Recombinant Human c-Myc protein (Tagged) is a Human Full Length protein, in the 1 to 439 aa range, expressed in Escherichia coli, with >85%, suitable for SDS-PAGE.
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BHLHE39, MYC, Myc proto-oncogene protein, Class E basic helix-loop-helix protein 39, Proto-oncogene c-Myc, Transcription factor p64, bHLHe39
- SDS-PAGE
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SDS-PAGE - Recombinant Human c-Myc protein (Tagged) (AB235798)
(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) analysis with 5% enrichment gel and 15% separation gel of ab235798.
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This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
C-Myc is involved in regulating cell growth and proliferation. It forms part of the Myc/Max complex which binds to DNA to regulate gene expression. This activity affects cellular metabolism ribosome biogenesis and cell cycle entry emphasizing its regulation of cellular energy and stress response. Its expression levels critically govern normal cellular functions and homeostasis.
Pathways
C-Myc plays an important role in the cell cycle pathway and apoptosis regulation. Specifically c-Myc is associated with the Wnt signaling pathway which influences cellular proliferation and differentiation. It also interacts with other proteins like Cyclin D1 influencing cell cycle control. These interactions ensure c-Myc's involvement in regulating key processes related to cell proliferation and stability.
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기능
Transcription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3' (PubMed : 24940000, PubMed : 25956029). Activates the transcription of growth-related genes (PubMed : 24940000, PubMed : 25956029). Binds to the VEGFA promoter, promoting VEGFA production and subsequent sprouting angiogenesis (PubMed : 24940000, PubMed : 25956029). Regulator of somatic reprogramming, controls self-renewal of embryonic stem cells (By similarity). Functions with TAF6L to activate target gene expression through RNA polymerase II pause release (By similarity). Positively regulates transcription of HNRNPA1, HNRNPA2 and PTBP1 which in turn regulate splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform (PubMed : 20010808).
Post-translational modifications
Phosphorylated by PRKDC (PubMed:1597196). Phosphorylation at Ser-344 by PIM2 leads to the stabilization of MYC (By similarity). Phosphorylation at Ser-77 by CDK2 prevents Ras-induced senescence (PubMed:19966300, PubMed:20713526). Phosphorylated at Ser-77 by DYRK2; this primes the protein for subsequent phosphorylation by GSK3B at Thr-73 (PubMed:22307329). Phosphorylation at Thr-73 and Ser-77 by GSK3 is required for ubiquitination and degradation by the proteasome (PubMed:15103331, PubMed:17558397, PubMed:8386367). Dephosphorylation at multiple sites by the PNUTS-PP1 complex promotes MYC stability by preventing ubiquitination by the SCF(FBXW7) complex (PubMed:30158517). Dephosphorylation at Ser-77 by protein phosphatase 2A (PPP2CA) promotes its degradation; interaction with PPP2CA is enhanced by AMBRA1 (PubMed:25438055, PubMed:25803737).. Ubiquitinated by the SCF(FBXW7) complex when phosphorylated at Thr-73 and Ser-77, leading to its degradation by the proteasome (PubMed:15103331, PubMed:17558397, PubMed:25775507, PubMed:30158517). In the nucleoplasm, ubiquitination is counteracted by USP28, which interacts with isoform 1 of FBXW7 (FBW7alpha), leading to its deubiquitination and preventing degradation (PubMed:17558397, PubMed:17873522). 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 (PubMed:17558397, PubMed:25775507). Also polyubiquitinated by the DCX(TRPC4AP) complex (PubMed:20551172, PubMed:29779948). Ubiquitinated by UBR5 when not forming a heterodimer with another bHLH protein, leading to its degradation: UBR5 recognizes and binds a degron that is only available upon heterodimer dissociation (PubMed:33208877, PubMed:37478862). Ubiquitinated by TRIM6 in a phosphorylation-independent manner (By similarity).
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