Reactive species
Human;Rat;Mouse;
Antibody type
Polyclonal Antibody
Protein name
Disintegrin and metalloproteinase domain-containing protein 10
Immunogen
Synthesized peptide derived from ADAM10 . at AA range: 170-250
Specificity
ADAM10 Polyclonal Antibody detects endogenous levels of ADAM10 protein.
Constitute
Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Source
Polyclonal, Rabbit,IgG
Dilution rate
Western Blot: 1/500 - 1/2000. ELISA: 1/20000. Not yet tested in other applications.
Purification process
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
Other name
ADAM10; KUZ; MADM; Disintegrin and metalloproteinase domain-containing protein 10; ADAM 10; CDw156; Kuzbanian protein homolog; Mammalian disintegrin-metalloprotease; CD antigen CD156c
Background
ADAM metallopeptidase domain 10(ADAM10) Homo sapiens Members of the ADAM family are cell surface proteins with a unique structure possessing both potential adhesion and protease domains. This gene encodes and ADAM family member that cleaves many proteins including TNF-alpha and E-cadherin. Alternate splicing results in multiple transcript variants encoding different proteins that may undergo similar processing. [provided by RefSeq, Feb 2016],
Function
catalytic activity:Endopeptidase of broad specificity.,cofactor:Binds 1 zinc ion.,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.,function:Cleaves the membrane-bound precursor of TNF-alpha at '76-Ala-|-Val-77' to its mature soluble form. Responsible for the proteolytic release of several other cell-surface proteins, including heparin-binding epidermal growth-like factor, ephrin-A2 and for constitutive and regulated alpha-secretase cleavage of amyloid precursor protein (APP). Contributes to the normal cleavage of the cellular prion protein. Involved in the cleavage of the adhesion molecule L1 at the cell surface and in released membrane vesicles, suggesting a vesicle-based protease activity. Controls also
