Analytical Data
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Gene name
HCNGP
- Application
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Alternative Names
Transcriptional regulator protein HCNGP
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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
Q9UHR5
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Expression Region
91-308aa
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AA Sequence
TEAEKRDPQELVASFSERVRNMSPDEIKIPPEPPGRCSNHLQDKIQKLYERKIKEGMDMNYIIQRKKEFRNPSIYEKLIQFCAIDELGTNYPKDMFDPHGWSEDSYYEALAKAQKIEMDKLEKAKKERTKIEFVTGTKKGTTTNATSTTTTTASTAVADAQKRKSKWDSAIPVTTIAQPTILTTTATLPAVVTVTTSASGSKTTVISAVGTIVKKAKQ
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Molecular Weight
28.4 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
Related Products
Protein Description
HCNGP, or Heterologous Co-Expression of Non-Glycosylated Proteins, has gained significant attention in the field of biotechnology and biopharmaceuticals due to its potential to improve the production of recombinant proteins. Traditional expression systems often struggle with the post-translational modifications that glycoproteins require for proper functionality. HCNGP focuses on expressing proteins in a non-glycosylated form, facilitating easier purification and characterization while ensuring that important structural features are retained. This approach is particularly valuable for the development of vaccines and therapeutic proteins, as it minimizes the risk of undesired immune responses associated with glycosylation variations. Researchers have been exploring various expression systems, including bacterial, yeast, and microbial platforms, to optimize the yield and functionality of HCNGP. The strategy helps to bypass complexities typically presented in mammalian systems, allowing for faster and more cost-effective production processes. As the demand for biopharmaceuticals grows, the HCNGP approach offers promising pathways for addressing the challenges associated with the effective production of therapeutic proteins, ultimately benefiting both research and clinical applications. This emerging technology paves the way for innovative solutions in the production of safe and effective biopharmaceuticals, enhancing their availability and accessibility in the healthcare sector.
