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anti-Prothrombin Precursor, mAb (28H5)
Product Details | |
---|---|
Synonyms | F2; EC=3.4.21.5 |
Product Type | Monoclonal Antibody |
Properties | |
Clone | 28H5 |
Isotype | Mouse IgG2b κ |
Immunogen/Antigen | Protein purified from human plasma. |
Application |
ELISA |
Crossreactivity | Human |
Purity Detail | Ammonium sulfate precipitation. |
Formulation | Liquid. HEPES with 0.15M NaCl, 0.01% BSA, 0.03% sodium azide, and 50% glycerol. |
Isotype Negative Control | |
Other Product Data |
Click here for Original Manufacturer Product Datasheet |
Declaration | Manufactured by AbFrontier |
Shipping and Handling | |
Shipping | BLUE ICE |
Short Term Storage | +4°C |
Long Term Storage | -20°C |
Use/Stability | Stable for at least 1 year after receipt when stored at -20°C. |
Documents | |
MSDS | Inquire |
Product Specification Sheet | |
Datasheet |
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Prothrombin precursor is synthesized in liver as a precursor of prothrombin containing a signal sequence and a propeptide domain at the N-terminus. Before its secretion into plasma, this precursor undergoes several posttranslational modifications, including removal of signal sequence and propeptide domains, glycosylation, and γ-glutamyl-carboxylation reaction. Prothrombin, cleaved by the prothrombinase enzyme complex that consists of serine protease factor Xa, cofactor Va, phospholipids and calcium, is converted to thrombin which converts fibrinogen into fibrin which in turn strengthens a protective clot. Activation of prothrombin is crucial in physiological and pathological coagulation. Various rare diseases involving prothrombin(e.g. hypoprothrombinemia) have been described. Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing.
1) Zhang P, Suttie JW, Blood (1994) vol.84: 169-75. (General)
2) Taylor R, Wallin R, Biochem J. (1991) vol.277(Pt 1) : pp.59–65. (General)
3) J W Suttie, et al, Proc Natl Acad Sci U S A. (1987) vol.84(3): pp.634–7. (General)