Background:

F13A1 encodes the coagulation factor XIII A subunit. Coagulation factor XIII is the last zymogen to become activated in the blood coagulation cascade. Plasma factor XIII is a heterotetramer composed of 2 A subunits and 2 B subunits. The A subunits have catalytic function, and the B subunits do not have enzymatic activity and may serve as plasma carrier molecules. Platelet factor XIII is comprised only of 2 A subunits, which are identical to those of plasma origin. Upon cleavage of the activation peptide by thrombin and in the presence of calcium ion, the plasma factor XIII dissociates its B subunits and yields the same active enzyme, factor XIIIa, as platelet factor XIII. This enzyme acts as a transglutaminase to catalyze the formation of gamma-glutamyl-epsilon-lysine crosslinking between fibrin molecules, thus stabilizing the fibrin clot. It also crosslinks alpha-2-plasmin inhibitor, or fibronectin, to the alpha chains of fibrin. Factor XIII deficiency is classified into two categories: type I deficiency, characterized by the lack of both the A and B subunits; and type II deficiency, characterized by the lack of the A subunit alone. These defects can result in a lifelong bleeding tendency, defective wound healing, and habitual abortion.

Classification:

Primary antibody

Alternative names:

F13A1; F13A; Coagulation factor XIII A chain; Coagulation factor XIIIa; Protein-glutamine gamma-glutamyltransferase A chain; Transglutaminase A chain

Species reactivity:

Human

Host:

Rabbit

Isotype:

IgG

Immunogen:

The antiserum was produced against synthesized peptide derived from human FA13A. AA range:20-69

Concentration:

1 mg/ml

Molecular weight:

83267

Applications:

WB, ELISA

Storage:

-20°C for one year

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