Analytical Data
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Gene name
CLEC1B
- Application
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Alternative Names
1810061I13Rik; C type lectin domain family 1 member B; C type lectin like receptor 2; C-type lectin domain family 1 member B; C-type lectin domain family 1; member B; C-type lectin-like receptor
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9P126
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Expression Region
1-196aa
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AA Sequence
MQDEDGYITLNIKTRKPALVSAVMQRNYLQDENENRTGTLQQLAKRFCQYVVKQSELKGTFKGHKCSPCDTNWRYYGDSCYGFFRHNLTWEESKQYCTDMNATLLKIDNRNIVEYIKARTHLIRWVGLSRQKSNEVWKWEDGSVISENMFEFLEDGKGNMNCAYFHNGKMHPTFCENKHYLMCERKAGMTKVDQLP
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Molecular Weight
49.5 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
CLEC1B, also known as C-type lectin domain family 1 member B, is a key protein involved in the immune response, specifically in the recognition of pathogens and the regulation of immune cell functions. This protein is predominantly expressed in dendritic cells and macrophages, where it plays a crucial role in antigen presentation and the modulation of inflammatory responses. Research on CLEC1B has gained prominence due to its potential implications in various diseases, including infections, autoimmune disorders, and cancer. The unique structure of CLEC1B, characterized by its C-type lectin domain, allows it to interact with specific carbohydrate structures on pathogens, thereby influencing immune signaling pathways. Recent studies have focused on the functional characterization of CLEC1B to better understand its mechanisms in immune modulation and its potential as a therapeutic target. Investigating the pathways regulated by CLEC1B may provide insights into the development of novel immunotherapies and vaccines, highlighting its importance in both basic research and clinical applications. Overall, unlocking the functional roles of CLEC1B offers promising avenues for enhancing immune responses and addressing a range of health challenges.
