SerpinC1 / SERPINC1 / AntithrombinIII Protein (His Tag)

SerpinC1 / SERPINC1 / Antithrombin-III Protein Datasheet

SerpinC1 / SERPINC1 / Antithrombin-III Protein Inquiry ( Available Sizes )

50μg:  Inquiring Price;    200ug: Inquiring Price;   ≥1mg Bulk:  Inquiring Price

SerpinC1 / SERPINC1 / Antithrombin-III Protein Product Information

• SerpinC1 Synonym: SerpinC1, AT3, ATIII, MGC22579
• Protein Construction: A DNA sequence encoding the human SerpinC1 precursor (NP_000479.1) (Met 1-Lys 464) was expressed with a C-terminal polyhistidine tag.
• Source: Human
• Expression Host: Human Cells

SerpinC1 / SERPINC1 / Antithrombin-III Protein QC Testing

• Purity: > 95% as determined by SDS-PAGE
• Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method.
• Stability: Samples are stable for up to twelve months from date of receipt at -70℃
• Predicted N terminal: His 33
• Molecular Mass: The recombinant human SerpinC1 consists of 443 amino acids and has a predicted molecular mass of 50.5 kDa. In SDS-PAGE, the apparent molecular mass of rhSerpinC1 is approximately 55-60 kDa due to glycosylation.
• Formulation: Lyophilized from sterile PBS , pH 7.4
  1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
  2. Please contact us for any concerns or special requirements.
• SDS-PAGE:

SerpinC1 / SERPINC1 / Antithrombin-III Protein Usage Guide

• Storage: Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

SerpinC1 / SERPINC1 / Antithrombin-III Protein Description

SerpinC1, also known as antithrombin III (AT III), is a member of the serpin superfamily of serine protease inhibitors. SerpinC1 synthesized in the liver is the principal plasma serpin of blood coagulation proteases and inhibits thrombin and other factors such as Xa by the formation of covalently linked complexes. In common with SerpinA5 and D1, the inhibitory activity of SerpinC1 undergoes a dramatic increase in the presence of heparin and other glycosaminoglycans. The deficiency or functional abnormality of ATIII may result in an increased risk of thromboembolic disease, such as deep vein thrombosis and pulmonary embolism. In addition, it has been reported that SerpinC1 can alter or influence inflammatory processes via inhibition of NF-κB activation or actin polymerization.

References

1. Chandra, T. et al., 1983, Proc. Natl. Acad. Sci. 80: 1845-1848.
2. Perry, D.J. et al., 1994, Blood. Rev. 8: 37-55.
3. Chuang, Y.J. et al., 2001, Biochemistry. 40: 6670-6679.
4. Saito, H. et al., 2005, J. Leukoc. Biol. 78: 777-784.
5. Oelschlager, C. et al., 2002, Blood. 99: 4015-4020.