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ADAMTS13 encodes a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motif) protein family. Zusätzlich bieten wir Ihnen ADAMTS13 Kits (36) und ADAMTS13 Proteine (6) und viele weitere Produktgruppen zu diesem Protein an.
Showing 10 out of 101 products:
Human Polyclonal ADAMTS13 Primary Antibody für WB - ABIN152016
Tao, Wang, Choi, Bernardo, Nishio, Sadler, López, Dong: Cleavage of ultralarge multimers of von Willebrand factor by C-terminal-truncated mutants of ADAMTS-13 under flow. in Blood 2005
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Human Polyclonal ADAMTS13 Primary Antibody für ELISA, IHC - ABIN4278265
Ganburged, Suda, Saito, Yamazaki, Isokawa, Moriyama: Dilated capillaries, disorganized collagen fibers and differential gene expression in periodontal ligaments of hypomorphic fibrillin-1 mice. in Cell and tissue research 2010
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Human Polyclonal ADAMTS13 Primary Antibody für IP, WB - ABIN251718
Feng, Eyler, Zhang, Maga, Nester, Kroll, Smith, Afshar-Kharghan: Partial ADAMTS13 deficiency in atypical hemolytic uremic syndrome. in Blood 2013
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Human Polyclonal ADAMTS13 Primary Antibody für WB - ABIN251717
Turner, Nolasco, Ruggeri, Moake: Endothelial cell ADAMTS-13 and VWF: production, release, and VWF string cleavage. in Blood 2009
Low ADAMTS-13 activity is associated with an increased risk of coronary heart disease in the elderly, independently of VWF (zeige VWF Antikörper) and established cardiovascular risk factors
As folding stability was progressively disrupted, proteolysis by ADAMTS13 increased. Due to the range of folding stabilities and wide distribution of VWF (zeige VWF Antikörper) A2 domain mutations studied, we conclude that these mutations disrupt regulated folding of the VWF (zeige VWF Antikörper) A2 domain
The 'closed' conformation of ADAMTS-13 restricts its specificity and protects against fibrinogenolysis
Our results indicate that the secondary TMA syndrome and its poor outcome is characterized by relative ADAMTS13 deficiency, inflammation, and complement activation with consumption via the classical and alternative pathways.
Diagnosis of thrombotic thrombocytopenic purpura among patients with ADAMTS13 Activity 10%-20.
Rare genetic variants in the ADAMTS13 on Willebrand factor-binding domain contribute to pediatric stroke.
No correlation was found between VWF (zeige VWF Antikörper)/ADAMTS13 and infarct size in patients. Patients suffering from intramyocardial hemorrhage had significantly higher VWF (zeige VWF Antikörper) activity and lower ADAMTS13 activity. Intracoronary administration of rADAMTS13 did not decrease infarct size or IMH in a porcine model of myocardial ischaemia-reperfusion, disputing the idea that the imbalance in ADAMTS13 and VWF (zeige VWF Antikörper) as the cause of no reflow.
both in acute and chronic cerebrovascular disease patients, ADAMTS13 levels were significantly decreased, with the lowest ADAMTS13 levels found in acute stroke patients. This difference was even more distinct when the ratio of VWF:ADAMTS13 was considered. These results demonstrate the potentially important involvement of the VWF (zeige VWF Antikörper)/ADAMTS13 axis in ischemic stroke.
Placental trophoblasts and villous vessel endothelial cells produce a full-length and functional ADAMTS13 protease. Placental expression of ADAMTS13 exhibits a dynamic change during pregnancy, which seems to be inhibited in late pregnancy and in patients with severe preeclampsia.
ADAMTS13 activity appears to be an independent risk factor for incident prediabetes and type 2 diabetes.
results suggest that ADAMTS13 controls key steps of ischemic vascular remodeling and that recombinant ADAMTS13 is a putative therapeutic avenue for promoting stroke recovery.
ADAMTS13 retards progression of diabetic nephropathy, most likely by inhibiting VWF (zeige VWF Antikörper)-dependent intrarenal thrombosis.
administration of ADAMTS13 5 minutes after occlusion dose-dependently dissolved these t-PA (zeige PLAT Antikörper)-resistant thrombi resulting in fast restoration of MCA (zeige RSPH1 Antikörper) patency and consequently reduced cerebral infarct sizes
Sleeping beauty transposon-mediated gene therapy achieved sustained expression of transgene ADAMTS13 and long-term prophylaxis against congenital thrombotic thrombocytopenic purpura in Adamts13(-/-) mice.
Results also suggest that Toxoplasma gondii-mediated apoptosis might play a pivotal role and a different type of role in the mechanism of neurodegeneration and neuropathology in the process of toxoplasma encephalitis. Furthermore, expression of ADAMTS-13 might give an idea of the progress and is critical for diagnosis of this disease.
Letter: deficiency of ADAMTS13 results in increased formation of venous thrombosis in mice.
ADAMTS13 substrate specificity
Data indicate that the p.D187H mutation impairs ADAMTS13 activity and secretion and may contribute to thrombotic thrombocytopenic purpura.
Data show that metalloendopeptidase (zeige THOP1 Antikörper) ADAMTS13 does not directly promote development of adipose tissue.
findings provide further evidence on the pathophysiological role for the ADAMTS13/VWF (zeige VWF Antikörper) axis in atherosclerosis
This gene encodes a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motif) protein family. Members of the family share several distinct protein modules, including a propeptide region, a metalloproteinase domain, a disintegrin-like domain, and a thrombospondin type 1 (TS) motif. Individual members of this family differ in the number of C-terminal TS motifs, and some have unique C-terminal domains. The enzyme encoded by this gene is the von Willebrand Factor (vWF)-cleaving protease, which is responsible for cleaving at the site of Tyr842-Met843 of the vWF molecule. A deficiency of this enzyme is associated with thrombotic thrombocytopenic purpura. Alternative splicing of this gene generates multiple transcript variants encoding different isoforms.
ADAM metallopeptidase with thrombospondin type 1 motif, 13
, A disintegrin and metalloproteinase with thrombospondin motifs 13
, a disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motif, 13
, vWF-cleaving protease
, von Willebrand factor-cleaving protease
, ADAM-TS 13
, ADAMTS13 isoform IAP-b
, vWF-CP mRNA for von Willebrand factor-cleaving
, ADAM metallopeptidase with thrombospondin type 1 motif, 13 isoform 1 preproprotein-like
, ADAM metallopeptidase with thrombospondin type 1 motif, 12
, A disintegrin and metalloproteinase with thrombospondin motifs 12
, A disintegrin and metalloproteinase with thrombospondin motifs 13-like
, a disintegrin-like and metallopeptidase (reprolysin type) with thrombospondin type 1 motif, 13