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Explore how neutrophils shape the immune response in health and disease. This poster highlights neutrophil pathogen defense mechanisms, including phagocytosis, degranulation, and NETosis, as well as neutrophil roles in inflammation and NET-associated pathologies.
DOWNLOAD NOWP-selectin, also known as CD62P, is a glycoprotein and cell adhesion molecule that is encoded by Selp in mice.1 It is a homodimer and is composed of an N-terminal calcium-dependent lectin domain that recognizes glycoproteins, an EGF-like domain, nine consensus repeats, a transmembrane domain, and an intracellular C-terminal tail. P-selectin is expressed in platelets, endothelial cells, and macrophages, is stored in α-granules of platelets, and localizes to the plasma membrane upon platelet activation.2,3,1 It also exists as a soluble form that results from alternative splicing of SELP.1 P-selectin is involved in tethering and rolling of leukocytes during inflammation and tissue healing mediated by binding to P-selectin glycoprotein ligand-1 (PSGL-1), a mucin expressed on the surface of leukocytes.1,4 Selp knockout delays fatty streak formation and progression to the fibrous plaque stage in LDL receptor-deficient mice fed an atherogenic diet.5 It also delays aortic lesion progression in ApoE-/- mice.6 Cayman's P-Selectin/CD62P (mouse, recombinant) protein can be used for cell-based assays. This protein consists of 679 amino acids, has a calculated molecular weight of 74 kDa, and a predicted N-terminus of Trp42 after signal peptide cleavage. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is 116 kDa due to glycosylation.
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1. Selectins-
2. Differential regulation of human and murine P-
3. Platelet dense granule membranes contain both granulophysin and P-
4. Selectins: Initiators of leucocyte adhesion and signalling at the vascular wall. Cardiovasc. Res. 107(3), 331-339 (2015).
5. Absence of P-
6. Prominent role of P-