Recombinant Human P-Selectin Protein (Fc Tag)

Name: Recombinant Human P-Selectin Protein (Fc Tag)
Brand: Beta LifeScience
SKU: BLPSN-3927
Availability: InStock

Collections: Antibody / cell therapy targets, Antibody therapeutic / adc target proteins, Recombinant proteins

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Tag	Fc
Host Species	Human
Accession	AAN06828.1
Synonym	CD62, CD62P, GMP140, GRMP, LECAM3, P-Selectin, PADGEM, PSEL
Background	P selectin (SELP) is a 14kDa protein that is stored in the alpha-granules of platelets and Weibel-Palade bodies of endothelial cells. SELP mediates rapid rolling of leukocyte rolling over vascular surfaces during the initial steps in inflammation through interaction with PSGL1. P selectin is a cell adhesion molecule on the surface of activated endothelial cells. Cellular adhesion molecules are a large family of proteins that attach the cytoskeleton and intracellular signaling cascades with the extracellular environment. SELP is a calcium-dependent receptor for myeloid cells that binds to sialylated forms of Lewis blood group carbohydrate antigens on neutrophils and monocytes. This protein redistributes to the plasma membrane during platelet activation and degranulation and mediates the interacton of activated endothelial cells or platelets with leukocytes.
Description	A DNA sequence encoding the human SELP (AAN06828.1) extracellular domain (Met 1-Ala 771) was fused with the Fc region of human IgG1 at the C-terminus.
Source	HEK293
Predicted N Terminal	Trp 42
AA Sequence	Met 1-Ala 771
Molecular Weight	The recombinant human SELP/Fc is a disulfide-linked homodimeric protein. The reduced monomer consists of 971 a.a. and has a predicted molecular mass of 107 kDa. The apparent molecular mass of the reduced monomer is approximately 130-150 kDa in SDS-PAGE under reducing conditions due to glycosylation.
Purity	>85% as determined by SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	Measured by the ability of the immobilized protein to support the adhesion of U937 human histiocytic lymphoma cells. When 5 x 10E4 cells/well are added to SELP/Fc Chimera coated plates (10 ug/mL with 100 uL/well), > 80% cells will adhere after 1 hour at 37°C.
Formulation	Lyophilized from sterile PBS, pH 7.4.
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.