL9R) to activate different signal transducer and activator (STAT) proteins. It also supports IL2 and IL4 independent growth of helper T-cells and affects TH17 and Tregs through STAT3 and STAT5 signalling activation. Furthermore, IL9 has been found to be a candidate gene for asthma as its presence determines the pathogenesis of bronchial hyper-responsiveness. Although human and mouse IL9 share a 56% amino acid identity, human IL9 is not active on mouse cells and can be found to inhibit melanoma growth in mice. |
Recombinant Human IL5 |
Z102625 |
ABM |
10 µg |
EUR 85 |
Description: Interleukin 5 (IL5) is a specific hematopoietic growth factor that is responsible for the growth and differentiation of eosinophils. IL5 promotes the growth of immature hematopoietic progenitor cells BFU-E while it causes differentiation of CFU-E the proliferation of which is inhibited by IL5. B cells can be made responsive to IL5 by treatment with suboptimal doses of IL1. Interleukin 5 also promotes the generation of cytotoxic T cells from thymocytes. In thymocytes IL5 induces the expression of high affinity IL2 receptors. Human and mouse IL5 is cross-species reactive. Recombinant Human IL5 is a 26.5 kDa disulfide-linked homodimerized protein. |
Recombinant Human HGF |
Z102775 |
ABM |
10 µg |
EUR 195 |
Description: Hepatocyte growth factor (HGF) is a multifunctional cytokine that was originally described as a mesenchymal-derived factor that regulates cell growth, cell motility, morphogenesis and angiogenesis through activation of its receptor, the transmembrane tyrosine kinase encoded by the c-Met proto-oncogene. HGF and c-Met are often co-expressed or over-expressed in a variety of human malignancies including glioblastoma and medullablastoma. The multifunctional effects of HGF: c-Met signaling in tumor cells are mediated by a network of signal transduction pathways including mitogen-activated protein kinase (MAPK) and phosphoinositide 3-kinase (PI3K). HGF consists of two subunits held by a disulfide bond. The alpha subunit (69 kDa) has a length of 440 amino acids and the beta subunit (34 kDa) has a length of 234 amino acids. The beta chain of the factor shows approximately 38% homology at the protein level to the serine protease domain of plasminogen. Recombinant HGF expressed in human 293 cells and has a molecular mass of 70 kDa, lower compared to the Molecular mass for this cytokine expressed in CHO cells which emphasizes the difference in post translational modifications. |
Recombinant Human HGF |
Z102777 |
ABM |
1.0 mg |
EUR 6300 |
Description: Hepatocyte growth factor (HGF) is a multifunctional cytokine that was originally described as a mesenchymal-derived factor that regulates cell growth, cell motility, morphogenesis and angiogenesis through activation of its receptor, the transmembrane tyrosine kinase encoded by the c-Met proto-oncogene. HGF and c-Met are often co-expressed or over-expressed in a variety of human malignancies including glioblastoma and medullablastoma. The multifunctional effects of HGF: c-Met signaling in tumor cells are mediated by a network of signal transduction pathways including mitogen-activated protein kinase (MAPK) and phosphoinositide 3-kinase (PI3K). HGF consists of two subunits held by a disulfide bond. The alpha subunit (69 kDa) has a length of 440 amino acids and the beta subunit (34 kDa) has a length of 234 amino acids. The beta chain of the factor shows approximately 38% homology at the protein level to the serine protease domain of plasminogen. Recombinant HGF expressed in human 293 cells and has a molecular mass of 70 kDa, lower compared to the Molecular mass for this cytokine expressed in CHO cells which emphasizes the difference in post translational modifications. |
Recombinant Human NSE |
HEENP-1402 |
Cyagen |
5ug |
Ask for price |
Recombinant Human PDI |
HEENP-1601 |
Cyagen |
100ug |
Ask for price |
Recombinant Human EGF |
HEGFP-0501 |
Cyagen |
100ug |
Ask for price |
Recombinant Human BNP |
HEOPP-0211 |
Cyagen |
100ug |
Ask for price |
Recombinant Human C5a |
HEOPP-0306 |
Cyagen |
5ug |
Ask for price |
Recombinant Human EPG |
HEOPP-0503 |
Cyagen |
5ug |
Ask for price |
Recombinant Human LIF |
HEOPP-1202 |
Cyagen |
5ug |
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Recombinant Human MIA |
HEOPP-1301 |
Cyagen |
5ug |
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Recombinant Human MIF |
HEOPP-1308 |
Cyagen |
10ug |
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Recombinant Human NOV |
HEOPP-1407 |
Cyagen |
5ug |
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Recombinant Human OSM |
HEOPP-1503 |
Cyagen |
10ug |
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Recombinant Human OPG |
