protein

Recombinant Human A Disintegrin and Metalloproteinase Domain 10

MBS143712

0.002 mg

140 USD

Recombinant Protein

Recombinant Human A Disintegrin and Metalloproteinase Domain 10

A Disintegrin and Metalloproteinase Domain 10

ADAM10 Human; A Disintegrin and Metalloproteinase Domain 10 Human Recombinant; Kuz; AD10; MADM; CD156c; HsT18717; ADAM metallopeptidase domain 10; A disintegrin and metalloproteinase domain 10; Mammalian disintegrin-metalloprotease; Kuzbanian protein homolog; CDw156; ADAM 10; ADAM10

disintegrin and metalloproteinase domain-containing protein 10; Disintegrin and metalloproteinase domain-containing protein 10; disintegrin and metalloproteinase domain-containing protein 10; CDw156; a disintegrin and metalloprotease domain 10; kuzbanian protein homolog; mammalian disintegrin-metalloprotease; ADAM metallopeptidase domain 10; CDw156; Kuzbanian protein homolog; Mammalian disintegrin-metalloprotease; CD_antigen: CD156c

ADAM10

ADAM10; ADAM10; RAK; kuz; AD10; AD18; MADM; CD156c; HsT18717; KUZ; MADM; ADAM 10

ADA10_HUMAN

E Coli

748

Greater than 95.0% as determined by SDS-PAGE.

The ADAM10 solution contains 20mM Tris (pH 8), 1mM EDTA and 50% Glycerol. Sterile Filtered colorless solution.

RECOMBINANT & NATURAL PROTEINS; Recombinant Proteins; A Disintegrin and Metalloproteinase Domain

Description: ADAM10 extracellular domain minus the signal peptide and pro-sequence Human Recombinant fused to N-terminal His-Tag produced in E Coli is a single, non-glycosylated polypeptide chain containing 459 amino acids (214-672) and having a molecular mass of 55.089kDa. Introduction: ADAM10 is part of the ADAM family which are cell surface proteins with a distinctive structure possessing both potential adhesion and protease domains. ADAM10 cleaves many proteins including TNF-alpha and E-cadherin. ADAM10 cleaves the membrane-bound precursor of tnf-alpha at 76- ala- -val-77 to its mature soluble form. ADAM10 is in charge 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 ADAM10 is involved in the normal cleavage of the cellular prion protein. ADAM10 is involved in the cleavage of the adhesion molecule l1 at the cell surface and in the release of membrane vesicles, suggesting a vesicle-based protease activity. ADAM10 controls the proteolytic processing of notch and mediates lateral inhibition during neurogenesis.

4557251

NP_001101.1

NM_001110.3

O14672

49,047 Da

Activated NOTCH1 Transmits Signal To The Nucleus Pathway (576270); Alzheimer's Disease Pathway (83097); Alzheimer's Disease Pathway (509); Alzheimers Disease Pathway (672448); Axon Guidance Pathway (105688); Collagen Degradation Pathway (730309); 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)

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]

ADAM10: 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. Protein type: Membrane protein, integral; Cell adhesion; Protease; Motility/polarity/chemotaxis; Vesicle; EC 3.4.24.81; Cell surface. Chromosomal Location of Human Ortholog: 15q22. Cellular Component: Golgi apparatus; cell surface; focal adhesion; membrane; intracellular membrane-bound organelle; cytoplasm; postsynaptic density; integral to membrane; plasma membrane; Golgi-associated vesicle; nucleus. Molecular Function: integrin binding; protein binding; protein homodimerization activity; zinc ion binding; metallopeptidase activity; metalloendopeptidase activity; endopeptidase activity; SH3 domain binding; protein kinase binding; receptor binding. Biological Process: integrin-mediated signaling pathway; epidermal growth factor receptor signaling pathway; axon guidance; extracellular matrix organization and biogenesis; Notch signaling pathway; in utero embryonic development; membrane protein ectodomain proteolysis; constitutive protein ectodomain proteolysis; Notch receptor processing; negative regulation of cell adhesion; positive regulation of cell growth; protein amino acid phosphorylation; collagen catabolic process; extracellular matrix disassembly; PMA-inducible membrane protein ectodomain proteolysis; monocyte activation; cell-cell signaling; positive regulation of cell proliferation; ephrin receptor signaling pathway; positive regulation of cell migration. Disease: Reticulate Acropigmentation Of Kitamura; Alzheimer Disease 18

0.002 mg

140 USD

0.01 mg

205

1 mg

4630