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anti-Mouse (Murine) MAX Antikörper:
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Studies suggest that inducible MYC Associated Factor X (MAX) knockout embryonic stem cells (ESCs (zeige NR2E3 Antikörper)) provide an excellent platform for exploring the molecular mechanisms of meiosis initiation.
Myc (zeige MYC Antikörper) represses C/EBPdelta (zeige CEBPD Antikörper) expression by associating with the C/EBPdelta (zeige CEBPD Antikörper) proximal promoter as a transient component of a repressive complex that includes Max and Miz1 (zeige PIAS2 Antikörper)
The switch from Mnt-Max to Myc (zeige MYC Antikörper)-Max during bile duct ligation (cholestasis) and in hepatocytes treated with lithocholic acid is responsible for the induction in p53 (zeige TP53 Antikörper) and cyclin D1 (zeige CCND1 Antikörper) expression and contributes to apoptosis.
the c-Myc (zeige MYC Antikörper)-Max complex exerts its transcriptional regulatory role and hnRNP U (zeige HNRNPU Antikörper) 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 (zeige MYC Antikörper) network in the brain and a behavior, suggesting a novel approach for exploiting the neuroplasticity associated with depression
Sequence-specific DNA binding by MYC (zeige MYC Antikörper)/MAX to low-affinity non-E-box motifs
The SDHA (zeige SDHA Antikörper), TMEM127 (zeige TMEM127 Antikörper), MAX, and SDHAF2 (zeige Sdhaf2 Antikörper) 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 (zeige MYC Antikörper) 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 (zeige MYC Antikörper).
The mechanism of inhibition of c-Myc (zeige MYC Antikörper) transcriptional activity by Miz-1 (zeige ZBTB17 Antikörper) that binds c-Myc (zeige MYC Antikörper) 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 (zeige MYC Antikörper) 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 (zeige MYC Antikörper)-Max heterodimers in tumor cells.
We confirmed that these dimeric inhibitors directly bind to Myc (zeige MYC Antikörper) blocking its interaction with Max and affect transcription of MYC (zeige MYC Antikörper) dependent genes.
MYC (zeige MYC Antikörper) is part of a network of bHLHLZ proteins centered on the MYC (zeige MYC Antikörper) heterodimeric partner MAX and its counterpart, the MAX-like protein MLX (zeige MLX Antikörper).
Myc (zeige MYC Antikörper) 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