Analytical Data
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Gene name
DEC-205/CD205
- Application
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Alternative Names
CD205; LY75; CLEC13B; DEC-205; GP200-MR6; C-type lectin domain family 13 member B
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O60449
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Expression Region
Cys216~Cys501
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Molecular Weight
34kDa
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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
DEC-205, also known as CD205, is a dendritic cell-specific receptor that plays a crucial role in the immune response by mediating the uptake and presentation of antigens. This receptor is known for its ability to internalize antigens effectively and subsequently present them to T cells, thereby influencing T cell activation and differentiation. Research into DEC-205/CD205 has gained traction due to its potential applications in immunotherapy, particularly in cancer and infectious diseases. By exploiting the antigen-presenting capabilities of DEC-205, scientists aim to enhance vaccine efficacy and develop targeted therapies that can manipulate the immune response. Recombinant proteins of DEC-205 are being studied to better understand its structure-function relationship, optimize antigen delivery systems, and improve the design of therapeutic vaccines. Additionally, the exploration of DEC-205's role in various immune pathways could uncover new strategies for disease modulation, making it a promising target in the realm of personalized medicine and immunological research.
