TMPRSS2 Protein, Human (P.pastoris, His)

TMPRSS2 Protein, a plasma membrane-anchored serine protease, exhibits a distinct role in various physiological and pathological processes. Known for its cleavage activity at arginine residues, TMPRSS2 plays a pivotal role in proteolytic cascades crucial for the normal physiological function of the prostate. In the context of prostate cancer, androgen-induced TMPRSS2 activation leads to the cleavage of substrates like pro-hepatocyte growth factor/HGF, protease-activated receptor-2/F2RL1, and matriptase/ST14, promoting extracellular matrix disruption and metastasis. Additionally, TMPRSS2 contributes to the modulation of pain sensitivity by activating trigeminal neurons, influencing both spontaneous pain and mechanical allodynia. In the realm of microbial infection, TMPRSS2 plays a critical role in facilitating infections by human coronaviruses SARS-CoV and SARS-CoV-2 through two independent mechanisms: the proteolytic cleavage of the ACE2 receptor, promoting viral uptake, and the cleavage of coronavirus spike glycoproteins, activating the glycoprotein for host cell entry. This protease is also essential for the spread and pathogenesis of influenza A virus, participating in the proteolytic cleavage and activation of the hemagglutinin (HA) protein, which is indispensable for viral infectivity. The diverse functions of TMPRSS2 underscore its significance in both normal physiological processes and disease pathogenesis.