AFfirm™ c-Myc Mouse Monoclonal Antibody - #BF8921
Product Info
*The optimal dilutions should be determined by the end user.
*Tips:
WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.
Fold/Unfold
AU016757; Avian myelocytomatosis viral oncogene homolog; bHLHe39; c Myc; Class E basic helix-loop-helix protein 39; MRTL; Myc; Myc protein; Myc proto oncogene protein; Myc proto-oncogene protein; myc-related translation/localization regulatory factor; MYC_HUMAN; Myc2; MYCC; Myelocytomatosis oncogene; Niard; Nird; Oncogene Myc; OTTHUMP00000158589; Proto-oncogene c-Myc; Protooncogene homologous to myelocytomatosis virus; RNCMYC; Transcription factor p64; Transcriptional regulator Myc-A; V-Myc avian myelocytomatosis viral oncogene homolog; v-myc myelocytomatosis viral oncogene homolog (avian);
Immunogens
- P01106 MYC_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSGSPNPARGHSVCSTSSLYLQDLSAAASECIDPSVVFPYPLNDSSSPKSCASQDSSAFSPSSDSLLSSTESSPQGSPEPLVLHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQAPGKRSESGSPSAGGHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRVKLDSVRVLRQISNNRKCTSPRSSDTEENVKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSVQAEEQKLISEEDLLRKRREQLKHKLEQLRNSCA
PTMs - P01106 As Substrate
Site | PTM Type | Enzyme | Source |
---|---|---|---|
Ubiquitination | Uniprot | ||
S6 | Phosphorylation | Uniprot | |
T8 | Phosphorylation | P04049 (RAF1) | Uniprot |
Y12 | Phosphorylation | Uniprot | |
Y16 | Phosphorylation | Uniprot | |
Y22 | Phosphorylation | Uniprot | |
Y32 | Phosphorylation | P00519 (ABL1) | Uniprot |
K51 | Sumoylation | Uniprot | |
K51 | Ubiquitination | Uniprot | |
K52 | Sumoylation | Uniprot | |
K52 | Ubiquitination | Uniprot | |
T58 | O-Glycosylation | Uniprot | |
T58 | Phosphorylation | P49841 (GSK3B) , P28482 (MAPK1) , P49840 (GSK3A) , P53779 (MAPK10) , P45983 (MAPK8) | Uniprot |
S62 | Phosphorylation | Q13627 (DYRK1A) , P45984 (MAPK9) , Q00535 (CDK5) , P28482 (MAPK1) , P45983 (MAPK8) , Q92630 (DYRK2) , P53779 (MAPK10) , P42345 (MTOR) | Uniprot |
S64 | Phosphorylation | Uniprot | |
S67 | Phosphorylation | Uniprot | |
S71 | Phosphorylation | P28482 (MAPK1) , P45984 (MAPK9) , P53779 (MAPK10) , P45983 (MAPK8) | Uniprot |
Y74 | Phosphorylation | P00519 (ABL1) | Uniprot |
T78 | Phosphorylation | Uniprot | |
S81 | Phosphorylation | Uniprot | |
K143 | Acetylation | Uniprot | |
K148 | Acetylation | Uniprot | |
K148 | Sumoylation | Uniprot | |
K148 | Ubiquitination | Uniprot | |
S151 | Phosphorylation | Uniprot | |
K157 | Acetylation | Uniprot | |
K157 | Sumoylation | Uniprot | |
K157 | Ubiquitination | Uniprot | |
S161 | Phosphorylation | Uniprot | |
T244 | Phosphorylation | Uniprot | |
S249 | Phosphorylation | P68400 (CSNK2A1) | Uniprot |
S250 | Phosphorylation | P68400 (CSNK2A1) | Uniprot |
S252 | Phosphorylation | P68400 (CSNK2A1) , P48729 (CSNK1A1) | Uniprot |
K275 | Acetylation | Uniprot | |
S277 | Phosphorylation | Uniprot | |
S279 | Phosphorylation | Uniprot | |
S281 | Phosphorylation | Uniprot | |
S288 | Phosphorylation | Uniprot | |
K289 | Ubiquitination | Uniprot | |
S293 | Phosphorylation | Uniprot | |
K298 | Ubiquitination | Uniprot | |
K317 | Acetylation | Uniprot | |
K317 | Sumoylation | Uniprot | |
K323 | Acetylation | Uniprot | |
K323 | Sumoylation | Uniprot | |
K323 | Ubiquitination | Uniprot | |
K326 | Sumoylation | Uniprot | |
K326 | Ubiquitination | Uniprot | |
S329 | Phosphorylation | P11309 (PIM1) , Q9P1W9 (PIM2) | Uniprot |
S337 | Phosphorylation | Uniprot | |
T343 | Phosphorylation | Uniprot | |
S344 | Phosphorylation | Uniprot | |
S347 | Phosphorylation | P68400 (CSNK2A1) | Uniprot |
S348 | Phosphorylation | P68400 (CSNK2A1) | Uniprot |
T350 | Phosphorylation | Uniprot | |
K355 | Sumoylation | Uniprot | |
K355 | Ubiquitination | Uniprot | |
T358 | Phosphorylation | Q13177 (PAK2) | Uniprot |
K371 | Acetylation | Uniprot | |
S373 | Phosphorylation | Q13177 (PAK2) | Uniprot |
K389 | Sumoylation | Uniprot | |
K389 | Ubiquitination | Uniprot | |
K392 | Sumoylation | Uniprot | |
K392 | Ubiquitination | Uniprot | |
K398 | Sumoylation | Uniprot | |
K398 | Ubiquitination | Uniprot | |
T400 | Phosphorylation | Q13177 (PAK2) | Uniprot |
S405 | Phosphorylation | Uniprot | |
K412 | Sumoylation | Uniprot | |
K412 | Ubiquitination | Uniprot | |
K422 | Ubiquitination | Uniprot | |
K430 | Sumoylation | Uniprot | |
K430 | Ubiquitination | Uniprot |
Research Backgrounds
Transcription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. Activates the transcription of growth-related genes. Binds to the VEGFA promoter, promoting VEGFA production and subsequent sprouting angiogenesis. Regulator of somatic reprogramming, controls self-renewal of embryonic stem cells. Functions with TAF6L to activate target gene expression through RNA polymerase II pause release (By similarity).
