PROZ Mouse anti-Human, Clone: OTI4F1, liquid, TrueMAB™

Description

• PROZ protein Z, vitamin K-dependent plasma glycoprotein
• It is 62 kDa large and 396 amino acids long
• It has four domains: a gla-rich region, two EGF-like domains and a trypsin-like domain
• It lacks the serine residue that would make it catalytically active as a serine protease
• It is a member of the coagulation cascade, the group of blood proteins that leads to the formation of blood clots
• It is vitamin K-dependent, and its functionality is therefore impaired in warfarin therapy
• It is a glycoprotein
• Although it is not enzymatically active, it is structurally related to several serine proteases of the coagulation cascade: factors VII, IX, X and protein C
• The carboxyglutamate residues (which require vitamin K) bind protein Z to phospholipid surfaces
• The main role of protein Z appears to be the degradation of factor Xa
• This is done by protein Z-related protease inhibitor (ZPI), but the reaction is accelerated 1000-fold by the presence of protein Z
• Oddly, ZPI also degrades factor XI, but this reaction does not require the presence of protein Z
• In some studies, deficiency states have been associated with a propensity to thrombosis
• Others, however, link it to bleeding tendency; there is no clear explanation for this, as it acts physiologically as an inhibitor, and deficiency would logically have led to a predisposition for thrombosis.