Analytical Data
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Gene name
MAX
- Application
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Alternative Names
MAX;BHLHD4;Protein max
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P61244
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Expression Region
1-160aa
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AA Sequence
MSDNDDIEVE SDEEQPRFQS AADKRAHHNA LERKRRDHIK DSFHSLRDSV PSLQGEKASR AQILDKATEY IQYMRRKNHT HQQDIDDLKR QNALLEQQVR ALEKARSSAQ LQTNYPSSDN SLYTNAKGST ISAFDGGSDS SSESEPEEPQ SRKKLRMEAS LEHHHHHH
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Molecular Weight
19 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, a member of the Myc family, plays a significant role in the regulation of gene expression and cell growth, functioning primarily as a transcription factor. It forms heterodimers with other proteins of the Myc family, like c-Myc, to activate or repress target genes involved in critical cellular processes such as proliferation, differentiation, and apoptosis. Dysregulation of the Myc/MAX pathway is often implicated in various cancers, as aberrant expression of these proteins can lead to uncontrolled cell division and tumorigenesis. Research into MAX has garnered attention for its potential as a therapeutic target, particularly in cancers where Myc is overexpressed. Moreover, understanding the structural and functional aspects of MAX, including its interactions with various cofactors and how these interactions influence its activity, is essential. This knowledge could pave the way for novel strategies to modulate MAX function in disease contexts. Additionally, studying the protein structure of MAX through methods like X-ray crystallography or cryo-electron microscopy provides insights into engineering inhibitors that specifically disrupt MAX interactions, which may contribute to cancer treatment or other related diseases. Therefore, MAX represents a critical focus in cancer biology and drug discovery, with ongoing investigations aimed at uncovering its multifaceted role in cellular dynamics and its potential as a biomarker and therapeutic target.
