ACE, also known as peptidyl-dipeptidase A, is a zinc metallopeptidase important for blood pressure control and osmotic balance. ACE is a type I membrane protein that exists in two functionally distinct and spatially restricted isoforms, somatic ACE and germinal ACE. It cleaves C-terminal dipeptides from Angiotensin I, Bradykinin, and various other oligopeptides to regulate their activity. Because of its expression patterns and specificities, ACE is important for immune, reproductive, and nervous system functions. It is also associated with Alzheimer's disease as it degrades Amyloid beta peptide, thereby retarding Amyloid beta aggregation, deposition, fibril formation, and cytotoxicity.
Catalog # 1513-ZN
Furin is a ubiquitously expressed member of the pro-protein convertase (PC) family, which belongs to the subtilisin superfamily of calcium-dependent serine proteases. Furin has a broad pH optimum and processes a variety of pro-proteins located on the cell surface and in secretory pathway compartments. It cleaves after R-X-K/R-R-like motifs, which usually reside at the ends of pro-protein pro regions. Pro-protein substrates include growth factors and receptors, extracellular matrix proteins, and other proteases. Furin plays an essential role in embryogenesis and homeostasis and is implicated in various pathologies such as cancer, neurodegenerative disease, and anthrax infection.
Catalog # 1503-SE
HGF activator (HGFA) is a serine endopeptidase that has been implicated in blood coagulation at sites of tissue injury. It cleaves the peptide bond between R494 and V495 of the single-chain human HGF precursor, generating the active heterodimer. HGFA is produced and secreted by the liver and usually circulates in the blood as an inactive zymogen. It can be activated by thrombin or thermolysin, or inhibited by HGFA inhibitors (HAIs). The HGFA zymogen has weak affinity for heparin but acquires strong affinity for heparin when activated, possibly ensuring restriction of enzyme activity to the site of tissue injury.
Catalog # 1514-SE
HtrA2/Omi is a serine protease and the mammalian homolog of bacterial high temperature requirement protein (HtrA). It is a nuclear-encoded protein but possesses a mitochondria localizing sequence that is cleaved off upon translocation into the mitochondrial intermembrane space. Like Smac/Diablo, this processing exposes an N-terminal IAP-binding/Reaper-like motif that is capable of binding IAP BIR2 or BIR3 domains. Upon release from mitochondria in response to pro-apoptotic Bcl-2 family member-associated stimuli, HtrA2/Omi reverses IAP inhibition of caspases. Unlike Smac/Diablo, the protease domain of HtrA2/Omi can cleave IAPs, irreversibly neutralizing caspase activity.
Catalog # 1458-HT
cIAP-1, also known as HIAP-2 and MIHB, is a member of the inhibitor of apoptosis (IAP) family of proteins that inhibit the proteolytic activity of mature caspases. cIAP-1 has 3 BIR (baculovirus inhibitor of apoptosis) domains, a caspase recruitment domain (CARD), and a RING finger domain. cIAP-1 binds caspases via its BIR and CARD domains, thereby inhibiting caspase activity. Caspase activity may be restored through interactions with IAP-binding/Reaper-like motifs on proteins such as SMAC/Diablo and HtrA2/Omi, which are released from the mitochondria via pro-apoptotic Bcl-2 family member-associated stimuli. cIAP-1 is also capable of ubiquitinating IAP inhibitors via its RING finger domain and targeting them for degradation.
Catalog # 818-IA
Serpin F2/alpha2-Antiplasmin, a member of the Serpin superfamily of serine protease inhibitors, is the primary physiological inhibitor of Plasmin, which is responsible for the dissolution of fibrin clots. While Serpin F2/alpha2-Antiplasmin is produced mainly by liver and kidney tissues, its mRNA is also expressed by muscle, intestine, nervous system, placenta, and other tissues suggesting that it may be a key regulator of Plasmin-mediated proteolysis in these tissues. Individuals lacking Serpin F2/alpha2-Antiplasmin have normal development and fertility but typically have bleeding complications. Serpin F2/alpha2-Antiplasmin is also capable of Trypsin and Chymotrypsin inhibition.
Catalog # 1470-PI