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Purified Mouse Anti-Eps8
Purified Mouse Anti-Eps8
Western blot analysis of Eps8 on a lysate from mouse macrophages (RAW 264.7) treated with 10 ng/mL IFNγ and 1 µg/mL LPS for 12 hours.  Lane 1:1:5000, lane 2: 1:10,000, lane 3: 1:20,000 dilution of the mouse anti-Eps8 antibody.
Purified Mouse Anti-Eps8

Immunofluorescence staining of rabbit cerebellum.

Western blot analysis of Eps8 on a lysate from mouse macrophages (RAW 264.7) treated with 10 ng/mL IFNγ and 1 µg/mL LPS for 12 hours.  Lane 1:1:5000, lane 2: 1:10,000, lane 3: 1:20,000 dilution of the mouse anti-Eps8 antibody.

Immunofluorescence staining of rabbit cerebellum.

Product Details
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BD Transduction Laboratories™
Mouse (QC Testing), Human, Rat, Dog (Tested in Development)
Mouse IgG1
Mouse Eps8 aa. 628-821
Western blot (Routinely Tested), Immunofluorescence, Immunohistochemistry, Immunoprecipitation (Tested During Development)
97 kDa
250 µg/ml
Aqueous buffered solution containing BSA, glycerol, and ≤0.09% sodium azide.

Preparation And Storage

Store undiluted at -20°C. The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography.

Recommended Assay Procedures

Western blot:  Please refer to

Product Notices

  1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
  2. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
  3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
  4. Please refer to for technical protocols.
Antibody Details
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The p97 [Eps8] protein, a substrate for EGF-R tyrosine kinase, contains an SH3 domain, but lacks a functional SH2 domain. Antibodies to Eps8 recognize the 97 kDa protein and a less abundant 68 kDa protein. Both forms are tyrosine-phosphorylated following treatment of cells with EGF. It is likely that p68 [Eps8] is synthesized from an alternatively spliced mRNA since two major Eps8-specific mRNAs are detected by Northern analysis. Co-immunoprecipitation studies have demonstrated a physical association between the Eps8 protein and the EGF-R both in vivo and in vitro. For many EGF-R substrates, this interaction is mediated through an SH2 domain of the substrate. Since Eps8 lacks a well defined SH2 domain and a fusion protein containing the SH2-like region of Eps8 could not bind EGF-R, the mechanism of Eps8-EGF-R association remains unclear. Overexpression of Eps8 in fibroblasts and hematopoietic cells results in an increased mitogenic response to EGF, suggesting that Eps8 has a role in the modulation of EGF-R function.

Format Details
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Tissue culture supernatant is purified by either protein A/G or affinity purification methods. Both methods yield antibody in solution that is free of most other soluble proteins, lipids, etc. This format provides pure antibody that is suitable for a number of downstream applications including: secondary labeling for flow cytometry or microscopy, ELISA, Western blot, etc.
Citations & References
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Development References (4)

  1. Burke P, Schooler K, Wiley HS. Regulation of epidermal growth factor receptor signaling by endocytosis and intracellular trafficking. Mol Cell Biol. 2001; 12(6):1897-1910. (Biology: Western blot). View Reference
  2. Fazioli F, Minichiello L, Matoska V. Eps8, a substrate for the epidermal growth factor receptor kinase, enhances EGF-dependent mitogenic signals. Science. 1993; 12(10):3799-3808. (Biology). View Reference
  3. Miyamoto S, Teramoto H, Gutkind JS, Yamada KM. Integrins can collaborate with growth factors for phosphorylation of receptor tyrosine kinases and MAP kinase activation: roles of integrin aggregation and occupancy of receptors. J Cell Biol. 1996; 135(6 pt 1):1633-1642. (Biology: Western blot). View Reference
  4. Xie QW, Cho HJ, Calaycay J, et al. Cloning and characterization of inducible nitric oxide synthase from mouse macrophages. Science. 1992; 256(5054):225-228. (Biology). View Reference
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Comparisons, where applicable, are made against older BD Technology, manual methods or are general performance claims.  Comparisons are not made against non-BD technologies, unless otherwise noted.

For Research Use Only. Not for use in diagnostic or therapeutic procedures.