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anti-Mouse (Murine) MAX Antibodies:
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Studies suggest that inducible MYC Associated Factor X (MAX) knockout embryonic stem cells (ESCs (show NR2E3 Antibodies)) provide an excellent platform for exploring the molecular mechanisms of meiosis initiation.
Myc (show MYC Antibodies) represses C/EBPdelta (show CEBPD Antibodies) expression by associating with the C/EBPdelta (show CEBPD Antibodies) proximal promoter as a transient component of a repressive complex that includes Max and Miz1 (show PIAS2 Antibodies)
The switch from Mnt-Max to Myc (show MYC Antibodies)-Max during bile duct ligation (cholestasis) and in hepatocytes treated with lithocholic acid is responsible for the induction in p53 (show TP53 Antibodies) and cyclin D1 (show CCND1 Antibodies) expression and contributes to apoptosis.
the c-Myc (show MYC Antibodies)-Max complex exerts its transcriptional regulatory role and hnRNP U (show HNRNPU Antibodies) may be a coactivator of this transcriptional activator complex.
To our knowledge, this is the first report of an association between dysregulation of the MAX-MYC (show MYC Antibodies) network in the brain and a behavior, suggesting a novel approach for exploiting the neuroplasticity associated with depression
Sequence-specific DNA binding by MYC (show MYC Antibodies)/MAX to low-affinity non-E-box motifs
The SDHA (show SDHA Antibodies), TMEM127 (show TMEM127 Antibodies), MAX, and SDHAF2 (show Sdhaf2 Antibodies) 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 Antibodies) 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 Antibodies).
The mechanism of inhibition of c-Myc (show MYC Antibodies) transcriptional activity by Miz-1 (show ZBTB17 Antibodies) that binds c-Myc (show MYC Antibodies) 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 Antibodies) 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 Antibodies)-Max heterodimers in tumor cells.
We confirmed that these dimeric inhibitors directly bind to Myc (show MYC Antibodies) blocking its interaction with Max and affect transcription of MYC (show MYC Antibodies) dependent genes.
MYC (show MYC Antibodies) is part of a network of bHLHLZ proteins centered on the MYC (show MYC Antibodies) heterodimeric partner MAX and its counterpart, the MAX-like protein MLX (show MLX Antibodies).
Myc (show MYC Antibodies) and its obligate heterodimeric partner, Max, are integral to the coordinated recruitment and post-translational modification of components of the core transcriptional machinery.
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.
myc-associated factor X
, myc-binding novel HLH/LZ protein
, protein max
, protein myn
, class D basic helix-loop-helix protein 4