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Each lot of this antibody is quality control tested by Western blotting. For Western blotting, suggested working dilution(s): Use 5 μg per 5 ml antibody dilution buffer for each mini-gel. It is recommended that the reagent be titrated for optimal performance for each application.
COA:
Application Notes:
Additional reported applications (for the relevant formats) include: immunohistochemistry5 of formalin-fixed, paraffin-embedded tissue sections, ELISA1, immunofluorescence microscopy3,4, immunoprecipitation4, and immunoaffinity of c-myc-tagged fusion proteins6.
Application References:
1. Schouten A, et al. 2002. J. Biol. Chem. 277:19339. (ELISA) 2. Maher SE, et al. 1998. Transplantation 66:1094. 3. Raftopoulou M, et al. 2004. Science 303:1179. (IF) 4. Fan H, et al. 1998. Biochem. Cell. Biol. 76:125. (IF IP) 5. Korkolopoulou P, et al. 1994. Leuk Lymphoma 13:151. (IHC) 6. Hillman MC, et al. 2001. Protein Expr. Purif. 23:359. 7. Kondo, S., et al. 2011. J. Virol. 85:11255. PubMed.
Jurkat extract was resolved by electrophoresis, transferred to nitrocellulose and probed with anti-c-myc monoclonal antibody. Proteins were visualized using a goat anti-mouse secondary conjugated to HRP and a chemiluminescence detection system. Intact (non-degraded) c-myc with a molecular weight of approximately 62 kD is detected in this Western blot experiment.
The c-myc protein is a 62 kD nuclear factor that is ubiquitously expressed in the nucleus. c-myc is part of a heterodimeric complex with MAX that acts as a potent transcriptional activator. c-myc is modified by glycosylation and phosphorylation and has been shown to interact with a number of proteins including SMAD2, SMAD3, Pam, cdc6, BRCA1, Mlh1, p34cdc2, MAD, and Sp1. c-myc is extremely labile and is degraded very quickly even in extracts prepared with boiling SDS sample buffer, such that the observed protein size is approximately 41 kD. The 9E10 monoclonal antibody recognizes human myc and the 10 amino acid epitope tag of human c-myc. The 9E10 antibody has been shown to be useful in a number of applications including Western blotting, direct ELISA, flow cytometry, immunoprecipitation, immunofluorescence, immunohistochemistry (paraffin), and immunoaffinity purification of proteins expressing the human c-myc tag.
Other Names:
Oncogene Myc, Myc proto-oncogene protein
Structure:
Highly conserved protein structure Drosophila to vertebrates. Contains HLH domain, coiled coil region, and leucine zipper domain, molecular weight approximately 62 kD
Distribution:
Ubiquitously expressed nuclear protein
Function:
Transcription factor, binds to DNA and activates transcription as part of a heterodimeric complex MAX. Structural rearrangements found in a number of cancers
MAX, SMAD2, SMAD3, Pam, cdc6, BRCA1, Mlh1, p34cdc2, MAD, Sp1, and many other proteins
Antigen References:
1. Adams JM, et al. 1983. Proc. Natl. Acad. Sci. USA 80:1982. 2. Atchley WR, et al. 1995. Proc. Natl. Acad. Sci. USA 92:10217. 3. Battey J, et al. 1983. Cell 34:779. 4. Beimling P, et al. 1985. Biochemistry 24:6349.
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This data display is provided for general comparisons between formats. Your actual data may vary due to variations in samples, target cells, instruments and their settings, staining conditions, and other factors. If you need assistance with selecting the best format contact our expert technical support team.
Purified anti-c-Myc
Jurkat extract was resolved by electrophoresis, transferred to nitrocellulose and probed with anti-c-myc monoclonal antibody. Proteins were visualized using a goat anti-mouse secondary conjugated to HRP and a chemiluminescence detection system. Intact (non-degraded) c-myc with a molecular weight of approximately 62 kD is detected in this Western blot experiment.
