protein

MAX Protein, Human (His)

HY-P70388

10 μg;50 μg

100;280 USD

MAX Protein, Human (His)

proteins

E. coli

10 μg;50 μg

100;280 USD

MAX protein is a transcriptional regulator that forms a complex with MYC to promote activation, or a complex with MAD to cause inhibition, binding to the core sequence 5'-CAC[GA]TG-3'. MAX acts as a repressor protein that recruits chromatin remodeling complexes with H3 "Lys-9" histone methyltransferase activity. MAX Protein, Human (His) is the recombinant human-derived MAX protein, expressed by E. coli , with C-6*His labeled tag. The total length of MAX Protein, Human (His) is 151 a.a., with molecular weight of ~21.0 kDa.

Human

MAX, a transcription regulator, forms a sequence-specific DNA-binding protein complex either with MYC, promoting transcriptional activation, or with MAD, leading to transcriptional repression, recognizing the core sequence 5'-CAC[GA]TG-3'. MAX may act as a transcriptional repressor by recruiting a chromatin remodeling complex with H3 'Lys-9' histone methyltransferase activity and repressing MYC transcriptional activity from E-box elements. Efficient DNA binding requires dimerization with another bHLH protein. It binds DNA as a heterodimer with either MYC or MAD. MAX is part of the E2F6.com-1 complex during the G0 phase, along with various other components. It is also a component of some MLL1/MLL complexes, contributing to the regulation of gene expression. MAX interacts with SPAG9, and when in a heterodimer with MYC, it interacts with ABI1, potentially enhancing MYC:MAX transcriptional activity. MAX's versatility in forming complexes with different partners underscores its role as a key modulator of gene expression.

rHuMAX, His; Protein Max; Class D Basic Helix-Loop-Helix Protein 4; bHLHd4; ; Myc-Associated Factor X; MAX; BHLHD4

Greater than 95% as determined by reducing SDS-PAGE.

Lyophilized from a 0.2 μm filtered solution of 20 mM Tris-HCl, 250 mM NaCl, pH 8.5.

Room temperature in continental US;may vary elsewhere.