Phosphorylated by PRKDC. Phosphorylation at Ser-329 by PIM2 leads to the stabilization of MYC (By similarity). Phosphorylation at Ser-62 by CDK2 prevents Ras-induced senescence. Phosphorylated at Ser-62 by DYRK2; this primes the protein for subsequent phosphorylation by GSK3B at Thr-58. Phosphorylation at Thr-58 and Ser-62 by GSK3 is required for ubiquitination and degradation by the proteasome.
Ubiquitinated by the SCF(FBXW7) complex when phosphorylated at Thr-58 and Ser-62, leading to its degradation by the proteasome. In the nucleoplasm, ubiquitination is counteracted by USP28, which interacts with isoform 1 of FBXW7 (FBW7alpha), leading to its deubiquitination and preventing degradation. In the nucleolus, however, ubiquitination is not counteracted by USP28 but by USP36, due to the lack of interaction between isoform 3 of FBXW7 (FBW7gamma) and USP28, explaining the selective MYC degradation in the nucleolus. Also polyubiquitinated by the DCX(TRUSS) complex. Ubiquitinated by TRIM6 in a phosphorylation-independent manner (By similarity).
Nucleus>Nucleoplasm. Nucleus>Nucleolus.
Efficient DNA binding requires dimerization with another bHLH protein. Binds DNA as a heterodimer with MAX. Interacts with TAF1C and SPAG9. Interacts with PARP10. Interacts with KDM5A and KDM5B. Interacts (when phosphorylated at Thr-58 and Ser-62) with FBXW7. Interacts with PIM2. Interacts with RIOX1. The heterodimer MYC:MAX interacts with ABI1; the interaction may enhance MYC:MAX transcriptional activity. Interacts with TRIM6 (By similarity). Interacts with NPM1; the binary complex is recruited to the promoter of MYC target genes and enhances their transcription. Interacts with CIP2A; leading to the stabilization of MYC.
Research Fields
· Cellular Processes > Cell growth and death > Cell cycle. (View pathway)
· Cellular Processes > Cell growth and death > Cellular senescence. (View pathway)
· Cellular Processes > Cellular community - eukaryotes > Signaling pathways regulating pluripotency of stem cells. (View pathway)
· Environmental Information Processing > Signal transduction > MAPK signaling pathway. (View pathway)
· Environmental Information Processing > Signal transduction > ErbB signaling pathway. (View pathway)
· Environmental Information Processing > Signal transduction > PI3K-Akt signaling pathway. (View pathway)
· Environmental Information Processing > Signal transduction > Wnt signaling pathway. (View pathway)
· Environmental Information Processing > Signal transduction > TGF-beta signaling pathway. (View pathway)
· Environmental Information Processing > Signal transduction > Hippo signaling pathway. (View pathway)
· Environmental Information Processing > Signal transduction > Jak-STAT signaling pathway. (View pathway)
· Human Diseases > Infectious diseases: Viral > Hepatitis B.
· Human Diseases > Infectious diseases: Viral > HTLV-I infection.
· Human Diseases > Infectious diseases: Viral > Epstein-Barr virus infection.
· Human Diseases > Cancers: Overview > Pathways in cancer. (View pathway)
· Human Diseases > Cancers: Overview > Transcriptional misregulation in cancer.
· Human Diseases > Cancers: Overview > Proteoglycans in cancer.
· Human Diseases > Cancers: Overview > MicroRNAs in cancer.
· Human Diseases > Cancers: Specific types > Colorectal cancer. (View pathway)
· Human Diseases > Cancers: Specific types > Endometrial cancer. (View pathway)
· Human Diseases > Cancers: Specific types > Thyroid cancer. (View pathway)
· Human Diseases > Cancers: Specific types > Bladder cancer. (View pathway)
· Human Diseases > Cancers: Specific types > Chronic myeloid leukemia. (View pathway)
· Human Diseases > Cancers: Specific types > Acute myeloid leukemia. (View pathway)
· Human Diseases > Cancers: Specific types > Small cell lung cancer. (View pathway)
· Human Diseases > Cancers: Specific types > Breast cancer. (View pathway)
· Human Diseases > Cancers: Specific types > Hepatocellular carcinoma. (View pathway)
· Human Diseases > Cancers: Specific types > Gastric cancer. (View pathway)
· Human Diseases > Cancers: Overview > Central carbon metabolism in cancer. (View pathway)
· Organismal Systems > Endocrine system > Thyroid hormone signaling pathway. (View pathway)
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