Synthesized peptide derived from ADAMTS-2 . at AA range: 1140-1220

ADAMTS-2 Polyclonal Antibody detects endogenous levels of ADAMTS-2 protein.

ADAMTS2

A disintegrin and metalloproteinase with thrombospondin motifs 2

ADAMTS2 ;
PCINP ;
PCPNI ;
A disintegrin and metalloproteinase with thrombospondin motifs 2 ;
ADAM-TS 2 ;
ADAM-TS2 ;
ADAMTS-2 ;
Procollagen I N-proteinase ;
PC I-NP ;
Procollagen I/II amino propeptide-processing enzyme ;
Procollagen N-endopeptidase ;
pNPI

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 encoded preproprotein is proteolytically processed to generate the mature procollagen N-proteinase. This proteinase excises the N-propeptide of the fibrillar procollagens types I-III and type V. Mutations in this gene cause Ehlers-Danlos syndrome type VIIC, a recessively inherited connective-tissue disorder. Alternative splicing results in multiple transcript variants, at least one of which encodes an isoform that is proteolytically

Catalytic activity:Cleaves the N-propeptide of collagen chain alpha-1(I) at Pro-|-Gln and of alpha-1(II) and alpha-2(I) at Ala-|-Gln.,Caution:Has sometimes been referred to as ADAMTS3.,cofactor:Binds 1 zinc ion per subunit.,Disease:Defects in ADAMTS2 are the cause of Ehlers-Danlos syndrome type 7C (EDS7C) [MIM:225410]. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS7C is marked by extremely fragile tissues, hyperextensible skin and easy bruising. Facial skin contains numerous folds, as in the cutis laxa syndrome.,Domain:The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix.,Function:Cleaves the propeptides of type I and II collagen prior to fibril assembly. Does not act on type III collagen. May also play a role in development that is independent of its role in collagen biosynthesis.,PTM:The precursor is cleaved by a furin endopeptidase.,similarity:Contains 1 disintegrin domain.,similarity:Contains 1 peptidase M12B domain.,similarity:Contains 1 PLAC domain.,similarity:Contains 4 TSP type-1 domains.,subunit:May belong to a multimeric complex. Binds specifically to collagen type XIV.,tissue specificity:Expressed at high level in skin, bone, tendon and aorta and at low levels in thymus and brain.,

Secreted, extracellular space, extracellular matrix .

Expressed at high level in skin, bone, tendon and aorta and at low levels in thymus and brain.