Anti-ADAM15 (mouse), Cytoplasmic Domain Antibody

This rabbit IgG polyclonal antibody was generated against the GST-ADAM15-cytoplasmic tail and is specific for the cytoplasmic domain of mouse ADAM15.

The ADAM (A Disintegrin And Metalloprotease Domain) family is a unique group of proteins that has the ability to cleave or shed extracellular portions of transmembrane proteins. In addition, ADAMs are involved in cell-cell and cell-matrix interactions (e.g., fertilization, muscle development and neurogenesis).

ADAM15 (Metargidin) is a membrane-anchored metalloproteinase that has been implicated in pathological neovascularization and prostate cancer metastasis.

From the laboratory of Carl P. Blobel, MD, PhD, Hospital for Special Surgery.

The Investigator's Annexe Part of The Investigator's Annexe program.

Catalog Number Product Size AVAILABILITY Price Qty
EHS005
Anti-ADAM15 (mouse), Cytoplasmic Domain Antibody, 100uL
100uL In stock
Price: $299.00
Specifications
Product Type: Antibody
Accession ID: AF006196
Antigen: GST-ADAM15 cytoplasmic domain
Molecular Weight: ~100 kDa
Isotype: IgG
Clonality: Polyclonal
Reactivity: Mouse
Immunogen: GST-cyto corresponding to the cytoplasmic domain of mouse ADAM15
Species Immunized: Rabbit
Epitope: Cytoplasmic domain
Purification Method: Serum, not purified
Tested Applications: WB (1:500)
Storage: -80C
Shipped: Dry ice
Research
Antibody Species Reactivity Specificity
ADAM9 Human Cytoplasmic Domain
ADAM9 Mouse Cytoplasmic Domain
ADAM12 Mouse Cytoplasmic Domain
ADAM15 Human Cytoplasmic Domain
ADAM15 Mouse Cytoplasmic Domain
ADAM15 Human Extracellular Domain
ADAM15 Mouse Disintegrin Domain
ADAM17 Mouse Cytoplasmic Domain
ADAM17 Mouse Pro domain
ADAM19 Mouse Cytoplasmic Domain
ADAM28 Mouse Cytoplasmic Domain
ADAM28 Mouse Extracellular Domain
SNX9 Mouse Cytoplasmic Domain
Data

Western Blot Analysis

Western blot of reduced glycoproteins from the indicated tissues were probed with ADAM15 cytoplasmic domain antibody.

Adapted from: Lum L, et al. J. Biol Chem. 1998, 273, 26236-26247.

Provider
From the laboratory of Carl P. Blobel, MD, PhD, Hospital for Special Surgery.
References
  1. Lum L.; Reid, M. S.; Blobel, C. P. Intracellular maturation of the mouse metalloprotease disintegrin MDC15. J. Biol Chem. 1998, 273, 26236-26247.
  2. Horiuchi K, Weskamp G, Lum L, Hammes HP, Cai H, Brodie TA, Ludwig T, Chiusaroli R, Baron R, Preissner KT, Manova K, Blobel CP. Potential role for ADAM15 in pathological neovascularization in mice. Mol Cell Biol. 2003 Aug;23(16):5614-24.
  3. Maretzky T, Yang G, Ouerfelli O, Overall CM, Worpenberg S, Hassiepen U, Eder J, Blobel CP. Characterization of the catalytic activity of the membrane-anchored metalloproteinase ADAM15 in cell-based assays. Biochem J. 2009 Apr 28;420(1):105-13.
  4. Maretzky T, Le Gall SM, Worpenberg-Pietruk S, Eder J, Overall CM, Huang XY, Poghosyan Z, Edwards DR, Blobel CP. Src stimulates fibroblast growth factor receptor-2 shedding by an ADAM15 splice variant linked to breast cancer. Cancer Res. 2009 Jun 1;69(11):4573-6.

If you publish research with this product, please let us know so we can cite your paper.

 
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