Analytical Data
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Gene name
CLEC2B
- Application
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Alternative Names
CLEC2B；AICL；CLECSF2；IFNRG1；C-type lectin domain family 2 member B
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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
Q92478
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Expression Region
1-149aa
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AA Sequence
MMTKHKKCFIIVGVLITTNIITLIVKLTRDSQSLCPYDWIGFQNKCYYFSKEEGDWNSSKYNCSTQHADLTIIDNIEEMNFLRRYKCSSDHWIGLKMAKNRTGQWVDGATFTKSFGMRGSEGCAYLSDDGAATARCYTERKWICRKRIH
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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
CLEC2B is a C-type lectin receptor that plays a critical role in various biological processes, including immune response, cell signaling, and pathogenesis. It is primarily expressed on the surface of myeloid cells, where it interacts with specific glycoproteins and polysaccharides, contributing to the recognition and clearance of pathogens. Research into CLEC2B has gained momentum due to its potential implications in understanding immune regulation and the development of novel therapeutic strategies. As a member of the C-type lectin family, CLEC2B exhibits unique structural features that enable it to bind to diverse ligands, which can influence cellular functions. Studies have also suggested that CLEC2B could be involved in disease mechanisms, including autoimmune disorders and inflammation. Understanding the structural and functional dynamics of CLEC2B through recombinant protein studies can provide insights into its roles in health and disease, paving the way for targeted interventions that harness its biological functions. Researchers are focused on characterizing CLEC2B's interactions and signaling pathways, which may lead to innovative treatments for diseases that involve immune dysregulation. Hence, generating and studying recombinant CLEC2B proteins is crucial for elucidating its function and exploring its potential as a biomarker or therapeutic target.
