Analytical Data
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Gene name
CLEC7A
- Application
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Alternative Names
CLEC7A；BGR；CLECSF12；DECTIN1；C-type lectin domain family 7 member A
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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
Q9BXN2
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Expression Region
1-77aa
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AA Sequence
MEYHPDLENLDEDGYTQLHFDSQSNTRIAVVSEKGSCAASPPWRLIAVIL GILCLVILVIAVVLGTMAGFKAVEFKG
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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
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Protein Description
CLEC7A, also known as Dectin-1, is a pattern recognition receptor primarily expressed on the surface of myeloid cells, including macrophages and dendritic cells. It plays a critical role in the immune system by recognizing beta-glucans, which are polysaccharides found in the cell walls of fungi and certain bacteria. The study of CLEC7A recombinant proteins has gained significant interest due to its potential applications in immunotherapy and vaccine development. Research indicates that CLEC7A activates immune responses through the induction of pro-inflammatory cytokines, promoting the phagocytosis of pathogens and the activation of T cells. Its ability to distinguish between self and non-self entities makes it a valuable target for enhancing immune responses against infections and cancer. Additionally, understanding the structure-function relationship of CLEC7A through recombinant protein studies may facilitate the design of novel therapeutic strategies. Recent advances in recombinant DNA technology have enabled the production of CLEC7A proteins with specific modifications, aiming to enhance their functionality and efficacy. Investigating these proteins can provide deeper insights into their mechanisms, paving the way for innovative approaches in treating diseases linked to immune dysregulation. Overall, the research on CLEC7A recombinant proteins holds promise for improving our understanding of innate immunity and developing new therapeutic avenues for a range of infectious and inflammatory diseases.
