Anti-Phospho-c-Myc (T58 + S62) Antibody [SZ02-06]

HUABIO

Anti-Phospho-c-Myc (T58 + S62) Antibody [SZ02-06]

7

Flow Cytometry, ImmunoPrecipitation, Western Blot

WB,IP,FC

Research Use Only

Monoclonal

SZ02-06

1 mg/ml

Unconjugated

MYC

MYC proto-oncogene, bHLH transcription factor

MRTL, MYCC, bHLHe39, c-Myc, myc proto-oncogene protein, avian myelocytomatosis viral oncogene homolog, class E basic helix-loop-helix protein 39, myc-related translation/localization regulatory factor, proto-oncogene c-Myc, transcription factor p64, v-myc avian myelocytomatosis viral oncogene homolog, v-myc myelocytomatosis viral oncogene homolog

Rabbit

IgG

Myc proto-oncogene protein

c-Myc-, N-Myc- and L-Myc-encoded proteins function in cell proliferation, differentiation and neoplastic disease. Myc proteins are nuclear proteins with relatively short half lives. Amplification of the c-Myc gene has been found in several types of human tumors including lung, breast and colon carcinomas, while the N-Myc gene has been found amplified in neuroblastomas. The L-Myc gene has been reported to be amplified and expressed at high level in human small cell lung carcinomas. The presence of three sequence motifs in the c-Myc COOH terminus, including the leucine zipper, the helix-loop-helix and a basic region provided initial evidence for a sequence-specific binding function. A basic region helix-loop-helix leucine zipper motif (bHLH-Zip) protein, designated Max, specifically associates with c-Myc, N-Myc and L-Myc proteins. The Myc-Max complex binds to DNA in a sequence-specific manner under conditions where neither Max nor Myc exhibit appreciable binding. Max can also form heterodimers with at least two additional bHLH-Zip proteins, Mad and Mxi1, and Mad-Max dimers have been shown to repress transcription through interaction with mSin3.

Human

Human

Rat

-20°C,2°C to 8°C

41116161