catalog number :
MBS125025
products full name :
Phospho-MAX-S11 Polyclonal Antibody
products short name :
MAX-S11
products name syn :
Phospho-MAX-S11: MGC10775; MGC11225; MGC18164; MGC34679; MGC36767; bHLHd4; bHLHd5; bHLHd6; bHLHd7; bHLHd8; orf1
other names :
Protein max; Protein max; protein max; class D basic helix-loop-helix protein 4; MYC associated factor X; Class D basic helix-loop-helix protein 4; bHLHd4; Myc-associated factor X
other gene names :
MAX; MAX; bHLHd4; BHLHD4; bHLHd4
uniprot entry name :
MAX_HUMAN
purity :
Affinity Purification
storage stability :
Store at -20 degree C (regular) or -80 degree C (long term). Avoid freeze / thaw cycles. Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3.
tested application :
Western Blot (WB), Immunofluorescence (IF)
app notes :
WB: 1:500 - 1:2000. IF: 1:50 - 1:200
other info1 :
Species: Human. Route: Synthetic Peptide
other info2 :
Immunogen: A phospho specific peptide corresponding to residues surrounding S11 of human MAX
products categories :
Phosphorylation
products description :
Members of the Myc/Max/Mad network function as transcriptional regulators with roles in various aspects of cell behavior including proliferation, differentiation and apoptosis (1). These proteins share a common basic-helix-loop-helix leucine zipper (bHLH-ZIP) motif required for dimerization and DNA-binding. Max was originally discovered based on its ability to associate with c-Myc and found to be required for the ability of Myc to bind DNA and activate transcription (2). Subsequently, Max has been viewed as a central component of the transcriptional network, forming homodimers as well as heterodimers with other members of the Myc and Mad families (1). The association between Max and either Myc or Mad can have opposing effects on transcriptional regulation and cell behavior (1). The Mad family consists of four related proteins; Mad1, Mad2 (Mxi1), Mad3 and Mad4, and the more distantly related members of the bHLH-ZIP family, Mnt and Mga. Like Myc, the Mad proteins are tightly regulated with short half-lives. In general, Mad family members interfere with Myc-mediated processes such as proliferation, transformation and prevention of apoptosis by inhibiting transcription (3,4).
ncbi pathways :
C-MYC Pathway (169344); Cell Cycle Pathway (530733); Cell Cycle, Mitotic Pathway (105765); Cyclin A:Cdk2-associated Events At S Phase Entry Pathway (105783); Cyclin E Associated Events During G1/S Transition Pathway (105770); G1/S Transition Pathway (105769); Integrated Breast Cancer Pathway (219801); MAPK Signaling Pathway (198779); MAPK Signaling Pathway (83048); MAPK Signaling Pathway (456)
ncbi summary :
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. [provided by RefSeq, Aug 2012]
uniprot summary :
MAX: a transcription factor. Forms a DNA- binding protein complex with MYC or MAD. The MYC-MAX complex is a transcriptional activator, whereas the MAD-MAX complex is a repressor. CPG methylation of the recognition site greatly inhibits DNA binding, suggesting that DNA methylation may regulate the MYC/MAX complex in vivo. May repress transcription via the recruitment of a chromatin remodeling complex containing H3-K9 histone methyltransferase activity. Three alternatively spliced isoforms have been reported. Protein type: DNA-binding; Transcription factor. Chromosomal Location of Human Ortholog: 14q23. Cellular Component: nucleoplasm; PML body; dendrite; cytoplasm; nucleus. Molecular Function: protein binding; protein homodimerization activity; sequence-specific DNA binding; protein heterodimerization activity; transcription coactivator activity; transcription cofactor activity; protein complex binding; transcription factor activity. Biological Process: transcription from RNA polymerase II promoter; neuron apoptosis; regulation of transcription, DNA-dependent; retina development in camera-type eye; protein complex assembly; response to axon injury; cellular response to starvation; response to insulin stimulus