HEOPP-1506 |
Cyagen |
10ug |
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Recombinant Human PTN |
HEOPP-1607 |
Cyagen |
5ug |
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Recombinant Human SCF |
HEOPP-1902 |
Cyagen |
10ug |
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Recombinant Human SHH |
HEOPP-1907 |
Cyagen |
5ug |
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Recombinant Human EGF |
EPT004 |
ELK Biotech |
10ug |
EUR 23.4 |
|
Description: Recombinant Human Epidermal Growth Factor is produced by our E.coli expression system and the target gene encoding Asn971-Arg1023 is expressed. |
Recombinant Human PTH |
EPT146 |
ELK Biotech |
50ug |
EUR 353.4 |
|
Description: Recombinant Human Parathyroid Hormone is produced by our E.coli expression system and the target gene encoding Ser32-Gln115 is expressed. |
Recombinant Human LIF |
EPT153 |
ELK Biotech |
10ug |
EUR 119.4 |
|
Description: Recombinant Human Leukemia Inhibitory Factor is produced by our E.coli expression system and the target gene encoding Ser23-Phe202 is expressed. |
Recombinant Human C3a |
EPT178 |
ELK Biotech |
50ug |
EUR 353.4 |
|
Description: Recombinant Human Complement Component C3a is produced by our E.coli expression system and the target gene encoding Ser672-Arg748 is expressed. |
Recombinant Human SCF |
EPT201 |
ELK Biotech |
50ug |
EUR 209.4 |
|
Description: Recombinant Human Stem Cell Factor is produced by our E.coli expression system and the target gene encoding Glu26-Ala189 is expressed. |
Recombinant Human PCT |
P0010 |
FN Test |
100ug |
EUR 626.83 |
|
Description: Recombinant Human protein for PCT |
Recombinant Human CKB |
P0020-B |
FN Test |
100ug |
EUR 626.83 |
|
Description: Recombinant Human protein for CKB |
Recombinant Human CKM |
P0020-M |
FN Test |
100ug |
EUR 626.83 |
|
Description: Recombinant Human protein for CKM |
Recombinant Human HE4 |
P0034 |
FN Test |
100ug |
EUR 626.83 |
|
Description: Recombinant Human protein for HE4 |
Recombinant Human NNE |
P0040 |
FN Test |
100ug |
EUR 626.83 |
|
Description: Recombinant Human protein for NNE |
Recombinant Human GLA |
P0494 |
FN Test |
100ug |
EUR 626.83 |
|
Description: Recombinant Human protein for GLA |
Recombinant human EDA |
P1422 |
FN Test |
100ug |
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|
Description: Recombinant protein for human EDA |
Recombinant human ENG |
P1433 |
FN Test |
100ug |
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|
Description: Recombinant protein for human ENG |
Recombinant human PXN |
P1439 |
FN Test |
100ug |
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|
Description: Recombinant protein for human PXN |
Recombinant human FAS |
P1464 |
FN Test |
100ug |
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|
Description: Recombinant protein for human FAS |
Recombinant human REL |
P1479 |
FN Test |
100ug |
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|
Description: Recombinant protein for human REL |
Recombinant human MET |
P1995 |
FN Test |
100ug |
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|
Description: Recombinant protein for human MET |
Recombinant human KIT |
P1996 |
FN Test |
100ug |
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|
Description: Recombinant protein for human KIT |
Recombinant human TEC |
P1997 |
FN Test |
100ug |
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|
Description: Recombinant protein for human TEC |
Recombinant human FRY |
P2014 |
FN Test |
100ug |
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|
Description: Recombinant protein for human FRY |
Recombinant human VHL |
P2120 |
FN Test |
100ug |
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|
Description: Recombinant protein for human VHL |
Recombinant human FEV |
P2435 |
FN Test |
100ug |
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|
Description: Recombinant protein for human FEV |
Recombinant human GGN |
P2440 |
FN Test |
100ug |
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|
Description: Recombinant protein for human GGN |
Recombinant human KLB |
P2441 |
FN Test |
100ug |
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|
Description: Recombinant protein for human KLB |
Recombinant human DBT |
P2445 |
FN Test |
100ug |
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|
Description: Recombinant protein for human DBT |
Recombinant human MT4 |
P2447 |
FN Test |
100ug |
Ask for price |
|
Description: Recombinant protein for human MT4 |
In short, these findings indicate that leptin may be the main molecule that mediates the effects of adipocytes in inflammatory cells such as basophiles by binding LEPR and activating cellular functions, which may worsen allergic inflammation.