V-Myc Myelocytomatosis Viral Oncogene Homolog (Avian) (MYC) antibody

Antigen: V-Myc Myelocytomatosis Viral Oncogene Homolog (Avian) (MYC)

Synonyms: MRTL, c-Myc, bHLHe39, MYC, CMYC, MGC138120, c-myc, C-MYC, LOC100136746

Clonality: Monoclonal (9-00E-10)

Host: Mouse

Reactivity: Human

Conjugate: Un-conjugated

Application: Western Blotting (WB), Immunohistochemistry (Formalin-fixed Paraffin-embedded Sections) (IHC (ffpe)), Fluorescence Microscopy (FM), Immunoelectron Microscopy (IEM)

Catalog no.: ABIN967320

Additional Information

Alternative name: c-Myc

Immunogen: Human c-Myc Peptide

Components: 1) 51-1485GR: Purified Mouse Anti-Human c-Myc.
Quantity: 50 µg (3 ea).
Immunogen: Human c-Myc Peptide.
Isotype: Mouse IgG1.
Storage Buffer: Aqueous buffered solution containing BSA, glycerol, and Less or equal than 0.09% sodium azide.

2) 51-16526N: Jurkat Cell Lysate.
Quantity: 50 µg (1 ea).
Concentration: 1.0 mg/ml.
Storage Buffer: SDS-PAGE buffer (62mM Tris pH 6.8, 2% SDS, 0.9% b-mercaptoethanol, 0.003% bromophenol blue, 5% glycerol).

Format: Liquid

Isotype: IgG1

Clone: 9-00E-10

Description: The myc gene family contains at least seven closely related genes, c-myc, N-myc, L-myc, P-myc, R-myc, S-myc, and B-myc. C-myc plays a role in proliferation, transformation, and differentiation. It is expressed during embryonic development, in a wide variety of adult tissues, and is amplified in many tumors, particularly lung, breast, cervical and colon carcinomas. Cellular localization has been described as nuclear and/or cytopasmic. C-myc has three sequence motifs in the carboxy terminus, a leucine zipper, a helix-loop-helix, and a basic region. It forms sequence-specific (CACGTG) DNA binding heterodimers with max, a helixloop-helix/leucine zipper protein. Both the leucine zipper domain and the helixloop-helix motif of c-myc contribute to heterodimer formation. DNA binding of myc-max dimers results in a conformational change of the DNA and transcriptional activation. C-myc migrates at 62 kDa in SDS-PAGE. Clone 9E10 recognizes human c-myc. A synthetic peptide corresponding to a C-terminal epitope of the human c-myc protein (AEEQKLISEEDL) was used as an immunogen.

Characteristics: 1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
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. Source of all serum proteins is from USDA inspected abattoirs located in the United States.

Comments:

Related Products: ABIN968537, ABIN967389

Application Details

Application Notes: It is particularly useful for western blot analysis of myc-tagged recombinant proteins, and recombinant c-myc. Jurkat control lysate [50 µg (1 µg/µl)] is provided as a western blot positive control (store lysate at -20 °C). Additional control lysate is sold separately.

Concentration: 1.0 mg/ml

Purity: Purified

Purification: Purified from tissue culture supernatant or ascites by affinity chromatography.

Buffer: Aqueous buffered solution containing BSA, glycerol.

Preservative: 0.09% Sodium azide.

Storage: Store undiluted at -20°C.

Research Area: Cancer, Cell Cycle, Transcription Factors

Restrictions: For Research Use only

Images

Western blot analysis of c-myc. Lysate from Jurkat cells was probed with anti-c-myc (clone 9E10) at concentrations of 2.0 (lane 1), 1.0 (lane 2), and 0.5 µg/ml (lane 3). C-myc is identified as a band of 62 kDa.

Publications

Royds, Sharrard, Wagner et al.: "Cellular localisation of c-myc product in human colorectal epithelial neoplasia." in: The Journal of pathology, Vol. 166, Issue 3, pp. 225-33, 1992 (PubMed).

Campbell, Kessler, Fambrough: "The alternative carboxyl termini of avian cardiac and brain sarcoplasmic reticulum/endoplasmic reticulum Ca(2+)-ATPases are on opposite sides of the membrane." in: The Journal of biological chemistry, Vol. 267, Issue 13, pp. 9321-5, 1992 (PubMed).

Tosca, Linardopoulos, Malliri et al.: "Implication of the ras and myc oncoproteins in the pathogenesis of mycosis fungoides." in: Anticancer research, Vol. 11, Issue 4, pp. 1433-8, 1992 (PubMed).

DePinho, Schreiber-Agus, Alt: "myc family oncogenes in the development of normal and neoplastic cells." in: Advances in cancer research, Vol. 57, pp. 1-46, 1991 (PubMed).

Blackwood, Eisenman: "Max: a helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc." in: Science (New York, N.Y.), Vol. 251, Issue 4998, pp. 1211-7, 1991 (PubMed).

Gosney, Field, Gosney et al.: "c-myc oncoprotein in bronchial carcinoma: expression in all major morphological types." in: Anticancer research, Vol. 10, Issue 3, pp. 623-8, 1990 (PubMed).

Williams, Piris, Wyllie: "Immunohistochemical demonstration of altered intracellular localization of the C-Myc oncogene product in human colorectal neoplasms." in: The Journal of pathology, Vol. 160, Issue 4, pp. 287-93, 1990 (PubMed).

Karayiannis, Yiagnisis, Papadimitriou et al.: "Evaluation of the ras and myc oncoproteins in benign gastric lesions." in: Anticancer research, Vol. 10, Issue 5A, pp. 1127-33, 1990 (PubMed).

Tiniakos, Spandidos, Kakkanas et al.: "Expression of ras and myc oncogenes in human hepatocellular carcinoma and non-neoplastic liver tissues." in: Anticancer research, Vol. 9, Issue 3, pp. 715-21, 1989 (PubMed).

Spandidos, Yiagnisis, Papadimitriou et al.: "ras, c-myc and c-erbB-2 oncoproteins in human breast cancer." in: Anticancer research, Vol. 9, Issue 5, pp. 1385-93, 1990 (PubMed).

Evan, Lewis, Ramsay et al.: "Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product." in: Molecular and cellular biology, Vol. 5, Issue 12, pp. 3610-6, 1986 (PubMed).

Lukas, Parry, Aagaard et al.: "Retinoblastoma-protein-dependent cell-cycle inhibition by the tumour suppressor p16." in: Nature, Vol. 375, Issue 6531, pp. 503-6, 1995 (PubMed).

Liu, Hsu, Goeddel et al.: "Dissection of TNF receptor 1 effector functions: JNK activation is not linked to apoptosis while NF-kappaB activation prevents cell death." in: Cell, Vol. 87, Issue 3, pp. 565-76, 1996 (PubMed).