FA10 (light chain, Cleaved-Arg179) rabbit pAb
CAT:
855-ES20000-01
Size:
50 μL
Price:
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- Availability: 24/48H Stock Items & 2 to 6 Weeks non Stock Items.
- Dry Ice Shipment: No

FA10 (light chain, Cleaved-Arg179) rabbit pAb
- Description: Catalytic activity: Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin. function: 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. similarity: Belongs to the peptidase S1 family. similarity: Contains 1 Gla (gamma-carboxy-glutamate) domain. similarity: Contains 1 peptidase S1 domain. similarity: 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.
- Synonyms: Coagulation factor X (EC 3.4.21.6;Stuart factor;Stuart-Prower factor) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain]
- Gene ID: 2159
- UniProt: P00742
- Cellular Locus: Secreted.
- Host: Rabbit
- Species Reactivity: Human, Rat, Mouse,
- Immunogen: Synthesized peptide derived from human FA10 (light chain, Cleaved-Arg179)
- Clonality: Polyclonal
- Validated Applications: WB, ELISA
- Stability: 1 year
- Concentration: 1 mg/mL
- Dilution: WB 1:1000-2000 ELISA 1:5000-20000
- Molecular Weight: 15 53kD
- Storage Conditions: PBS with 0.02% sodium azide and 50% glycerol pH 7.4. Store at -20°C. Avoid repeated freeze-thaw cycles.