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ADAMTS13 encodes a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motif) protein family. Additionally we are shipping ADAMTS13 Kits (27) and ADAMTS13 Proteins (5) and many more products for this protein.
Showing 10 out of 78 products:
Human Polyclonal ADAMTS13 Primary Antibody for EIA, IHC (p) - ABIN359601
Levy, Nichols, Lian, Foroud, McClintick, McGee, Yang, Siemieniak, Stark, Gruppo, Sarode, Shurin, Chandrasekaran, Stabler, Sabio, Bouhassira, Upshaw, Ginsburg, Tsai: Mutations in a member of the ADAMTS gene family cause thrombotic thrombocytopenic purpura. in Nature 2001
Show all 7 references for ABIN359601
Human Polyclonal ADAMTS13 Primary Antibody for 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
Show all 3 references for ABIN4278265
Human Polyclonal ADAMTS13 Primary Antibody for IHC (p), WB - ABIN391641
Zheng, Chung, Takayama, Majerus, Sadler, Fujikawa: Structure of von Willebrand factor-cleaving protease (ADAMTS13), a metalloprotease involved in thrombotic thrombocytopenic purpura. in The Journal of biological chemistry 2001
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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 (show THOP1 Antibodies) ADAMTS13 does not directly promote development of adipose tissue.
findings provide further evidence on the pathophysiological role for the ADAMTS13/VWF (show VWF Antibodies) axis in atherosclerosis
Carboxyl terminus of ADAMTS13 directly inhibits platelet aggregation and ultra large von Willebrand factor (show VWF Antibodies) string formation under flow in a free-thiol-dependent manner.
The results indicate that the microvascular process induced by ADAMTS13 deficiency triggers complement activation on platelets and the endothelium, which may contribute to formation of thrombotic microangiopathy.
model of acute myocardial infarction in ADAMTS13 gene deleted (Adamts13 -/-) mice
We hypothesize that ADAMTS13 protects brain from ischemia-reperfusion injury by regulating von Willebrand factor (show VWF Antibodies) -dependent inflammation as well as microvascular plugging
Cyclophilin B (show PPIB Antibodies) activity regulated secretion and activity of ADAMTS13.
ADAMTS13 is the key protease that regulates the multimeric state of VWF (show VWF Antibodies). Without ADAMTS13, VWF (show VWF Antibodies) multimers can grow to pathologically large sizes. This is a risk factor for the life-threatening condition thrombotic thrombocytopenic purpura (TTP)
Stroke in human immunodeficiency virus infection is associated with a prothrombotic state, characterized by elevated von Willebrand factor (show VWF Antibodies) and low ADAMTS13 levels
An in vitro model for LVAD associated aVWD demonstrated that ADAMTS-13 and platelets contribute to the depletion of HMWM of VWF (show VWF Antibodies).
Case Report: D173G mutation in the catalytic domain of ADAMTS-13, never described before, causes a severe form of Upshaw-Schulman syndrome.
Type 2B mutations localized in the A1 domain could enhance the sensitivity to ADAMTS13-mediated proteolysis. When GPIbalpha (show GP1BA Antibodies) participated, there was a dramatically increased proteolytic cleavage of VWF (show VWF Antibodies) by ADAMTS13 to rVWF-WT, excluding some type 2B mutants.
ADAMTS-13 conformational activation leads to cryptic epitope/exosite exposure in proximal and distal domains, increasing activity. 3 linker regions in the distal domains make it flexible, enabling the interaction of the proximal and the T8-CUB2 domains.
ADAMTS-13 is a clinical target to reduce vWF (show VWF Antibodies) degradation, improve vWF (show VWF Antibodies) function, and potentially reduce bleeding during LVAD support.
Glycan stabilization of the VWF (show VWF Antibodies) A2 domain acts together with the Ca(2 (show CA2 Antibodies)+)binding site and vicinal cysteine disulfide bond to control unfolding and ADAMTS13 proteolysis.
These data provide evidence for the involvement of CUB2 domain of ADAMTS13 - reactive CD4 (show CD4 Antibodies)(+)T cells in the etiology of acquired thrombotic thrombocytopenic purpura.
Congenital thrombotic thrombocytopenic purpura (Upshaw-Schulman syndrome) caused by novel ADAMTS13 mutations.
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
, ADAM metallopeptidase with thrombospondin type 1 motif, 13 isoform 1 preproprotein-like
, A disintegrin and metalloproteinase with thrombospondin motifs 13-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
, ADAM-TS 13
, ADAMTS13 isoform IAP-b
, a disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motif, 13
, vWF-CP mRNA for von Willebrand factor-cleaving
, vWF-cleaving protease
, von Willebrand factor-cleaving protease
, a disintegrin-like and metallopeptidase (reprolysin type) with thrombospondin type 1 motif, 13