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The protein encoded by SERPINC1 is a plasma protease inhibitor and a member of the serpin superfamily. 再加上，我们可以发Serine (Or Cysteine) Peptidase Inhibitor, Clade C (Antithrombin), Member 1 抗体 (289) 和 Serine (Or Cysteine) Peptidase Inhibitor, Clade C (Antithrombin), Member 1 蛋白 (33)和数多这个蛋白质的别的产品。
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Human SERPINC1 ELISA Kit for Sandwich ELISA - ABIN2685464
Kulka, Tryba, Lange: [Are there certified indications for the use of antithrombin III in intensive care]. in Anästhesiologie, Intensivmedizin, Notfallmedizin, Schmerztherapie : AINS 2001
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Mouse (Murine) SERPINC1 ELISA Kit for Sandwich ELISA - ABIN2685465
Oelschläger, Römisch, Staubitz, Stauss, Leithäuser, Tillmanns, Hölschermann: Antithrombin III inhibits nuclear factor kappaB activation in human monocytes and vascular endothelial cells. in Blood 2002
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Human SERPINC1 ELISA Kit for Competition ELISA - ABIN2685463
Peltier, Roperch, Audebert, Borg, Camoin: Quantitative proteomic analysis exploring progression of colorectal cancer: Modulation of the serpin family. in Journal of proteomics 2016
Human SERPINC1 ELISA Kit for Sandwich ELISA - ABIN418021
Gao, Ma, Liu, Teng, Wang, Su: Thalidomide and multiple myeloma serum synergistically induce a hemostatic imbalance in endothelial cells in vitro. in Thrombosis research 2015
Human SERPINC1 ELISA Kit for Sandwich ELISA - ABIN832327
Wang, Yuan, Zhong, Wen, Deng, Liang, Zheng: The anticoagulant effect of PGI2S and tPA in transgenic umbilical vein endothelial cells is linked to up-regulation of PKA and PKC. in International journal of molecular sciences 2014
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 (显示 SERPINA1 ELISA试剂盒), SERPINA3 (显示 SERPINA3 ELISA试剂盒) 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).
In Hungary, the founder mutation, ATBp3, is the most common Antithrombin deficiency
Our studies of ATIII in-cell folding reveal a surprising, biased order of disulfide bond formation, with early formation of the C-terminal disulfide, before formation of the N-terminal disulfides, critical for folding to the active, metastable state
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