ADAMTS2 Antibody

1. 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 PMID: 26765342
2. 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] PMID: 25863161
3. IL-1a is a strong positive regulator of ADAMTS-2 and ADAMTS-3 expression. PMID: 26232334
4. 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 PMID: 25674217
5. Pathway inhibition studies revealed that ADAMTS-2 upregulation by IL-6 was mediated by JNK pathway. PMID: 24752352
6. 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. PMID: 20574651
7. Determination of the processing, activity and cleavage specificity of the bovine ADAMTS2 protein. PMID: 16046392
8. when conditioned media of TSP2-transfectants were added to cultures of bovine pulmonary microvascular endothelial cells (BPMEC), the BPMEC proliferation was significantly inhibited; suggesting that human TSP2 is a potential inhibitor of angiogenesis PMID: 11788898
9. 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 PMID: 15373769

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HGNC: 218

OMIM: 225410

KEGG: hsa:9509

STRING: 9606.ENSP00000251582

UniGene: Hs.23871