Analytical Data
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Gene name
Hepc
- Application
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Alternative Names
Hepc；HEPC；LEAP1；Hepcidin
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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
P81172
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Expression Region
25-84aa
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AA Sequence
SVFPQQTGQLAELQPQDRAGARASWMPMFQRRRRRDTHFPICIFCCGCCH RSKCGMCCKT
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Molecular Weight
32 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
Hepatitis C virus (HCV) infection remains a significant global health challenge, affecting millions of people worldwide. The development of effective vaccines and therapeutics has been hampered by the virus's complex and variable nature. Research into HCV recombinant proteins has gained momentum as a promising strategy for the identification of antigens that can elicit robust immune responses. Recombinant proteins derived from HCV structural and non-structural genes can be used for both diagnostic purposes and as potential vaccine candidates. Key studies have focused on the production of these proteins through recombinant DNA technology, enabling detailed investigation of their immunogenic properties. This research aims to enhance our understanding of the host immune response to HCV and to facilitate the development of safe and effective vaccines. Furthermore, the exploration of HCV recombinant proteins has highlighted the importance of understanding the virus's interactions with the immune system, paving the way for novel therapeutic strategies. Overall, ongoing studies in this field are crucial for improving prevention, diagnosis, and treatment of hepatitis C, ultimately contributing to global health efforts to eradicate this viral infection.
