Analytical Data
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Gene name
MAX
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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 (sf9, His-GST) is the recombinant human-derived MAX protein, expressed by Sf9 insect cells , with N-His, N-GST labeled tag.
- Application
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Alternative Names
Protein Max; MAX; BHLHD4; Myc-associated factor X
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Species
Human
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Source
Baculovirus
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Tag
N-His;N-GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P61244-1
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Expression Region
M1-S160
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Protein Length
Full Length of Isoform-1
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Molecular Weight
73 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
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Protein Description
The MAX protein, an essential member of the MYC family, plays a pivotal role in regulating cellular processes such as growth, proliferation, and apoptosis. Structurally, MAX serves as a dimerization partner for MYC and MAD proteins, forming heterodimers that distinctly influence gene expression. Research into MAX has gained traction due to its involvement in various cancers, where dysregulation of the MYC/MAX network often leads to aberrant cell proliferation and tumorigenesis. Moreover, MAX is crucial for maintaining cellular homeostasis and differentiation, making it a significant focus in cancer biology and therapeutic development. Studies indicate that impairments in MAX function can disrupt normal cellular pathways, thus linking it to multiple malignancies. The exploration of MAX's role in oncogenesis, alongside its potential as a therapeutic target, continues to be a vital area of investigation, particularly in understanding how to manipulate its interactions within the MYC network for cancer treatment. By elucidating the mechanisms through which MAX operates, researchers hope to uncover novel strategies for intervention in cancers where this protein’s function is compromised, ultimately leading to more effective therapeutics.
