Ubiquitous endoprotease within constitutive secretory pathways capable of cleavage at the RX(K/R)R consensus motif (PubMed: 11799113, PubMed: 1629222, PubMed: 1713771, PubMed: 2251280, PubMed: 24666235, PubMed: 25974265, PubMed: 7592877, PubMed: 7690548, PubMed: 9130696). Mediates processing of TGFB1, an essential step in TGF-beta-1 activation (PubMed: 7737999). Converts through proteolytic cleavage the non-functional Brain natriuretic factor prohormone into its active hormone BNP(1-32) (PubMed: 20489134, PubMed: 21763278). (Microbial infection) Probably cleaves and activates anthrax and diphtheria toxins. (Microbial infection) Required for H7N1 and H5N1 influenza virus infection probably by cleaving hemagglutinin. (Microbial infection)...
Ubiquitous endoprotease within constitutive secretory pathways capable of cleavage at the RX(K/R)R consensus motif (PubMed: 11799113, PubMed: 1629222, PubMed: 1713771, PubMed: 2251280, PubMed: 24666235, PubMed: 25974265, PubMed: 7592877, PubMed: 7690548, PubMed: 9130696). Mediates processing of TGFB1, an essential step in TGF-beta-1 activation (PubMed: 7737999). Converts through proteolytic cleavage the non-functional Brain natriuretic factor prohormone into its active hormone BNP(1-32) (PubMed: 20489134, PubMed: 21763278). (Microbial infection) Probably cleaves and activates anthrax and diphtheria toxins. (Microbial infection) Required for H7N1 and H5N1 influenza virus infection probably by cleaving hemagglutinin. (Microbial infection) Able to cleave S.pneumoniae serine-rich repeat protein PsrP. (Microbial infection) Facilitates human coronaviruses EMC and SARS-CoV-2 infections by proteolytically cleaving the spike protein at the monobasic S1/S2 cleavage site. This cleavage is essential for spike protein-mediated cell-cell fusion and entry into human lung cells.
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