ELISA/assay

Hamster A Disintegrin and Metalloprotease 10 ELISA Kit

MBS031378

96 Strip Wells

600 USD

ELISA Kit

Hamster A Disintegrin and Metalloprotease 10 ELISA Kit

A Disintegrin and Metalloprotease 10

ADAM10; Disintegrin and metalloproteinase domain-containing protein 10; disintegrin and metalloproteinase domain-containing protein 10; CDw156; ADAM 10; kuzbanian protein homolog; mammalian disintegrin-metalloprotease; a disintegrin and metalloprotease domain 10; a disintegrin and metalloproteinase domain 10; ADAM metallopeptidase domain 10; CDw156; Kuzbanian protein homolog; Mammalian disintegrin-metalloprotease

ADAM10

ADAM10; ADAM10; kuz; AD10; MADM; CD156c; HsT18717; KUZ; MADM; ADAM 10

ADA10_HUMAN

Hamster

Store all reagents at 2-8 degree C

ELISA Type: Sandwich

2393947

AAC51766.1

O14672

84,142 Da

Activated NOTCH1 Transmits Signal To The Nucleus Pathway 576270!!Alzheimer's Disease Pathway 83097!!Alzheimer's Disease Pathway 509!!Alzheimers Disease Pathway 672448!!Constitutive Signaling By NOTCH1 HD Domain Mutants Pathway 771591!!Constitutive Signaling By NOTCH1 HD+PEST Domain Mutants Pathway 771595!!Constitutive Signaling By NOTCH1 PEST Domain Mutants Pathway 771593!!Constitutive Signaling By NOTCH1 T(7;9)(NOTCH1:M1580_K2555) Translocation Mutant Pathway 771589!!Degradation Of Collagen Pathway 730309!!Degradation Of The Extracellular Matrix Pathway 576263

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. [provided by RefSeq, Jul 2008]

Function: Cleaves the membrane-bound precursor of TNF-alpha at '76-Ala- -Val-77' to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface. 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 the proteolytic processing of Notch and mediates lateral inhibition during neurogenesis. Responsible for the FasL ectodomain shedding and for the generation of the remnant ADAM10-processed FasL (FasL APL) transmembrane form. Also cleaves the ectodomain of the integral membrane proteins CORIN and ITM2B. May regulate the EFNA5-EPHA3 signaling. Ref.4 Ref.5 Ref.7 Ref.8 Ref.10 Ref.11 Ref.14 Ref.16. Catalytic activity: Endopeptidase of broad specificity. Cofactor: Binds 1 zinc ion . By similarity. Subunit structure: Interacts with EPHA2 . By similarity. Forms a ternary EFNA5-EPHA3-ADAM10 complex mediating EFNA5 extracellular domain shedding by ADAM10 which regulates the EFNA5-EPHA3 complex internalization and function, the cleavage occurs in trans, with ADAM10 and its substrate being on the membranes of opposing cells. Ref.8. Subcellular location: Cell membrane; Single-pass type I membrane protein. Endomembrane system; Single-pass type I membrane protein. Note: Is localized in the plasma membrane but is predominantly expressed in the Golgi apparatus and in released membrane vesicles derived likely from the Golgi. Tissue specificity: Expressed in spleen, lymph node, thymus, peripheral blood leukocyte, bone marrow, cartilage, chondrocytes and fetal liver. Ref.3 Ref.6. Induction: In osteoarthritis affected-cartilage. 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.The Cys-rich region C-terminal to the disintegrin domain functions as a substrate-recognition module, it recognizes the EFNA5-EPHA3 Complex but not the individual proteins . By similarity. Post-translational modification: The precursor is cleaved by a furin endopeptidase . By similarity. Sequence similarities: Contains 1 disintegrin domain.Contains 1 peptidase M12B domain.

96 Strip Wells

600 USD