MAX
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Official Full Name
MYC associated factor X
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Overview
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] -
Synonyms
MAX; MYC associated factor X; bHLHd4; protein max; class D basic helix-loop-helix protein 4;
- Recombinant Proteins
- Cell & Tissue Lysates
- Protein Pre-coupled Magnetic Beads
- Human
- Mouse
- Rat
- Rhesus Macaque
- Zebrafish
- E.coli
- HEK293
- HEK293T
- Insect Cell
- Insect Cells
- Mamanlian cells
- Mammalian Cell
- Wheat Germ
- C
- His
- Flag
- GST
- His (Fc)
- Avi
- His|GST
- Myc
- DDK
- Myc|DDK
- N/A
- N
- Involved Pathway
- Protein Function
- Interacting Protein
- MAX Related Articles
- MAX Related Research Area
MAX involved in several pathways and played different roles in them. We selected most pathways MAX participated on our site, such as MAPK signaling pathway, Pathways in cancer, Transcriptional misregulation in cancer, which may be useful for your reference. Also, other proteins which involved in the same pathway with MAX were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
Pathway Name | Pathway Related Protein |
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MAPK signaling pathway | PPP3R2;PDGFAB;RAC3A;TP53;NFATC3;ARR3A;FGF21;FGF10A;Casp3 |
Pathways in cancer | PLD1;VEGFB;WNT6;IKBKB;MAPK1;NTRK1;PTGER3;SMAD2;MMP9 |
Transcriptional misregulation in cancer | BCL2A1;H3F3A;MYCN;ZEB1;TRP53;CLSTN2;HPGD;GOLPH3;SIX4 |
Small cell lung cancer | RARB;LAMA1;BIRC7;CCNE2;ITGB1;BIRC3;COL4A1;BCL2;XIAP |
MAX has several biochemical functions, for example, RNA polymerase II core promoter proximal region sequence-specific DNA binding, protein binding, protein dimerization activity. Some of the functions are cooperated with other proteins, some of the functions could acted by MAX itself. We selected most functions MAX had, and list some proteins which have the same functions with MAX. You can find most of the proteins on our site.
Function | Related Protein |
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RNA polymerase II core promoter proximal region sequence-specific DNA binding | FOSL1A;GLI2;ELK1;FOS;TBX20;ZNF114;GRHL1;KLF13;ETV1 |
protein binding | NOTCH2NL;MCCC1;HNRNPUL1;PGLS;CNOT2;BLOC1S2A;ITSN1;SPSB4;ALDH3B1 |
protein dimerization activity | ARNTL1B;TFE3B;MYCL1;TWIST1A;AIFM1;ATOH1;HER11;BTRC;MSGN1 |
transcription coactivator activity | SUPT7L;SMARCB1;GABPA;MED16;NCOA1;WWTR1;KLF7;JUN;GTF2A1 |
transcription cofactor activity | KAT2B;ELK4;PTPN14;TADA2A;ZFP865;NFE2L1;PHF21B;TFDP2;MSX2 |
transcription factor activity, RNA polymerase II core promoter sequence-specific | HEYL;PAX7;HEY2;TFAP2B;MEF2C;HEY1;NKX3;SMAD3;MAX |
transcription factor activity, sequence-specific DNA binding | KDM5B;ZC3H8;SUPT6H;LHX1A;ETV5A;FOXG1;TADA2B;POU1F1;RELA |
MAX has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with MAX here. Most of them are supplied by our site. Hope this information will be useful for your research of MAX.
MYC
- Q&As
- Reviews
Q&As (6)
Ask a questionEvaluating the potential of MAX proteins as drug targets can involve several aspects, including their expression levels in organisms, their role in biological processes, and their changes in disease. In addition, factors such as ease of drug development for this protein and potential drug side effects need to be considered.
The function of MAX proteins may be related to their localization and structure within the cell. It may be a nuclear protein that regulates the transcription of specific genes by binding to DNA. In addition, it may also regulate processes such as cell signaling and cell proliferation by interacting with other proteins.
Mutations or modifications of MAX proteins may affect their function and thus on the organism. The specific effects may vary depending on the type and location of the mutation or modification and may involve various biological processes, such as growth and development, immune response, etc.
MAX proteins may be involved in a variety of biological processes, including cell proliferation, cell differentiation, apoptosis, etc. It may influence tumorigenesis and progression by modulating these processes.
The expression level of MAX protein may be regulated by a variety of factors, including gene transcription, translation, post-transcriptional modification, etc. Studying these regulatory mechanisms can help to understand the expression patterns of MAX proteins in organisms and their effects on biological processes.
MAX proteins may interact with other proteins to fulfill their functions. These interactions can involve various types of protein-protein interactions like electrostatic interactions, hydrogen bonding, etc. Understanding these interactions can help uncover the mechanism of action of MAX proteins in cells.
Customer Reviews (3)
Write a reviewGreatly improve the rate and selectivity of chemical reactions, and its scientific research value is incomparable.
MAX has excellent labeling results and can be used for a wide range of experimental methods, such as fluorescent labeling.
The high catalytic efficiency, high safety, and high expression level make the experimental results extremely confident.
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