Analytical Data
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Gene name
CLECL1P
- Application
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Alternative Names
Dendritic cell-associated lectin 1
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Species
Human
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Source
Baculovirus
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Tag
N- His & C- Myc
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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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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
Related Products
Protein Description
CLECL1P, a member of the C-type lectin domain family, has garnered attention in recent years due to its potential roles in immune response and pathogen recognition. This protein is primarily expressed in immune cells and is involved in various biological processes, including cell adhesion and signaling. Research indicates that CLECL1P may play a crucial role in modulating immune responses, particularly in the context of infections and inflammatory conditions. Understanding the structural and functional characteristics of CLECL1P through recombinant protein studies is vital for elucidating its mechanisms of action. This knowledge can pave the way for therapeutic applications, particularly in developing strategies to enhance immune responses against pathogens or to mitigate excessive inflammation. Moreover, as a glycoprotein, the post-translational modifications of CLECL1P are significant for its biological activity, warranting detailed investigations into its glycosylation patterns. Overall, exploring CLECL1P as a recombinant protein provides important insights into its functional properties and potential as a biomarker or therapeutic target in immune-related diseases.
