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c-Myc DyLight® 488 (MYC) antibody RabMAb®

Cat.#: 4581-1

Rabbit Monoclonal Antibody


Clone ID: Y69
Swiss Prot: P01106
Mol Weight: 57kDa
Size: 100ul
Price: $275*
Availability: Ship next business day
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Description

Oncogene-encoded proteins c-Myc, N-Myc, and L-Myc function in cell proliferation, differentiation and neoplastic disease. Amplification of the c-Myc gene has been found in several types of human tumors, the N-Myc gene in neuroblastomas (1), and the L-Myc gene in human small cell lung carcinomas (2). c-Myc protein is a transcription factor localized to the nucleus of the cell. It seems to be involved in activating the transcription of growth-related genes. c-Myc binds to DNA during transcription as a heterodimeric complex with Max. c-Myc is phosphorylated in vitro by p44/42 MAP kinase at Ser62 (3) and in vivo at both Thr58 and Ser62. Mutation of Thr58 and Ser62 to Ala inhibits the ability of c-Myc to activate transcription (3).

Recommended Applications

ICC

Applications and Recommended Dilution Factors

ICC: 1:50 - 100

Species Reactivity

Human


Products Data

Immunofluorescent staining of HeLa cells using anti-c-Myc antibody conjugated with Dylight 488 (green, Cat# 4581-1) and Dapi (blue).

Specificity

A synthetic peptide corresponding to residues in N-terminus of human c-Myc was used as immunogen.

Storage Condition and Buffer

Store at 2-8° C. PBS (pH 7.2), 0.02% sodium azide, 0.05% BSA. Protect from light. Stable for 6 months from date of receipt.

Alternative Names

MYC antibody, MRTL antibody, bHLHe39 antibody, c-Myc antibody, Myc proto-oncogene protein antibody, Proto-oncogene c-Myc antibody, Transcription factor p64 antibody

Description References

1. Nisen, P.D. et al. Enhanced expression of the N-myc gene in Wilms’ tumors. Cancer Res. 46: 6217–6222 (1986).
2. Nau, M.N. et al. L-myc, a new myc-related gene amplified and expressed in human small cell lung cancer. Nature 318: 69–73 (1985).
3. Gupta, S. et al. Transactivation of Gene Expression by Myc is Inhibited by Mutation at the Phosphorylation Sites Thr-58 and Ser-62. Proc. Natl. Acad. Sci. USA 90: 3216–3220 (1993).

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