Anti-Hu CD62P PE-Cy™5

CD62P (P-selectin) is an adhesion glycoprotein that is expressed on platelets and endothelial cells upon their activation. Interaction between CD62P and its mucin-like ligand PSGL-1 (P-selectin glycoprotein ligand-1) expressed on the microvilli of most leukocytes supports leukocyte rolling along postkapillary venules at the earliest time of inflammation. Both CD62P and PSGL-1 are extended glycoproteins that form homodimers. CD62P dimerization is probably mediated through interactions of the transmembrane domains and stabilizes leukocyte tethering and rolling, probably by increasing rebinding within a bond cluster.

Product Specifications

Certification

RUO

Reactivity

Human, Non-human primates

Immunogen

Human platelets

Target Antigen

CD62P

Clone

AK4

Applications

FC (QC tested)

Format

PE-Cy

Buffer

Stabilizing phosphate buffered saline (PBS), pH 7.4, 15 mM sodium azide

References & Citations

*Skinner MP, Lucas CM, Burns GF, Chesterman CN, Berndt MC: GMP-140 binding to neutrophils is inhibited by sulfated glycans. J Biol Chem. 1991 Mar 25;266 (9) :5371-4., URL: http://www.ncbi.nlm.nih.gov/pubmed/?term=skinner+mp+lucas+cm+burns+gf , *Ludwig RJ, Schultz JE, Boehncke WH, Podda M, Tandi C, Krombach F, Baatz H, Kaufmann R, von Andrian UH, Zollner TM: Activated, not resting, platelets increase leukocyte rolling in murine skin utilizing a distinct set of adhesion molecules. J Invest Dermatol. 2004 Mar;122 (3) :830-6., URL: http://www.ncbi.nlm.nih.gov/pubmed/15086572 , *Kowalska MA, Ratajczak J, Hoxie J, Brass LF, Gewirtz A, Poncz M, Ratajczak MZ: Megakaryocyte precursors, megakaryocytes and platelets express the HIV co-receptor CXCR4 on their surface: determination of response to stromal-derived factor-1 by megakaryocytes and platelets. Br J Haematol. 1999 Feb;104 (2) :220-9., URL: https://www.ncbi.nlm.nih.gov/pubmed/10050701, *Holme PA, Müller F, Solum NO, Brosstad F, Frøland SS, Aukrust P: Enhanced activation of platelets with abnormal release of RANTES in human immunodeficiency virus type 1 infection. FASEB J. 1998 Jan;12 (1) :79-89., URL: https://www.ncbi.nlm.nih.gov/pubmed/9438413, *Dunlop LC, Skinner MP, Bendall LJ, Favaloro EJ, Castaldi PA, Gorman JJ, Gamble JR, Vadas MA, Berndt MC: Characterization of GMP-140 (P-selectin) as a circulating plasma protein. J Exp Med. 1992 Apr 1;175 (4) :1147-50., URL: https://www.ncbi.nlm.nih.gov/pubmed/1372646, *Skinner MP, Lucas CM, Burns GF, Chesterman CN, Berndt MC: GMP-140 binding to neutrophils is inhibited by sulfated glycans. J Biol Chem. 1991 Mar 25;266 (9) :5371-4., URL: http://www.ncbi.nlm.nih.gov/pubmed/?term=skinner+mp+lucas+cm+burns+gf

Other References

*Harakawa N, Shigeta A, Wato M, Merrill-Skoloff G, Furie BC, Furie B, Okazaki T, Domae N, Miyasaka M, Hirata T. P-selectin glycoprotein ligand-1 mediates L-selectin-independent leukocyte rolling in high endothelial venules of peripheral lymph nodes. Int Immunol. 2007 Mar;19 (3) :321-9., URL: https://www.ncbi.nlm.nih.gov/pubmed/17267415?ordin, *Martinez M, Joffraud M, Giraud S, Baïsse B, Bernimoulin MP, Schapira M, Spertini O: Regulation of PSGL-1 interactions with L-selectin, P-selectin, and E-selectin: role of human fucosyltransferase-IV and -VII. J Biol Chem. 2005 Feb 18;280 (7) :5378-90., URL: https://www.ncbi.nlm.nih.gov/pubmed/15579466?ordin, *Ramachandran V, Williams M, Yago T, Schmidtke DW, McEver RP: Dynamic alterations of membrane tethers stabilize leukocyte rolling on P-selectin. Proc Natl Acad Sci U S A. 2004 Sep 14;101 (37) :13519-24., URL: https://www.ncbi.nlm.nih.gov/pubmed/15353601?ordin, *Ramachandran V, Yago T, Epperson TK, Kobzdej MM, Nollert MU, Cummings RD, Zhu C, McEver RP: Dimerization of a selectin and its ligand stabilizes cell rolling and enhances tether strength in shear flow. Proc Natl Acad Sci U S A. 2001 Aug 28;98 (18) :10166-71., URL: https://www.ncbi.nlm.nih.gov/pubmed/11481445?ordin

Storage Conditions

Store at 2-8°C. Protect from prolonged exposure to light. Do not freeze.

Specificity

The antibody AK4 recognizes an extracellular epitope of CD62P (P-selectin), a 140 kD single chain type I transmembrane glycoprotein present in secretory alpha-granules in platelets, in Weibel-Palade bodies in endothelial cells and in megakaryocytes; it is relocated to the plasma membrane upon activation.