Analytical Data
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Gene name
CHT
- Application
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Alternative Names
CHT1
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Species
Human
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Source
HEK293
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Tag
Strep;His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9GZV3
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Expression Region
M1-Q580
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Protein Length
Full Length
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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
Related Products
Protein Description
ATG101 is a protein that plays a critical role in the autophagy process, a fundamental cellular mechanism responsible for degrading and recycling cellular components. As a relatively newly identified protein, ATG101 has garnered attention in the field of cellular biology due to its involvement in regulating autophagosome formation. It interacts with other key autophagy proteins, such as ULK1 and ATG13, to facilitate the assembly of the autophagy initiation complex. This process is essential for maintaining cellular homeostasis, particularly under stress conditions, where cells must adapt by removing damaged organelles and misfolded proteins. Recent studies have suggested that dysregulation of ATG101 and its associated pathways may contribute to various diseases, including neurodegenerative disorders and cancer. Understanding the molecular mechanisms underlying ATG101's function can provide insights into potential therapeutic targets for enhancing autophagy in pathological conditions. This makes the recombinant expression and purification of ATG101 crucial for further biochemical and structural studies to elucidate its roles and functions within the autophagic pathway. Thus, ongoing research into ATG101 promises to expand our knowledge of cellular degradation mechanisms and their implications in health and disease.
