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The protein encoded by SERPINC1 is a plasma protease inhibitor and a member of the serpin superfamily. Additionally we are shipping Serine (Or Cysteine) Peptidase Inhibitor, Clade C (Antithrombin), Member 1 Antibodies (289) and Serine (Or Cysteine) Peptidase Inhibitor, Clade C (Antithrombin), Member 1 Kits (69) and many more products for this protein.
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Human SERPINC1 Protein expressed in Human - ABIN491621
Gardell, Krueger, Antrilli, Elokdah, Mayer, Orcutt, Crandall, Vlasuk: Neutralization of plasminogen activator inhibitor I (PAI-1) by the synthetic antagonist PAI-749 via a dual mechanism of action. in Molecular pharmacology 2007
Report high levels of latent antithrombin in plasma from patients with antithrombin deficiency caused by mutations affecting the stability of the native conformation.
Study identified one new small deletion within AT, which results in the loss of four amino acids (INEL) and is located at strand 3 of beta-sheet A, a region highly conserved in SERPINC1. This mutation leads to type I AT deficiency by promoting the intracellular retention of AT, which induces ER stress.
It was our aim to identify mutations in SERPINC1 causing transient antithrombin deficiency. SERPINC1 was sequenced in 214 cases with a positive test for antithrombin deficiency, including 67 with no deficiency in the sample delivered to our laboratory. The p.Val30Glu mutation (Antithrombin Dublin) was identified in five out of these 67 cases, as well as in three out of 127 cases with other SERPINC1 mutations.
different types of SERPINC1 mutations may play different roles in the development of VTE
aberrant N-glycosylation causing a recessive or transient antithrombin deficiency is a new form of thrombophilia that does not have a SERPINC1 gene defect
evaluation of serum proteins reveals that SERPINA1 (show SERPINA1 Proteins), SERPINA3 (show SERPINA3 Proteins) and SERPINC1 could be useful to discriminate healthy from colorectal carcinoma patients with a high sensitivity and specificity
The results this study reveal several novel mutations to the already growing list of SERPINC1 mutations, thereby adding to our knowledge of the molecular background of antithrombin deficiency.
Data indicate that all patients suffered from homozygous antithrombin (AT) deficiency caused by the mutation p.Leu131Phe in the AT gene (SERPINC1).
Studies indicate that antithrombin III (ATIII) and its gene SerpinC1 may be related to many diseases, including hypertension and kidney diseases.
The odds ratio of developing idiopathic fatal pulmonary embolism as a variant carrier for SERPINC1 is 144.2 (95% CI, 26.3-779.4; P = 1.7 x 10- 7).
RNA interference of Serpinc1 and/or Proc allows for evaluation of the function of these genes in vivo and provides a novel, controlled mouse model for spontaneous venous thrombosis.
ATIII may be protective in HIV-1 disease by inhibiting HIV-1 replication
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.
, serine (or cysteine) proteinase inhibitor, clade C (antithrombin), member 1
, serpin peptidase inhibitor, clade C (antithrombin), member 1
, anti-thrombin 3
, serpin C1
, serpin peptidase inhibitor, clade C, member 1
, antithrombin III
, serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1