Fagus Antibody Services

Recombinant Human P-selectin/CD62P (C-6His)

£74.40£221.60 excluding VAT

P-selectin/CD62P is a single-pass type I membrane protein which is a member of the Selectin family. It consists 768 amino acid (aa). P-selectin is a cell surface glycoprotein expressed by activated platelets and endothelial cells. It induced expression in lung, liver, kidney and heart after endotoxin treatment. Ca2+-dependent receptor for myeloid cells that binds to carbohydrates on neutrophils and monocytes. It mediates the interaction of activated endothelial cells or platelets with leukocytes. The ligand recognized is sialyl-Lewis X. it also mediates rapid rolling of leukocyte rolling over vascular surfaces during the initial steps in inflammation through interaction with PSGL1. P-selectin interacts with SNX17, PSGL1/SEPL, PODXL2, mediates neutrophil adhesion and leukocyte rolling. This interaction requires the sialyl-Lewis X epitope of PSGL1 and PODXL2, and specific tyrosine sulfation on PSGL1.

Size

10µg, 50µg

Active Protein
Activity
Protein Construction

Recombinant Human P-selectin is produced by our Mammalian expression system and the target gene encoding Trp42-Ala771 is expressed with a 6His tag at the C-terminus.

Sequence

Trp42-Ala771

Fusion Tag

C-6His

Accession

P16109

Species

Human

Expressed Host

Human Cells

Shipping

This product is provided as lyophilized powder which is shipped with ice packs.

Purity

> 95 % as determined by reducing SDS-PAGE.

Endotoxin

< 1.0 EU per µg as determined by the LAL method.

Stability and Storage

Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

Mol Mass

80.8 kDa

AP Mol Mass

110-130 kDa

Formulation

Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.

Research Areas

Cardiovascular, immunology, Stem cells

Reconstitution

Please refer to the printed manual for detailed information.

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