N-Myc Antibody

9405:

Immunoprecipitation , Western Blotting

N-Myc Antibody detects endogenous levels human N-Myc and transfected levels of mouse N-Myc. It does not cross-react with other Myc family members.

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding lysine 351 of human N-Myc. Antibodies were purified by protein A and peptide affinity chromatography.

Western Blotting

Western blot analysis of extracts from the IMR-32 neuroblastoma cell line, using N-Myc Antibody.

Western Blotting

Western blot analysis of extracts from HeLa cells either mock transfected or transfected with murine N-Myc, using N-Myc Antibody.

Members of the Myc/Max/Mad network function as transcriptional regulators with roles in various aspects of cell behavior including proliferation, differentiation and apoptosis (1). These proteins share a common basic-helix-loop-helix leucine zipper (bHLH-ZIP) motif required for dimerization and DNA-binding. Max was originally discovered based on its ability to associate with c-Myc and found to be required for the ability of Myc to bind DNA and activate transcription (2). Subsequently, Max has been viewed as a central component of the transcriptional network, forming homodimers as well as heterodimers with other members of the Myc and Mad families (1). The association between Max and either Myc or Mad can have opposing effects on transcriptional regulation and cell behavior (1). The Mad family consists of four related proteins; Mad1, Mad2 (Mxi1), Mad3 and Mad4, and the more distantly related members of the bHLH-ZIP family, Mnt and Mga. Like Myc, the Mad proteins are tightly regulated with short half-lives. In general, Mad family members interfere with Myc-mediated processes such as proliferation, transformation and prevention of apoptosis by inhibiting transcription (3,4).

In humans the Myc family consists of 5 genes: c-Myc, N-Myc, L-Myc, R-Myc, and B-Myc. While c-Myc is expressed in many proliferating cells, N-Myc expression is very restricted, with highest levels in during embryonic development and then in the adult during B-cell development. These expression patterns and results from targeted deletion of N-Myc suggest that N-Myc plays an important role in tissue development and differentiation (5). In addition, amplification or overexpression of N-Myc has been found in human neuroblastomas and is associated with rapid progression and poor prognosis (6,7).

1. Baudino, T.A. and Cleveland, J.L. (2001) Mol. Cell. Biol. 21, 691-702.
2. Blackwood, E.M. and Eisenman, R.N. (1991) Science 251, 1211-1217.
3. Henriksson, M. and Lüscher, B. (1996) Adv. Cancer Res. 68, 109-182.
4. Grandori, C. et al. (2000) Annu. Rev. Cell Dev. Biol. 16, 653-699.
5. Sawai, S. et al. (1993) Development 117, 1445-1455.
6. Schwab, M. et al. (1984) Proc. Natl. Acad. Sci. USA 81, 4940-4944.
7. Brodeur, G.M. et al. (1984) Science 224, 1121-1124.

• Popkie, A.P. et al. (2010) J Biol Chem 285, 41337-47. Applications: Western Blotting

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• 5605 c-Myc (D84C12) XP^® Rabbit mAb
• 4739 Max (S20) Antibody
• 4682 Mad-1 Antibody
• 7071 Phototope^® -HRP Western Blot Detection System, Anti-rabbit IgG, HRP-linked Antibody
• 7074 Anti-rabbit IgG, HRP-linked Antibody
• 7720 Prestained Protein Marker, Broad Range (Premixed Format)
• 7727 Biotinylated Protein Ladder Detection Pack
• 7003 20X LumiGLO^® Reagent and 20X Peroxide

For Research Use Only. Not For Use In Diagnostic Procedures.