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Adamts2 encodes a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) protein family. De plus, nous expédions Adamts2 Anticorps (42) et Adamts2 Kits (19) et beaucoup plus de produits pour cette protéine.
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ADAMTS2 plays a critical role in cardiac hypertrophy induced by pressure overload in mouse model.
Data show that the high titer and specific rabbit anti-ADAMTS2 antibody has been prepared successfully.
There is no significant genotype effect of ADAMTS2 on age, height, weight, BMI or sex on risk of Achilles tendon pathology.
Data show that ADAMTS-2 is able to reduce proliferation of endothelial cells, and to induce their retraction and detachment from the substrate resulting in apoptosis.
The extent of liver fibrosis is reduced in ADAMTS2-deficient mice in comparison with their wild type littermates.
Data show thatincreased mRNA of Lamb3 (Montrer LAMB3 Protéines) and Adamts2 and enhanced activities of metalloproteinases MMP1 (Montrer MMP1 Protéines), 2 and 7 in transgenic mice expressing the HLA-DQ8.
We identified three novel homozygous loss-of-function mutations (c.2927_2928delCT, p.(Pro976Argfs*42); c.669_670dupG, p.(Pro224Argfs*24); and c.2751-2A>T) and one compound heterozygous mutation (c.2T>C, p.? and c.884_887delTGAA, p.(Met295Thrfs26*)) in ADAMTS2 in five patients from four unrelated families
Data indicate that ADAMTS2 and 3 cleave the amino-propeptide of fibrillar collagens and regulate blood vessels homeostasis and lymphangiogenesis. Also, ADAMTS2 deficiency leads to the dermatosparactic type of Ehlers-Danlos syndrome. [review]
IL-1a is a strong positive regulator of ADAMTS-2 and ADAMTS-3 expression.
ADAMTS2 was significantly overexpressed in Fibrous dysplasia (FD) tissues, but rarely expressed in normal bone tissues, suggesting that ADAMTS2 could be a potential biomarker for FD
Pathway inhibition studies revealed that ADAMTS-2 (Montrer ADAMTS4 Protéines) upregulation by IL-6 (Montrer IL6 Protéines) was mediated by JNK (Montrer MAPK8 Protéines) pathway.
ADAMTS-2 (Montrer ADAMTS4 Protéines), -3, and -13 expression, but not that of ADAMTS-14, are increased in plaques causing AMI (Montrer CFD Protéines) compared those associated with stable angina.
Determination of the processing, activity and cleavage specificity of the bovine ADAMTS2 protein.
when conditioned media of TSP2 (Montrer THBS2 Protéines)-transfectants were added to cultures of bovine pulmonary microvascular endothelial cells (BPMEC), the BPMEC proliferation was significantly inhibited; suggesting that human TSP2 (Montrer THBS2 Protéines) is a potential inhibitor of angiogenesis
Although exons 3-5 or 14-16 encode protein domains that have not been recognized as crucial for ADAMTS-2 activity, the aminoprocollagen processing was strongly impaired, providing evidence for the requirement of these domains for proper enzyme function
specific ADAMTS-2 domains cleave the aminopropeptide of fibrillar procollagens types I-III and V
This gene encodes a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) 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 excises the N-propeptide of type I, type II and type V procollagens. Mutations in this gene cause Ehlers-Danlos syndrome type VIIC, a recessively inherited connective-tissue disorder. Alternative splicing results in multiple transcript variants.
A disintegrin and metalloproteinase with thrombospondin motifs 2
, ADAM-TS 2
, PC I-NP
, a disintegrin and metalloproteinase with thrombospondin repeats
, a disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motif, 2
, procollagen I/II amino propeptide-processing enzyme
, procollagen N-endopeptidase
, procollagen N-proteinase
, procollagen I N-proteinase
, a disintegrin-like and metallopeptidase (reprolysin type) with thrombospondin type 1 motif, 2