免疫原
Synthesized peptide derived from human ATS15 AA range: 165-215
特异性
This antibody detects endogenous levels of ATS15 at Human/Mouse
来源
Polyclonal, Rabbit,IgG
组成(Formulation)
Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.207% sodium azide.
纯化工艺(Immunogen)
The antibody was affinity-purified from rabbit serum by affinity-chromatography using specific immunogen.
背景(Background)
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 encoded preproprotein is proteolytically processed to generate the mature enzyme, which may play a role in versican processing during skeletal muscle development. This gene may function as a tumor suppressor in colorectal and breast cancers. [provided by RefSeq, May 2016],
功能
cofactor:Binds 1 zinc ion per subunit.,domain: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.,domain:The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix.,PTM:The precursor is cleaved by a furin endopeptidase.,similarity:Contains 1 disintegrin domain.,similarity:Contains 1 peptidase M12B domain.,similarity:Contains 3 TSP type-1 domains.,tissue specificity:Expressed in fetal liver and kidney, but not in any of the adult tissues examined.,
其他名称
A disintegrin and metalloproteinase with thrombospondin motifs 15 (ADAM-TS 15) (ADAM-TS15) (ADAMTS-15) (EC 3.4.24.-)
细胞定位
Secreted, extracellular space, extracellular matrix . Cell surface .
组织表达
Expressed in fetal liver and kidney, but not in any of the adult tissues examined.