Analytical Data
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Gene name
C17L
- Application
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Alternative Names
C17L；Envelope phospholipase OPG057
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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
P33815
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Expression Region
1-372aa
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AA Sequence
MWPFTSAPAGAKCRLVETLPENMDFRSDHLTTFECFNEIITLAKKYIYIASFCCNPLSTTRGALIFDKLKEASEKGIKIIVLLDERGKRNLGELQSHCPDINFITVNIDKKNNVGLLLGCFWVSDDERCYVGNASFTGGSIHTIKTLGVYSDYPPLATDLRRRFDTFKAFNSVKNSWLNLYSSACCLPVSTAYHIKNPIGGVFFTDSPEHLLGYSRDLDTDVVIDKLRSAKTSIDIEHLAIVPTTRVDGNSYYWPDIYNSIIEAAINRGVKIRLLVGNWDKNDVYSMATAESLDALCVQNDLSVKVFTIQNNTKLLIVDDEYVHITSANFDGTHYQNHGFVSFNSIDKQLVSEAKKIFERDWVSSHSKSLKI
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Molecular Weight
49.4 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
C17L recombinant protein, derived from the herpes simplex virus, has garnered significant attention in immunological research due to its intriguing properties as a potential therapeutic agent. It is situated within a context where the development of effective vaccines and immune modulators is critical for combating viral infections and enhancing immune responses. Researchers have been particularly interested in C17L's ability to modulate the immune system, as it can influence cytokine production and T-cell activation. Initial studies have indicated that C17L may have a role in promoting Th1-type immune responses, which are essential for effective viral clearance. Furthermore, it has been suggested that C17L could serve as an adjuvant in vaccine formulations, potentially improving the efficacy of vaccines against various pathogens. The mechanistic understanding of C17L’s interaction with immune cells is still an active area of research, with ongoing studies focusing on its structure-function relationship and the pathways it influences. As the field of immunotherapy continues to evolve, C17L recombinant protein represents a promising candidate for novel therapeutic applications, demonstrating the need for continued exploration of its biological functions and potential clinical utility.
