ELISA/assay

Fish A Disintegrin and Metalloproteinase With Thrombospondin 1 ELISA Kit

MBS012901

96 Strip Wells

600 USD

ELISA Kit

Fish A Disintegrin and Metalloproteinase With Thrombospondin 1 ELISA Kit

A Disintegrin and Metalloproteinase With Thrombospondin 1

A disintegrin and metalloproteinase with thrombospondin motifs 15 preproprotein; A disintegrin and metalloproteinase with thrombospondin motifs 15; A disintegrin and metalloproteinase with thrombospondin motifs 15; ADAM-TS15; ADAMTS-15; ADAM-TS 15; metalloprotease disintegrin 15 with thrombospondin domains; a disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motif, 15, preproprotein; ADAM metallopeptidase with thrombospondin type 1 motif, 15

ADAMTS1

ADAMTS15; ADAMTS15; ADAM-TS 15; ADAM-TS15; ADAMTS-15

ATS15_HUMAN

Fish

950

Store all reagents at 2-8 degree C

ELISA Type: Sandwich

21265058

NP_620686.1

NM_139055.2

Q8TE58

103,287 Da

Metabolism Of Proteins Pathway 106230!!O-glycosylation Of TSR Domain-containing Proteins Pathway 980460!!O-linked Glycosylation Pathway 980459!!Post-translational Protein Modification Pathway 161012

This gene encodes a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) protein family. ADAMTS family members 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 protein encoded by this gene has a high sequence similarity to the proteins encoded by ADAMTS1 and ADAMTS8. [provided by RefSeq, Jul 2008]

Cofactor: Binds 1 zinc ion per subunit . By similarity. Subcellular location: Secreted extracellular space extracellular matrix . By similarity. Tissue specificity: Expressed in fetal liver and kidney, but not in any of the adult tissues examined. Domain: The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix . By similarity.The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. Post-translational modification: The precursor is cleaved by a furin endopeptidase . By similarity.Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Also can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion . By similarity. Sequence similarities: Contains 1 disintegrin domain.Contains 1 peptidase M12B domain.Contains 3 TSP type-1 domains.

96 Strip Wells

600 USD