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The protein encoded by SERPINC1 is a plasma protease inhibitor and a member of the serpin superfamily. De plus, nous expédions Serine (Or Cysteine) Peptidase Inhibitor, Clade C (Antithrombin), Member 1 Kits (71) et Serine (Or Cysteine) Peptidase Inhibitor, Clade C (Antithrombin), Member 1 Protéines (38) et beaucoup plus de produits pour cette protéine.
Showing 10 out of 316 products:
Dog (Canine) Polyclonal SERPINC1 Primary Antibody pour WB - ABIN610759
Cool, Normant, Shen, Chen, Pannell, Zhang, Loh: Carboxypeptidase E is a regulated secretory pathway sorting receptor: genetic obliteration leads to endocrine disorders in Cpe(fat) mice. dans Cell 1997
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Human Polyclonal SERPINC1 Primary Antibody pour IHC, IHC (p) - ABIN4352910
Kuusisto, Haapasaari, Remes, Bloigu, Karihtala, Turpeenniemi-Hujanen, Kuittinen: Antithrombin III is probably not a suitable biomarker for diagnosis of primary central nervous system lymphoma. dans Annals of hematology 2015
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Human Monoclonal SERPINC1 Primary Antibody pour IHC (p), IHC - ABIN449427
Wang, Zhang, Sze, van de Weg, Vernooij, Schoneveld, Tan, Versteeg, Timmers, Lam, de Kleijn: Lowering Low-Density Lipoprotein Particles in Plasma Using Dextran Sulphate Co-Precipitates Procoagulant Extracellular Vesicles. dans International journal of molecular sciences 2018
Laboratory tests and direct sequencing of PROC and SERPINC1 were conducted for the patient and his family members. Coagulation tests revealed that the patient presented type I antithrombin deficiency combined with decreased protein C activity resulting from a small insertion mutation c.848_849insGATGT in SERPINC1 and a short deletion variant c.572_574delAGA in PROC.
Thirty-one members of a single family were included. Clinical data was collected regarding thrombotic history. The mutation was identified by direct sequencing of the SERPINC1 gene. HEK293 cells were transfected with wild type and mutant SERPINC1 plasmids.
the first report of regulatory region polymorphisms in SERPINC1 gene in Indian population
this study shows that risk for thrombosis is associated with the different SERPINC1 genotypes
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 (Montrer SERPINA1 Anticorps), SERPINA3 (Montrer SERPINA3 Anticorps) and SERPINC1 could be useful to discriminate healthy from colorectal carcinoma patients with a high sensitivity and specificity
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