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Rabbit anti-Human ADAM15 Polyclonal Antibody

The antibody against ADAM15 was raised in rabbit using the Recombinant Human Disintegrin and metalloproteinase domain-containing protein 15 protein (207-452AA) as the immunogen. This antibody exists as a non-conjugated isotype IgG, purified by protein G with a purity greater than 95%. This antibody has been validated on ELISA, IHC.

ADC-50842A

The antibody against ADAM15 was raised in rabbit using the Recombinant Human Disintegrin and metalloproteinase domain-containing protein 15 protein (207-452AA) as the immunogen. This antibody exists as a non-conjugated isotype IgG, purified by protein G with a purity greater than 95%. This antibody has been validated on ELISA, IHC.

$299.00

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Specifications


Cat.No ADC-50842A ClonalityPolyclonal
Host SpeciesRabbitTarget NameADAM15
FormLiquidSpecies ReactivityHuman
IsotypeIgGStorage Buffer0.01M PBS, 0.03% Proclin 300; Constituents: 50% Glycerol, PH 7.4
Purification Method>95%, Protein G purifiedConjugateNon-conjugated
ApplicationELISA, IHCStorageUpon receipt

Immunogen Information


Immunogen DescriptionRecombinant Human Disintegrin and metalloproteinase domain-containing protein 15 protein (207-452AA)Target SpeciesHuman
Immunogen SequenceComplete sequences for the immunogen, target protein, and peptides are available upon request.Uniprot IDQ13444
Background Information
  • Uniprot Id

    Q13444

  • Target Species

    Human

  • Target Name

    ADAM15

  • Target Full Name

    Disintegrin and metalloproteinase domain-containing protein 15

  • Target Function

    Active metalloproteinase with gelatinolytic and collagenolytic activity. Plays a role in the wound healing process. Mediates both heterotypic intraepithelial cell/T-cell interactions and homotypic T-cell aggregation. Inhibits beta-1 integrin-mediated cell adhesion and migration of airway smooth muscle cells. Suppresses cell motility on or towards fibronectin possibly by driving alpha-v/beta-1 integrin (ITAGV-ITGB1) cell surface expression via ERK1/2 inactivation. Cleaves E-cadherin in response to growth factor deprivation. Plays a role in glomerular cell migration. Plays a role in pathological neovascularization. May play a role in cartilage remodeling. May be proteolytically processed, during sperm epididymal maturation and the acrosome reaction. May play a role in sperm-egg binding through its disintegrin domain.

  • Target Subcellular Location

    Endomembrane system; Single-pass type I membrane protein. Cell junction, adherens junction. Cell projection, cilium, flagellum. Cytoplasmic vesicle, secretory vesicle, acrosome.

  • Target Tissue Specificity

    Expressed in colon and small intestine. Expressed in airway smooth muscle and glomerular mesangial cells (at protein level). Ubiquitously expressed. Overexpressed in atherosclerotic lesions. Constitutively expressed in cultured endothelium and smooth musc

  • Target Research Area

    Cancer

  • Target Synonyms

    A disintegrin and metalloproteinase domain 15 (metargidin); A disintegrin and metalloproteinase domain 15; ADA15_HUMAN; ADAM 15; ADAM metallopeptidase domain 15; Adam15; and cysteine-rich protein 15; Disintegrin and metalloproteinase domain-containing protein 15; disintegrin-like; EC 3.4.24.; MDC 15; MDC-15; MDC15; Metalloprotease RGD disintegrin protein; Metalloproteinase like disintegrin like and cysteine rich protein 15; Metalloproteinase-like; Metargidin

  • Target Background

    The protein encoded by this gene is a member of the ADAM (a disintegrin and metalloproteinase) protein family. ADAM family members are type I transmembrane glycoproteins known to be involved in cell adhesion and proteolytic ectodomain processing of cytokines and adhesion molecules. This protein contains multiple functional domains including a zinc-binding metalloprotease domain, a disintegrin-like domain, as well as a EGF-like domain. Through its disintegrin-like domain, this protein specifically interacts with the integrin beta chain, beta 3. It also interacts with Src family protein-tyrosine kinases in a phosphorylation-dependent manner, suggesting that this protein may function in cell-cell adhesion as well as in cellular signaling. Multiple alternatively spliced transcript variants encoding distinct isoforms have been observed.

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