Anti-CD11b/ITGAM Antibody Picoband® Fluoro647 Conjugated

Integrin alpha M (ITGAM) is one protein subunit that forms the heterodimeric integrin alpha-M beta-2 (αMβ2) molecule, also known as macrophage-1 antigen (Mac-1) or complement receptor 3 (CR3) . It is mapped to 16p11.2. ITGAM has a role in vascular repair after mechanical arterial injury. It is implicated in various adhesive interactions of monocytes, macrophages and granulocytes as well as in mediating the uptake of complement-coated particles. What's more, ITGAM probably recognizes the R-G-D peptide in C3b, and it is also a receptor for fibrinogen, factor X and ICAM1.

Integrin alpha-M; CD11 antigen-like family member B; CR-3 alpha chain; Cell surface glycoprotein MAC-1 subunit alpha; Leukocyte adhesion receptor MO1; Neutrophil adherence receptor; CD11b; ITGAM; CD11B, CR3A

E.coli-derived human CD11b recombinant protein (Position: F17-T382) . Human CD11b shares 79% and 61% amino acid (aa) sequences identity with mouse and rat CD11b, respectively.

Cell Adhesion, Cell Type Marker, Cell Type Markers, Cytoskeleton/ECM, Hematopoietic Progenitors, Integrins, Lymphoid, Mesenchymal Stem Cells, Myeloid, Neuroscience, Signal Transduction, Stem Cells, T Lymphocytic Lineage

Integrin alpha-M/beta-2 is implicated in various adhesive interactions of monocytes, macrophages and granulocytes as well as in mediating the uptake of complement-coated particles. It is identical with CR-3, the receptor for the iC3b fragment of the third complement component. It probably recognizes the R-G-D peptide in C3b. Integrin alpha-M/beta-2 is also a receptor for fibrinogen, factor X and ICAM1. It recognizes P1 and P2 peptides of fibrinogen gamma chain.

1. Arnaout, M. A., Remold-O'Donnell, E., Pierce, M. W., Harris, P., Tenen, D. G. Molecular cloning of the alpha-subunit of human and guinea pig leukocyte adhesion glycoprotein Mo1: chromosomal localization and homology to the alpha-subunits of integrins. Proc. Nat. Acad. Sci. 85: 2776-2780, 1988. 2. Solovjov D, Pluskota E, Plow E (2005) . Distinct roles for the alpha and beta subunits in the functions of integrin alphaMbeta2. J Biol Chem 280 (2) : 1336–45. 3. Simon, D. I., Chen, Z., Seifert, P., Edelman, E. R., Ballantyne, C. M., Rogers, C. Decreased neointimal formation in Mac-1 -/- mice reveals a role for inflammation in vascular repair after angioplasty. J. Clin. Invest. 105: 293-300, 2000.