Analytical Data
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Gene name
CLECL1P
- Application
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Alternative Names
CLECL1P；CLECL1；DCAL1；Putative C-type lectin-like domain family 1
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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
Q8IZS7
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Expression Region
89-167aa
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AA Sequence
KTVRTSPLELAFPLQRSVSFNFSTVHKSCPAKDWKVHKGKCYWIAETKKSWNKSQNDCAINNSYLMVIQDITAMVRFNI
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Molecular Weight
13 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
CLECL1P, short for C-type lectin domain family 1 member P, is a type of receptor implicated in various immune responses. Research into CLECL1P has gained momentum due to its potential role in pathogen recognition and modulation of inflammatory processes. As a member of the C-type lectin family, CLECL1P is known to bind carbohydrate structures, facilitating cell-cell interactions and influencing immune signaling pathways. Studies have indicated that alterations in CLECL1P expression may be linked to various diseases, including infectious diseases and autoimmune disorders. Understanding the structure and function of CLECL1P at the molecular level is crucial for uncovering its biological roles and potential therapeutic applications. Recent advancements in recombinant protein technology enable the production of CLECL1P, providing valuable tools for studying its properties in vitro and in vivo. By investigating the binding affinities and downstream effects of CLECL1P, researchers aim to elucidate its contribution to innate immunity and identify targets for therapeutic intervention. Overall, the exploration of CLECL1P not only enhances our understanding of immune mechanisms but also opens new avenues for developing strategies to combat various health conditions linked to immune dysregulation.
