Analytical Data
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Gene name
MYC
- Application
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Alternative Names
Class E basic helix-loop-helix protein 39 ;bHLHe39Proto-oncogene c-MycTranscription factor p64
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Species
Human
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P01106
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Expression Region
1-439aa
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Molecular Weight
52.8 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 MYC protein is a well-known transcription factor that plays a crucial role in cell proliferation, growth, and metabolism. Its dysregulation is frequently associated with various types of cancers, making it a significant target for therapeutic interventions. MYC is often overexpressed due to chromosomal translocations, amplifications, or mutations in cancer cells, leading to uncontrolled cell division and tumor progression. Research focusing on recombinant MYC protein has gained momentum as scientists aim to understand its function at a molecular level and its interactions with other proteins within the cell. By producing MYC as a recombinant protein, researchers can study its biochemical properties, post-translational modifications, and binding affinities with target genes. This approach allows for the identification of potential small-molecule inhibitors that can disrupt MYC's activity, offering new avenues for cancer treatment. Additionally, the use of MYC as a model for protein engineering and synthetic biology has opened new research pathways, enabling the design of novel therapeutic strategies and advancing our understanding of oncogenic processes. Overall, the study of recombinant MYC protein not only contributes to our knowledge of cancer biology but also holds promise for the development of innovative therapies targeting MYC-driven tumors.
