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anti-ADAM10 antibody :: Rabbit ADAM 10 (kuz) (TNFa converting enzyme) Polyclonal Antibody

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Catalog # MBS395858
Unit / Price
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  0.1 mg  /  $510 +1 FREE 8GB USB
Western Blot/Blotting
Product Name

ADAM 10 (kuz) (TNFa converting enzyme) (ADAM10), Polyclonal Antibody

Full Product Name

ADAM 10 (CT) (kuz) (TNFa converting enzyme)

Product Synonym Names
Research Use Only
For Research Use Only. Not for use in diagnostic procedures.
Chromosome Location
Chromosome: 15; NC_000015.9 (58888510..59042177, complement). Location: 15q22
3D Structure
ModBase 3D Structure for O14672
Species Reactivity
Human, Mouse, Rat
Antigen Immunoaffiinity Purification
Provided in phosphate buffered saline solution containing 0.02% sodium azide as a preservative
Synthetic peptide corresponding to amino acids 732 to 748 off the human ADAM10. Immungen sequence is identical in bovine and rat and differs from the mouse protein by one amino acid.
Positive Control
Jurkat whole cell lysate
Preparation and Storage
Product should be stored at -20 degree C. Aliquot to avoid freeze/thaw cycles
Other Notes
Small volumes of anti-ADAM10 antibody vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.
Related Product Information for
anti-ADAM10 antibody
Proinflammatory cytokine tumor necrosis factor- (TNF-) contributes to a variety of inflammatory responses and programmed cell death. Notch receptor and its ligand participate in cell fate decisions during vertebrate development and are associated with several human disorders, including a T-cell lymphoma. TNF-, notch and its ligand delta are all membrane-bond molecules, which are cleaved by proteases to release mature proteins or functional receptor. ADAM10, a metalloprotease-disintegrin in the family of mammalian ADAM (for a disintegrin and metalloprotease), was recently identified to cleave TNF-, notch and its ligand delta (1-3). The genes encoding human, mouse, and bovine ADAM10 were recently cloned and designated ADAM 10, kuzbanian (KUZ), and MADM, respectively, (1,2,4). ADAM10 mRNA is expressed in a variety of human and bovine tissues (1,4).
Applications Tested/Suitable for anti-ADAM10 antibody
Western Blot (WB)

Western Blot/Blotting of anti-ADAM10 antibody
Western blot analysis
anti-ADAM10 antibody Western Blot/Blotting (WB) image
NCBI/Uniprot data below describe general gene information for ADAM10. It may not necessarily be applicable to this product.
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Primary Accession #
UniProt Secondary Accession #
UniProt Related Accession #
Molecular Weight
85 kDa
NCBI Official Full Name
disintegrin and metalloproteinase domain-containing protein 10
NCBI Official Synonym Full Names
ADAM metallopeptidase domain 10
NCBI Official Symbol
ADAM10  [Similar Products]
NCBI Official Synonym Symbols
kuz; AD10; MADM; CD156c; HsT18717
  [Similar Products]
NCBI Protein Information
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
UniProt Protein Name
Disintegrin and metalloproteinase domain-containing protein 10
UniProt Synonym Protein Names
CDw156; Kuzbanian protein homolog; Mammalian disintegrin-metalloprotease
UniProt Gene Name
ADAM10  [Similar Products]
UniProt Synonym Gene Names
KUZ; MADM; ADAM 10  [Similar Products]
UniProt Entry Name
NCBI Summary for ADAM10
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]
UniProt Comments for ADAM10
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.
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