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The protein encoded by MAX is a member of the basic helix-loop-helix leucine zipper (bHLHZ) family of transcription factors.
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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.
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.
Here we review the activities of MYC (show MYC Antibodies), MNT (show MNT Antibodies) and other MAX interacting proteins in the setting of T and B cell activation (show BLNK Antibodies) and oncogenesis
Delta Max, but not full-length Max, rescues Myc (show MYC Antibodies)-dependent glycolytic gene expression upon induced EGFRvIII loss, and correlates with hnRNPA1 (show HNRNPA1 Antibodies) expression and downstream Myc (show MYC Antibodies)-dependent gene transcription in patients.
Data show that Sirt1 (show SIRT1 Antibodies), p53 (show TP53 Antibodies), and p38(MAPK (show MAPK14 Antibodies)) are involved in the detrimental phenotype of Max-null ESCs (show NR2E3 Antibodies). Analyses revealed these proteins are involved at varying levels to one another in the hierarchy of the pathway leading to cell death in Max-null ESCs (show NR2E3 Antibodies).
New structural determinants for c-Myc specific heterodimerization with Max and development of a novel homodimeric c-Myc b-HLH-LZ.
Max b-HLH-LZ can transduce into cells and inhibit c-Myc (show MYC Antibodies) transcriptional activities
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