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ADAMTS2 encodes a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) protein family.
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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 (show ADAMTS4 Antibodies) in five patients from four unrelated families
Data indicate that ADAMTS2 (show ADAMTS4 Antibodies) and 3 cleave the amino-propeptide of fibrillar collagens and regulate blood vessels homeostasis and lymphangiogenesis. Also, ADAMTS2 (show ADAMTS4 Antibodies) 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 (show ADAMTS4 Antibodies) was significantly overexpressed in Fibrous dysplasia (FD) tissues, but rarely expressed in normal bone tissues, suggesting that ADAMTS2 (show ADAMTS4 Antibodies) could be a potential biomarker for FD
Pathway inhibition studies revealed that ADAMTS-2 (show ADAMTS4 Antibodies) upregulation by IL-6 (show IL6 Antibodies) was mediated by JNK (show MAPK8 Antibodies) pathway.
ADAMTS-2 (show ADAMTS4 Antibodies), -3, and -13 expression, but not that of ADAMTS-14 (show ADAMTS14 Antibodies), are increased in plaques causing AMI (show CFD Antibodies) compared those associated with stable angina.
Data show that ADAMTS-2 (show ADAMTS4 Antibodies) is able to reduce proliferation of endothelial cells, and to induce their retraction and detachment from the substrate resulting in apoptosis.
Determination of the processing, activity and cleavage specificity of the bovine ADAMTS2 (show ADAMTS4 Antibodies) protein.
when conditioned media of TSP2 (show THBS2 Antibodies)-transfectants were added to cultures of bovine pulmonary microvascular endothelial cells (BPMEC), the BPMEC proliferation was significantly inhibited; suggesting that human TSP2 (show THBS2 Antibodies) 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 (show ADAMTS4 Antibodies) activity, the aminoprocollagen processing was strongly impaired, providing evidence for the requirement of these domains for proper enzyme function
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
, a disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motif, 2
, procollagen I N-proteinase
, procollagen I/II amino propeptide-processing enzyme
, procollagen N-endopeptidase