Anti-TMPRSS2 antibody

Target data

Plasma membrane-anchored serine protease that cleaves at arginine residues (PubMed : 32703818, PubMed : 35676539, PubMed : 37990007, PubMed : 38964328). Participates in proteolytic cascades of relevance for the normal physiologic function of the prostate (PubMed : 25122198). 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 (PubMed : 15537383, PubMed : 25122198, PubMed : 26018085). In addition, activates trigeminal neurons and contribute to both spontaneous pain and mechanical allodynia (By similarity).. (Microbial infection) 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 (PubMed : 24227843, PubMed : 32142651, PubMed : 32404436, PubMed : 33051876, PubMed : 34159616, PubMed : 35676539, PubMed : 37990007). The cleavage of SARS-COV2 spike glycoprotein occurs between the S2 and S2' site (PubMed : 32703818). Upon SARS-CoV-2 infection, increases syncytia formation by accelerating the fusion process (PubMed : 33051876, PubMed : 34159616, PubMed : 35676539). 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); involved in proteolytic cleavage and activation of hemagglutinin (HA) protein which is essential for viral infectivity.. (Microbial infection) Receptor for human coronavirus HKU1-CoV, acts synergistically with disialoside glycans to facilitate the entry of the virus. After binding to cell-surface disialoside glycans, the viral S protein interacts with the inactive form of TMPRSS2 and inhibits its protease activity.