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We find that many biological activities of Myc (show MYC ELISA Kits) do not, or only partly, require the association with Max--
Studies suggest that inducible MYC Associated Factor X (MAX) knockout embryonic stem cells (ESCs (show NR2E3 ELISA Kits)) provide an excellent platform for exploring the molecular mechanisms of meiosis initiation.
Myc (show MYC ELISA Kits) represses C/EBPdelta (show CEBPD ELISA Kits) expression by associating with the C/EBPdelta (show CEBPD ELISA Kits) proximal promoter as a transient component of a repressive complex that includes Max and Miz1 (show PIAS2 ELISA Kits)
The switch from Mnt-Max to Myc (show MYC ELISA Kits)-Max during bile duct ligation (cholestasis) and in hepatocytes treated with lithocholic acid is responsible for the induction in p53 (show TP53 ELISA Kits) and cyclin D1 (show CCND1 ELISA Kits) expression and contributes to apoptosis.
the c-Myc (show MYC ELISA Kits)-Max complex exerts its transcriptional regulatory role and hnRNP U (show HNRNPU ELISA Kits) may be a coactivator of this transcriptional activator complex.
Sequence-specific DNA binding by MYC (show MYC ELISA Kits)/MAX to low-affinity non-E-box motifs
The SDHA, TMEM127, MAX, and SDHAF2 genes contribute to hereditary pheochromocytoma and paraganglioma.
These results suggest that the wild type Max homodimer is important for attenuating the binding of c-Myc (show MYC ELISA Kits) to specific and non-specific DNA, whereas alternative splicing (e.g. DeltaMax) is unable to do so. Conversely, the splicing of Max into DeltaMax could provoke an increase in overall chromatin bound c-Myc (show MYC ELISA Kits).
The mechanism of inhibition of c-Myc (show MYC ELISA Kits) transcriptional activity by Miz-1 (show ZBTB17 ELISA Kits) that binds c-Myc (show MYC ELISA Kits) while competing for binding with Max has been described.
The introduction of wild-type MAX cDNA into PC12 cells significantly decreased MYC's ability to bind to canonical E-boxes, while pathogenic MAX proteins were not able to fully repress MYC (show MYC ELISA Kits) activity. Further clinical and molecular evaluation of variant carriers corroborated the results obtained with the functional assessment.
Celastrol and some of its quinone methidecontaining analogs directly inhibit c-Myc (show MYC ELISA Kits)-Max heterodimers in tumor cells.
We confirmed that these dimeric inhibitors directly bind to Myc (show MYC ELISA Kits) blocking its interaction with Max and affect transcription of MYC (show MYC ELISA Kits) dependent genes.
MYC (show MYC ELISA Kits) is part of a network of bHLHLZ proteins centered on the MYC (show MYC ELISA Kits) heterodimeric partner MAX and its counterpart, the MAX-like protein MLX (show MLX ELISA Kits).
Myc (show MYC ELISA Kits) and its obligate heterodimeric partner, Max, are integral to the coordinated recruitment and post-translational modification of components of the core transcriptional machinery.
Here we review the activities of MYC (show MYC ELISA Kits), MNT and other MAX interacting proteins in the setting of T and B cell activation (show BLNK ELISA Kits) and oncogenesis
The protein encoded by this gene is a member of the basic helix-loop-helix leucine zipper (bHLHZ) family of transcription factors. It is able to form homodimers and heterodimers with other family members, which include Mad, Mxi1 and Myc. Myc is an oncoprotein implicated in cell proliferation, differentiation and apoptosis. The homodimers and heterodimers compete for a common DNA target site (the E box) and rearrangement among these dimer forms provides a complex system of transcriptional regulation. Mutations of this gene have been reported to be associated with hereditary pheochromocytoma. A pseudogene of this gene is located on the long arm of chromosome 7. Alternative splicing results in multiple transcript variants.
, Max homologue 2
, Myc binding protein Xmax4
, myc-associated factor X
, protein max
, MYC associated factor X
, myc-binding novel HLH/LZ protein
, protein myn
, class D basic helix-loop-helix protein 4
, Myc binding protein Xmax2