Anti-ADAM9 (mouse), Cytoplasmic Domain Antibody
This rabbit IgG polyclonal antibody was generated against the GST-ADAM9-cytoplasmic tail and is specific for the cytoplasmic domain of mouse ADAM9.
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).
ADAM9 (MDC9, meltrin gamma) is widely expressed and catalytically active. ADAM9 is highly conserved in mouse and human (82% identical). ADAM9 contains the following domains: a signal sequence followed by a prodomain, a domain with sequence similarity to snake venom metalloproteases, a disintegrin domain, a cysteine-rich region, an EGF repeat, a membrane anchor and a cytoplasmic tail. The cytoplasmic tail of ADAM9 has two proline-rich sequences which can bind the SH3 domain of Src, and may therefore function as SH3 ligand domains. To clone the full-length cDNA for human ADAM9, a human cDNA library from mammary epithelial carcinoma cells were synthesized. For experiments involving ADAM9-reactive antibodies, the antibodies were raised against the GST-ADAM9-cytoplasmic tail.
From the laboratory of Carl P. Blobel, MD, PhD, Hospital for Special Surgery.
Part of The Investigator's Annexe program.
This rabbit IgG polyclonal antibody was generated against the GST-ADAM9-cytoplasmic tail and is specific for the cytoplasmic domain of mouse ADAM9.
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).
ADAM9 (MDC9, meltrin gamma) is widely expressed and catalytically active. ADAM9 is highly conserved in mouse and human (82% identical). ADAM9 contains the following domains: a signal sequence followed by a prodomain, a domain with sequence similarity to snake venom metalloproteases, a disintegrin domain, a cysteine-rich region, an EGF repeat, a membrane anchor and a cytoplasmic tail. The cytoplasmic tail of ADAM9 has two proline-rich sequences which can bind the SH3 domain of Src, and may therefore function as SH3 ligand domains. To clone the full-length cDNA for human ADAM9, a human cDNA library from mammary epithelial carcinoma cells were synthesized. For experiments involving ADAM9-reactive antibodies, the antibodies were raised against the GST-ADAM9-cytoplasmic tail.
From the laboratory of Carl P. Blobel, MD, PhD, Hospital for Special Surgery.
Part of The Investigator's Annexe program.
| Product Type: | Antibody |
| Antigen: | GST-ADAM9 cytoplasmic domain |
| Accession ID: | Q13443 |
| Molecular Weight: | ~84 kDa (mature form), ~115 kDa (pro-form) |
| Isotype: | IgG |
| Clonality: | Polyclonal |
| Reactivity: | Mouse |
| Immunogen: | GST-cyto corresponding to the cytoplasmic domain of mouse ADAM9 |
| Species Immunized: | Rabbit |
| Epitope: | Cytoplasmic domain |
| Purification Method: | Serum, not purified |
| Tested Applications: | WB (1:500) |
| Storage: | -80C |
| Shipped: | Dry ice |
| 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 |
Western Blot Analysis
Western blot of a separate sample of wild-type full-length MDC9 expressed in COS-7 separated on a 7.5% SDS-gel.
Adapted from: Roghani M, et al. J Biol Chem. 1999 Feb 5;274(6):3531-40.
- Weskamp G, Krätzschmar J, Reid MS, Blobel CP. MDC9, a widely expressed cellular disintegrin containing cytoplasmic SH3 ligand domains. J Cell Biol. 1996 Feb;132(4):717-26.
- Roghani M, Becherer JD, Moss ML, Atherton RE, Erdjument-Bromage H, Arribas J, Blackburn RK, Weskamp G, Tempst P, Blobel CP. Metalloprotease-disintegrin MDC9: intracellular maturation and catalytic activity. J Biol Chem. 1999 Feb 5;274(6):3531-40.
- Peduto L, Reuter VE, Shaffer DR, Scher HI, Blobel CP. Critical function for ADAM9 in mouse prostate cancer. Cancer Res. 2005 Oct 15;65(20):9312-9.
- Guaiquil V, Swendeman S, Yoshida T, Chavala S, Campochiaro PA, Blobel CP. ADAM9 is involved in pathological retinal neovascularization. Mol Cell Biol. 2009 May;29(10):2694-703.
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