Coagulation Factor IX, also known as Christmas Factor, is a secreted by the liver and plays a key role in the activation of the intrinsic clotting cascade (1). Factor IX consists of a Gla domain, two tandem EGF-like domains, an activation peptide, and an S1 serine protease domain (2). Mature human Factor IX shares approximately 81% amino acid sequence identity with mouse and rat Factor IX. Alternative splicing generates an additional isoform that lacks the first EGF-like domain. The Gla domain is modified by Vitamin K-dependent gamma-carboxylation and mediates the association of Factor IX with phospholipid bilayers (3, 4). The activation peptide is removed by Factor XIa mediated cleavage, resulting in heavy and light chains that remain disulfide-linked (5). Factor IX can also be activated by proteolytic factors in multiple snake venoms (6, 7). Active Factor IX associates with Factor VIIIa on the platelet surface where it cleaves and activates Factor X, leading to Fibrin deposition and clot formation (8-10). The human Factor IX gene is highly polymorphic, and Hemophilia B can be caused by X-linked deficiency of Factor IX activity (11-14).

Cf9;F9

Mouse

Detects Mouse F9 in ELISAs

Capture Antibody:PBS with 0.04% Proclin 300, 50% glycerol, pH 7.4; Detection Antibody:PBS with 0.04% Proclin 300, 1% protective protein, 50% glycerol, pH 7.4

-20℃

12个月