Analytical Data
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Gene name
HCV-Core
- Application
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Alternative Names
ACY3;ASPA2;N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming)
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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
Q8TC12
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Expression Region
22-318aa
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AA Sequence
PQIRKMLSSGVCTSTVQLPGKVVVVTGANTGIGKETAKELAQRGARVYLACRDVEKGELVAKEIQTTTGNQQVLVRKLDLSDTKSIRAFAKGFLAEEKHLHVLINNAGVMMCPYSKTADGFEMHIGVNHLGHFLLTHLLLEKLKESAPSRIVNVSSLAHHLGRIHFHNLQGEKFYNAGLAYCHSKLANILFTQELARRLKGSGVTTYSVHPGTVQSELVRHSSFMRWMWWLFSFFIKTPQQGAQTSLHCALTEGLEILSGNHFSDCHVAWVSAQARNETIARRLWDVSCDLLGLPID
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Molecular Weight
49.0kDa
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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
The HCV-Core recombinant protein has garnered significant attention in the field of hepatitis C virus (HCV) research due to its pivotal role in viral structure and immune response. HCV is a major global health concern, linked to chronic liver disease and hepatocellular carcinoma, affecting millions worldwide. The core protein, encoded by the HCV genome, forms the viral capsid and is crucial for the virus's assembly and release. Understanding the structure and function of the HCV-Core protein is essential for developing effective vaccines and therapeutics. Moreover, this protein is a key target for immune recognition, and it induces epitope-specific T-cell responses, which could be harnessed for immunotherapy. Research efforts have focused on the recombinant production of HCV-Core protein to create diagnostic tools and study its interactions with host immune components. Investigating the conformational properties of the HCV-Core protein enhances our knowledge of HCV pathogenesis and facilitates the identification of potential targets for drug development. With the continued evolution of therapeutic strategies, the characterization of HCV-Core and its role in inducing protective immunity remains a critical area of study, paving the way for innovative approaches to combat HCV infection and improve patient outcomes.
