Description: Mouse polyclonal to TMPRSS2

Description: Human transmembrane serine protease 2 (TMPRSS2) is an enzyme primarily expressed by endothelial cells across the respiratory and digestive tracts. It is involved in viral entry and spread of coronaviruses including SARS-CoV-2, the virus that causes COVID19. TMPRSS2 primes the spike protein by cleaving at the S1/S2 site, leading to the virus fusing to the respiratory epithelia on the cell surface through binding to ACE2. Blocking TMPRSS2 activity could potentially be an effective clinical therapy for COVID-19._x000D_
The TMPRSS2 Lentivirus are replication incompetent, HIV-based, VSV-G pseudotyped lentiviral particles that are ready to be transduced into almost all types of mammalian cells, including primary and non-dividing cells. The particles contain an TMPRSS2 gene (NM_005656.4) driven by an EF1a promoter._x000D_

Description: Human transmembrane serine protease 2 (TMPRSS2) is an enzyme primarily expressed by endothelial cells across the respiratory and digestive tracts. It is involved in viral entry and spread of coronaviruses including SARS-CoV-2, the virus that causes COVID19. TMPRSS2 primes the spike protein by cleaving at the S1/S2 site, leading to the virus fusing to the respiratory epithelia on the cell surface through binding to ACE2. Blocking TMPRSS2 activity could potentially be an effective clinical therapy for COVID-19._x000D_
The TMPRSS2 Lentivirus are replication incompetent, HIV-based, VSV-G pseudotyped lentiviral particles that are ready to be transduced into almost all types of mammalian cells, including primary and non-dividing cells. The particles contain an TMPRSS2 gene (NM_005656.4) driven by an EF1a promoter._x000D_

Description: Human transmembrane serine protease 2 (TMPRSS2) is an enzyme primarily expressed by endothelial cells across the respiratory and digestive tracts. It is involved in viral entry and spread of coronaviruses including SARS-CoV-2, the virus that causes COVID19. TMPRSS2 primes the spike protein by cleaving at the S1/S2 site, leading to the virus fusing to the respiratory epithelia on the cell surface through binding to ACE2. Blocking TMPRSS2 activity could potentially be an effective clinical therapy for COVID-19._x000D_
The TMPRSS2 Lentivirus are replication incompetent, HIV-based, VSV-G pseudotyped lentiviral particles that are ready to be transduced into almost all types of mammalian cells, including primary and non-dividing cells. The particles contain an TMPRSS2 gene (NM_005656.4) driven by an EF1a promoter._x000D_

Description: Description of target: This gene encodes a protein that belongs to the serine protease family. The encoded protein contains a type II transmembrane domain, a receptor class A domain, a scavenger receptor cysteine-rich domain and a protease domain. Serine proteases are known to be involved in many physiological and pathological processes. This gene was demonstrated to be up-regulated by androgenic hormones in prostate cancer cells and down-regulated in androgen-independent prostate cancer tissue. The protease domain of this protein is thought to be cleaved and secreted into cell media after autocleavage. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.;Species reactivity: Human;Application: ELISA;Assay info: ;Sensitivity: < 0.059ng/mL

Description: Description of target: This gene encodes a protein that belongs to the serine protease family. The encoded protein contains a type II transmembrane domain, a receptor class A domain, a scavenger receptor cysteine-rich domain and a protease domain. Serine proteases are known to be involved in many physiological and pathological processes. This gene was demonstrated to be up-regulated by androgenic hormones in prostate cancer cells and down-regulated in androgen-independent prostate cancer tissue. The protease domain of this protein is thought to be cleaved and secreted into cell media after autocleavage. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.;Species reactivity: Human;Application: ;Assay info: Quantitative Sandwich ELISA;Sensitivity: < 0.056 ng/mL

