Background:

Catalytic activity:Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin.|Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va| calcium and phospholipid during blood clotting.|online information:Factor X entry|PTM:N- and O-glycosylated.|PTM:The activation peptide is cleaved by factor IXa (in the intrinsic pathway)| or by factor VIIa (in the extrinsic pathway).|PTM:The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.|PTM:The vitamin K-dependent| enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium.|Belongs to the peptidase S1 family.|Contains 1 Gla (gamma-carboxy-glutamate) domain.|Contains 1 peptidase S1 domain.|Contains 2 EGF-like domains.|subunit:The two chains are formed from a single-chain precursor by the excision of two Arg residues and are held together by 1 or more disulfide bonds.|tissue specificity:Plasma; synthesized in the liver.|

Classification:

Primary antibody

Alternative names:

FA10 ;light chain; Cleaved-Arg179; Coagulation factor X; EC 3.4.21.6; Stuart factor; Stuart-Prower factor; Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain;

Species reactivity:

Human, Rat, Mouse

Host:

Rabbit

Isotype:

IgG

Immunogen:

Synthesized peptide derived from human FA10 (light chain| Cleaved-Arg179)

Concentration:

1 mg/ml

Molecular weight:

53680

Applications:

WB, ELISA

Storage:

-20°C for 1 year

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