Analytical Data
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Gene name
CLEC4C
- Application
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Alternative Names
Blood dendritic cell antigen 2 Short name: BDCA-2 C-type lectin superfamily member 7 Dendritic lectin CD_antigen: CD303
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Species
Human
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Source
Yeast
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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
Q8WTT0
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Expression Region
45-213aa
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Molecular Weight
22 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
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Protein Description
CLEC4C, also known as the C-type lectin domain family 4 member C, is a protein that plays a critical role in the immune system, particularly in the recognition and response to pathogens. As a receptor expressed on the surface of dendritic cells, CLEC4C is involved in the detection of various microbial components, facilitating the initiation of immune responses. Research into CLEC4C has gained momentum due to its potential implications in understanding infectious diseases, autoimmune disorders, and cancer immunotherapy. Its ability to bind specific carbohydrate structures on pathogens suggests it may serve as a target for vaccine development and therapeutic interventions. The study of CLEC4C also offers insights into the mechanisms of immune tolerance and regulation, highlighting its importance in maintaining homeostasis in the immune system. Furthermore, recombinant proteins based on CLEC4C have been explored for their application in enhancing vaccine efficacy and modulating immune responses. Overall, the investigation of CLEC4C as a therapeutic target and its functional roles in immunity continues to be a significant area of research with promising prospects for improving human health.
