Analytical Data
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Gene name
P-Selectin
- Application
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Alternative Names
CD62P; Selectin, Platelet; PSEL; GMP140; LECAM3; GRMP; GMRP; PADGEM; Leukocyte-endothelial cell adhesion molecule 3; Platelet activation dependent granule-external membrane
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Species
Pig
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q29097
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Expression Region
Trp42~Tyr159
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Molecular Weight
17kDa
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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
P-selectin, a member of the selectin family of cell adhesion molecules, plays a critical role in the immune response and inflammation by mediating the rolling of leukocytes along the endothelium. This glycoprotein is expressed on the surface of activated endothelial cells and platelets, facilitating the recruitment of immune cells to sites of injury or infection. Understanding the function and mechanisms of P-selectin is essential for developing therapeutic strategies for various inflammatory diseases, cardiovascular disorders, and cancer metastasis. Research on recombinant P-selectin proteins has emerged as a valuable tool for elucidating these mechanisms. By producing P-selectin in a recombinant form, scientists can study its binding interactions, structure, and role in cell adhesion more effectively. This advance allows for the potential development of P-selectin inhibitors that could be used to modulate immune responses or treat diseases characterized by excessive inflammation. The recombinant protein can also serve as a platform for studying the effects of post-translational modifications and for screening drug candidates that target P-selectin. Overall, the exploration of P-selectin recombinant proteins represents an important avenue in the field of immunology and therapeutic development, with implications for improving patient outcomes in inflammatory and malignant conditions.
