|Application ||WB, IHC-P, FC, E|
|Calculated MW||54732 Da|
|Antigen Region||351-381 aa|
|Other Names||Coagulation factor X, Stuart factor, Stuart-Prower factor, Factor X light chain, Factor X heavy chain, Activated factor Xa heavy chain, F10|
|Target/Specificity||This F10 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 351-381 amino acids from the C-terminal region of human F10.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||F10 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|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.|
|Tissue Location||Plasma; synthesized in the liver.|
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Provided below are standard protocols that you may find useful for product applications.
F10 is the vitamin K-dependent coagulation factor X of the blood coagulation cascade. This factor undergoes multiple processing steps before its preproprotein is converted to a mature two-chain form by the excision of the tripeptide RKR. Two chains of the factor are held together by 1 or more disulfide bonds; the light chain contains 2 EGF-like domains, while the heavy chain contains the catalytic domain which is structurally homologous to those of the other hemostatic serine proteases. The mature factor is activated by the cleavage of the activation peptide by factor IXa (in the intrisic pathway), or by factor VIIa (in the extrinsic pathway). The activated factor then converts prothrombin to thrombin in the presence of factor Va, Ca+2, and phospholipid during blood clotting.
Alba,R., Blood 114 (5), 965-971 (2009)
Borensztajn,K., Thromb. Res. 124 (2), 219-225 (2009)
Larson,P.J., Biochemistry 37 (14), 5029-5038 (1998)
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