Lane 1: HL-60 cell lysate
Lane 2: HepG2 cell lysate
Lane 3: SiHa cell lysate
Mouse monoclonal primary
SERPINC1 Mouse Monoclonal Antibody [15F2] (EM1901-10)
Recombinant protein within human serpinc1 aa 150-370 / 464.
HL-60 cell, HepG2 cell, SiHa cell, rat testis tissue, human lung carcinoma tissue, human liver tissue, human liver carcinoma tissue, mouse kidney tissue, HCT116 cell.
Store at +4C after thawing. Aliquot store at -20C. Avoid repeated freeze / thaw cycles.
1*PBS (pH7.4), 0.2% BSA, 50% Glycerol. Preservative: 0.05% Sodium Azide.
Protein A purified.
ANT3_HUMAN antibody; Antithrombin antibody; Antithrombin III antibody; Antithrombin-III antibody; AntithrombinIII antibody; AT 3 antibody; AT III antibody; AT3 antibody; AT3D antibody; ATIII antibody; Heparin cofactor I antibody; MGC22579 antibody; Serine (or cysteine) proteinase inhibitor clade C (antithrombin) member 1 antibody; Serine cysteine proteinase inhibitor clade C member 1 antibody; Serine proteinase inhibitor clade C member 1 antibody; Serpin C1 antibody; Serpin family C member 1 antibody; Serpin peptidase inhibitor clade C (antithrombin) member 1 antibody; SERPINC1 antibody; THPH7 antibody
Belongs to the serpin family.
Found in plasma.
Phosphorylated by FAM20C in the extracellular medium.
Extracellular space or secreted.
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. Most important serine protease inhibitor in plasma that regulates the blood coagulation cascade. AT-III inhibits thrombin, matriptase-3/TMPRSS7, as well as factors IXa, Xa and XIa. Its inhibitory activity is greatly enhanced in the presence of heparin.