Sony Biotechnology Inc. Sony Biotechnology Inc.cart
About Us Products What's New Library News Calendar Contact Us Place Order
Safety Data Sheet (SDS) Purified Anti-c-Myc Antibody     Product Data Sheet (PDF)    
Purified Anti-c-Myc Antibody
3734005 25 µg $90.00       
3734010 100 µg $180.00       
Clone: 9E10
Isotype: Mouse IgG1, κ
Reactivity: Human and fusion protein (EQKLISEEDL tag epitope) in all species
Immunogen: Amino acids 408-439, C-terminal region of human c-myc
Formulation: This antibody is provided in phosphate-buffered solution, pH 7.2, containing 0.09% sodium azide at 0.5 mg/ml.
Preparation: The antibody was purified by affinity chromatography.
Concentration: 0.5 mg/ml
Storage & Handling: Upon receipt, store undiluted between 2°C and 8°C.

WB - Quality tested
ELISA, IF, IP, IHC - Reported in the literature

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.

Recommended Usage:

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.

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
8. Decarpentrie F, et al. 2012. Hum Mol Genet. PubMed
9. Bourgeois-Daigneault MC, et al. 2012. J Immunol. 188:4959. PubMed
10. Peters BM, et al. 2012. Microbiology. 158:2975. PubMed
11. Robu M, et al. 2013. PNAS. 110:1658.  PubMed
12. Eilert E, et al. 2013. J Biotechnol. 167:85. PubMed
13. Bi J, et al. 2013. Am J Physiol Renal Physiol. 305:532. PubMed
14. Poe JC, et al. 2013. J exp Med. 511:57. PubMed
15. Shkoporov AN, et al. 2015. FEMS Microbial Lett. 362:83. PubMed

Total cell lysates (15 µg

Total cell lysates (15 µg protein) from HeLa, Jurkat, and Raw264.7 were resolved by 4-12% Bis-tris gel electrophoresis, transferred to nitrocellulose, and probed with purified anti-c-Myc antibody (clone 9E10). Proteins were visualized using a goat anti-mouse IgG secondary antibody conjugated to HRP and chemiluminescence detection. GAPDH antibody was used as a loading control.


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
Modification: Glycosylation, Phosphorylation (Thr58, Ser62, Ser71)
Interaction: 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.