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SERPINC1 Antibody (Ascites)
Mouse Monoclonal Antibody (Mab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, E |
|---|---|
| Primary Accession | P01008 |
| Other Accession | NP_000479.1 |
| Reactivity | Human, Rat |
| Host | Mouse |
| Clonality | Monoclonal |
| Isotype | IgG1 |
| Clone/Animal Names | 435CT4.7.4 |
| Calculated MW | 52602 Da |
| Antigen Region | 50-79 aa |
| Gene ID | 462 |
|---|---|
| Other Names | Antithrombin-III, ATIII, Serpin C1, SERPINC1, AT3 |
| Target/Specificity | This SERPINC1 antibody is generated from mice immunized with a KLH conjugated synthetic peptide between 50-79 amino acids from human SERPINC1. |
| Dilution | WB~~1:100~1600 |
| Format | Mouse monoclonal antibody supplied in crude ascites with 0.09% (W/V) sodium azide. |
| 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 | SERPINC1 Antibody (Ascites) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | SERPINC1 |
|---|---|
| Synonyms | AT3 |
| Function | Most important serine protease inhibitor in plasma that regulates the blood coagulation cascade (PubMed:15140129, PubMed:15853774). AT-III inhibits thrombin, matriptase-3/TMPRSS7, as well as factors IXa, Xa and XIa (PubMed:15140129). Its inhibitory activity is greatly enhanced in the presence of heparin. |
| Cellular Location | Secreted, extracellular space. |
| Tissue Location | Found in plasma. |
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Provided below are standard protocols that you may find useful for product applications.
Background
The protein encoded by this gene is a plasma protease inhibitor and a member of the serpin superfamily. This protein inhibits thrombin as well as other activated serine proteases of the coagulation system, and it regulates the blood coagulation cascade. The protein includes two functional domains: the heparin binding-domain at the N-terminus of the mature protein, and the reactive site domain at the C-terminus. The inhibitory activity is enhanced by the presence of heparin. More than 120 mutations have been identified for this gene, many of which are known to cause antithrombin-III deficiency.
References
Romero, R., et al. Am. J. Obstet. Gynecol. 203 (4), 361 (2010) :
Bailey, S.D., et al. Diabetes Care 33(10):2250-2253(2010)
Zhang, G.S., et al. Blood Coagul. Fibrinolysis 21(6):588-591(2010)
Bunkenborg, J., et al. Proteomics 4(2):454-465(2004)
Picard, V., et al. Biochemistry 34(26):8433-8440(1995)
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