Description: Description of target: Serine protease that proteolytically cleaves and activates the viral spike glycoproteins which facilitate virus-cell membrane fusions. The spike proteins are synthesized and maintained in precursor intermediate folding states and proteolysis permits the refolding and energy release required to create stable virus-cell linkages and membrane coalescence. Facilitates human SARS coronavirus (SARS-CoV) infection via two independent mechanisms, proteolytic cleavage of ACE2, which might promote viral uptake, and cleavage of coronavirus spike glycoprotein which activates the glycoprotein for cathepsin L-independent host cell entry. Proteolytically cleaves and activates the spike glycoproteins of human coronavirus 229E (HCoV-229E) and human coronavirus EMC (HCoV-EMC) and the fusion glycoproteins F0 of Sendai virus (SeV), human metapneumovirus (HMPV), human parainfluenza 1, 2, 3, 4a and 4b viruses (HPIV). Essential for spread and pathogenesis of influenza A virus (strains H1N1, H3N2 and H7N9) and is involved in proteolytic cleavage and activation of hemagglutinin (HA) protein which is essential for viral infectivity.4 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment iniRef.5"Tmprss2 is essential for influenza H1N1 virus pathogenesis in mice."_x005F_x005F_x000D_Hatesuer B., Bertram S., Mehnert N., Bahgat M.M., Nelson P.S., Poehlman S., Schughart K._x005F_x005F_x000D_PLoS Pathog. 9:E1003774-E1003774(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION.Ref.6"The host protease TMPRSS2 plays a major role for in vivo replication of emerging H7N9 and seasonal influenza viruses."_x005F_x005F_x000D_Sakai K., Ami Y., Tahara M., Kubota T., Anraku M., Abe M., Nakajima N., Sekizuka T., Shirato K., Suzaki Y., Ainai A., Nakatsu Y., Kanou K., Nakamura K., Suzuki T., Komase K., Nobusawa E., Maenaka K. , Kuroda M., Hasegawa H., Kawaoka Y., Tashiro M., Takeda M._x005F_x005F_x000D_J. Virol. 88:5608-5616(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, DISRUPTION PHENOTYPE.Ref.7"TMPRSS2 is a host factor that is essential for pneumotropism and pathogenicity of H7N9 influenza A virus in mice."_x005F_x005F_x000D_Tarnow C., Engels G., Arendt A., Schwalm F., Sediri H., Preuss A., Nelson P.S., Garten W., Klenk H.D., Gabriel G., Boettcher-Friebertshaeuser E._x005F_x005F_x000D_J. Virol. 88:4744-4751(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.Ref.8"TMPRSS2 and ADAM17 cleave ACE2 differentially and only proteolysis by TMPRSS2 augments entry driven by the severe acute respiratory syndrome coronavirus spike protein."_x005F_x005F_x000D_Heurich A., Hofmann-Winkler H., Gierer S., Liepold T., Jahn O., Poehlmann S._x005F_x005F_x000D_J. Virol. 88:1293-1307(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. ;Species reactivity: Mouse;Application: ELISA;Assay info: Assay Methodology: Quantitative Sandwich Immunoassay;Sensitivity: < 0.113 ng/mL

Description: TMPRSS2 Antibody: TMPRSS2 is a plasma membrane-anchored serine protease that participates in proteolytic cascades of relevance for the normal physiologic function of the prostate. Androgen-induced TMPRSS2 activates several substrates that include pro-hepatocyte growth factor/HGF, the protease activated receptor-2/F2RL1 or matriptase/ST14 leading to extracellular matrix disruption and metastasis of prostate cancer cells. It facilitates human coronaviruses SARS-CoV and SARS-CoV-2 infections via two independent mechanisms, proteolytic cleavage of ACE2 receptor which promotes viral uptake, and cleavage of coronavirus spike glycoproteins which activates the glycoprotein for host cell entry. It proteolytically cleaves and activates the spike glycoproteins of human coronavirus 229E (HCoV-229E) and human coronavirus EMC (HCoV-EMC) and the fusion glycoproteins F0 of Sendai virus (SeV), human metapneumovirus (HMPV), human parainfluenza 1, 2, 3, 4a and 4b viruses (HPIV). TMPRSS2 is essential for spread and pathogenesis of influenza A virus (strains H1N1, H3N2 and H7N9), and it is involved in proteolytic cleavage and activation of hemagglutinin (HA) protein which is essential for viral infectivity.

Description: TMPRSS2 Antibody: TMPRSS2 is a plasma membrane-anchored serine protease that participates in proteolytic cascades of relevance for the normal physiologic function of the prostate. Androgen-induced TMPRSS2 activates several substrates that include pro-hepatocyte growth factor/HGF, the protease activated receptor-2/F2RL1 or matriptase/ST14 leading to extracellular matrix disruption and metastasis of prostate cancer cells. It facilitates human coronaviruses SARS-CoV and SARS-CoV-2 infections via two independent mechanisms, proteolytic cleavage of ACE2 receptor which promotes viral uptake, and cleavage of coronavirus spike glycoproteins which activates the glycoprotein for host cell entry. It proteolytically cleaves and activates the spike glycoproteins of human coronavirus 229E (HCoV-229E) and human coronavirus EMC (HCoV-EMC) and the fusion glycoproteins F0 of Sendai virus (SeV), human metapneumovirus (HMPV), human parainfluenza 1, 2, 3, 4a and 4b viruses (HPIV). TMPRSS2 is essential for spread and pathogenesis of influenza A virus (strains H1N1, H3N2 and H7N9), and it is involved in proteolytic cleavage and activation of hemagglutinin (HA) protein which is essential for viral infectivity.

Description: TMPRSS2 (CT)