ELISA/assay

Goat A Disintegrin and Metalloprotease 11 ELISA Kit

MBS089245

96 Strip Wells

600 USD

ELISA Kit

Goat A Disintegrin and Metalloprotease 11 ELISA Kit

A Disintegrin and Metalloprotease 11

A disintegrin and metalloproteinase with thrombospondin motifs 5; A disintegrin and metalloproteinase with thrombospondin motifs 5; A disintegrin and metalloproteinase with thrombospondin motifs 5; aggrecanase-2; a disintegrin and metalloproteinase with thrombospondin motifs 11; a disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motif, 5 (aggrecanase-2); ADAM metallopeptidase with thrombospondin type 1 motif, 5; A disintegrin and metalloproteinase with thrombospondin motifs 11; ADAM-TS 11; ADAMTS-11; ADMP-2; Aggrecanase-2

ADAM11

ADAMTS5; ADAMTS5; ADMP-2; ADAM-TS5; ADAMTS-5; ADAMTS11; ADAM-TS 5; ADAMTS-11; ADAM-TS 11; ADAMTS11; ADMP2; ADAM-TS 5; ADAM-TS5; ADAMTS-5; ADAM-TS 11; ADAMTS-11

ATS5_HUMAN

Goat

930

Store all reagents at 2-8 degree C

317373326

Q9UNA0.2

Q9UNA0

101,718 Da

Degradation Of The Extracellular Matrix Pathway 576263!!Endochondral Ossification Pathway 198812!!Extracellular Matrix Organization Pathway 576262!!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. 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 contains two C-terminal TS motifs and functions as aggrecanase to cleave aggrecan, a major proteoglycan of cartilage. [provided by RefSeq, Jul 2008]

Function: Cleaves aggrecan, a cartilage proteoglycan, and may be involved in its turnover. May play an important role in the destruction of aggrecan in arthritic diseases. May play a role in proteolytic processing mostly during the peri-implantation period. Catalytic activity: Cleaves aggrecan at the 392-Glu- -Ala-393 site. Cofactor: Binds 1 zinc ion per subunit. Ref.6. Subcellular location: Secreted extracellular space extracellular matrix . By similarity. Tissue specificity: Expressed at low level in placenta primarily but also detected in heart and brain, cervix, uterus, bladder, esophagus, rib cartilage, chondroblastoma, fibrous tissue and a joint capsule from an arthritic patient. Domain: The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix.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.C- and O-glycosylated. 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 can mediate the efficient secretion of ADAMTS family members. 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. Ref.5 Ref.6Glycosylated. 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. Ref.5 Ref.6. Sequence similarities: Contains 1 disintegrin domain.Contains 1 peptidase M12B domain.Contains 2 TSP type-1 domains.

96 Strip Wells

600 USD