Analytical Data
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Gene name
SELP
- Application
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Alternative Names
SELP；SELP；SEPP1；SelenoProtein P
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Species
Human
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Source
E. coli
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Tag
N-6His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P16109
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Expression Region
58~195aa
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Molecular Weight
18kDa
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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
Identification
Protein Description
The study of SELP (selectin P ligand) recombinant protein is rooted in the broader context of understanding cell adhesion and the immune response. Selectins are a family of cell adhesion molecules that play a crucial role in the interaction between leukocytes and endothelial cells during inflammation and immune surveillance. SELP, specifically expressed on leukocytes, mediates their binding to activated endothelium, influencing processes such as rolling, adhesion, and migration to sites of tissue injury or infection. Research into SELP recombinant proteins aims to elucidate the molecular mechanisms underlying these interactions, with potential applications in treating various inflammatory diseases, including autoimmune disorders and cardiovascular diseases. By producing SELP in a recombinant form, scientists can study its structure-function relationships, assess its binding affinity to ligands, and explore its role in mediating cell signaling pathways. Furthermore, SELP recombinant proteins could serve as therapeutic agents or targets for drug development, providing insights into novel strategies for modulating immune responses and improving health outcomes. This growing field of inquiry underscores the importance of SELP in both basic research and clinical applications, paving the way for advanced therapies in inflammation and immune modulation.
