Analytical Data
-
Gene name
MAX
-
简介
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.
- Application
-
Alternative Names
rHuMAX, His; Protein Max; Class D Basic Helix-Loop-Helix Protein 4; bHLHd4; Myc-Associated Factor X; MAX; BHLHD4
-
Species
Human
-
Source
E. coli
-
Tag
C-6*His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P61244-2
-
Expression Region
M1-S151
-
Protein Length
Full Length of Isoform-2
-
Molecular Weight
21.0 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
The MAX (MYC-associated factor X) protein is a crucial member of the Myc family of transcription factors that plays a pivotal role in cellular processes such as proliferation, differentiation, and apoptosis. Since its discovery, research has revealed that MAX functions primarily as a dimerization partner for Myc and other bHLH-LZ proteins, thereby modulating gene expression and cellular responses. Importantly, the dysregulation of Myc and its interaction with MAX has been implicated in various cancers, emphasizing the need to understand this protein's function in tumorigenesis. Beyond its role in cancer, studies have also highlighted MAX's involvement in various physiological processes, including neural development and metabolic regulation. Thus, uncovering the structural and functional dynamics of MAX is essential for elucidating its contributions to both normal cellular functions and disease states. Current research employs advanced techniques such as structural biology, molecular biology, and genetic models to elucidate the mechanisms by which MAX exerts its effects, aiming to identify potential therapeutic targets for diseases associated with Myc dysregulation. Understanding MAX's role in the cellular context may pave the way for novel cancer treatment strategies, making it a significant focus of ongoing biomedical research.
