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Western blotAntibody data
- Antibody Data
- Antigen structure
- References [5]
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- Product number
- ABIN361939 - Provider product page
- Provider
- antibodies-online
- Proper citation
- Antibodies-Online Cat#ABIN361939, RRID:AB_10953105
- Product name
- anti-V-Myc Myelocytomatosis Viral Oncogene Homolog (Avian) (MYC) (pThr58) antibody
- Antibody type
- Polyclonal
- Antigen
- Peptide sequence around phosphorylation site of pThr58 (L-P-T (p) -P-P) derived from Human Myc. Antibodies were produced by immunizing rabbits with synthetic phosphopeptide and KLH conjugates.
- Description
- The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific phosphopeptide. The antibody against non-phosphopeptide was removed by chromatography using non-phosphopeptide corresponding to the phosphorylation site.
- Reactivity
- Human, Mouse, Rat
- Host
- Rabbit
- Epitope
- pThr58
- Isotype
- IgG
- Vial size
- 50 μL
- Concentration
- 1 mg/mL
- Storage
- Store at -20°C for long term preservation (recommended). Store at 4°C for short term use.
Submitted references Tobacco-specific nitrosamine 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone promotes functional cooperation of Bcl2 and c-Myc through phosphorylation in regulating cell survival and proliferation.
The Fbw7 tumor suppressor regulates glycogen synthase kinase 3 phosphorylation-dependent c-Myc protein degradation.
The Max network gone mad.
Proteins of the Myc network: essential regulators of cell growth and differentiation.
Max: a helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc.
Jin Z, Gao F, Flagg T, Deng X
The Journal of biological chemistry 2004 Sep 17;279(38):40209-19
The Journal of biological chemistry 2004 Sep 17;279(38):40209-19
The Fbw7 tumor suppressor regulates glycogen synthase kinase 3 phosphorylation-dependent c-Myc protein degradation.
Welcker M, Orian A, Jin J, Grim JE, Harper JW, Eisenman RN, Clurman BE
Proceedings of the National Academy of Sciences of the United States of America 2004 Jun 15;101(24):9085-90
Proceedings of the National Academy of Sciences of the United States of America 2004 Jun 15;101(24):9085-90
The Max network gone mad.
Baudino TA, Cleveland JL
Molecular and cellular biology 2001 Feb;21(3):691-702
Molecular and cellular biology 2001 Feb;21(3):691-702
Proteins of the Myc network: essential regulators of cell growth and differentiation.
Henriksson M, Lüscher B
Advances in cancer research 1996;68:109-82
Advances in cancer research 1996;68:109-82
Max: a helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc.
Blackwood EM, Eisenman RN
Science (New York, N.Y.) 1991 Mar 8;251(4998):1211-7
Science (New York, N.Y.) 1991 Mar 8;251(4998):1211-7
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