Anti-Human CD11b (activation epitope) SAFIRE Purified
The CBRM1/5 monoclonal antibody binds with the 165 kDa human adhesion glycoprotein CD11b, which forms, together with the 95 kDa CD18 (integrin β2) a complex known as Mac-1. CD11b is expressed on the surface of activated lymphocytes, a subset of natural killer cells, granulocytes, and monocytes. It functions as a receptor in cell-cell and cell-matrix interactions and as a receptor for iC3b, ICAM-1, ICAM-2, and ICAM-3 intercellular adhesion molecules. The CBRM1/5 specifically reacts with the activation-specific epitope of the Mac-1 molecule, in the I domain on the alpha chain near the ligand binding site. The antibody has been reported to inhibit the cellular adhesion mediated by Mac-1.
Mouse IgG1, kappa
|Research Interest:||Innate Immunity, Angiogenesis|
|Cell Type:||Macrophage / Monocyte, NK and NKT Cells|
The product should be stored undiluted at 4°C. Do not freeze. The monoclonal antibody was purified utilizing affinity chromatography. The endotoxin level is determined by LAL test to be less than 0.01 EU/µg of the protein.
Phosphate-buffered aqueous solution, ph7.2.
Oxvig, C., Lu, C., & Springer, T. A. (1999). Conformational changes in tertiary structure near the ligand binding site of an integrin I domain. Proceedings of the National Academy of Sciences, 96(5), 2215-2220.
Diamond, M. S., & Springer, T. A. (1993). A subpopulation of Mac-1 (CD11b/CD18) molecules mediates neutrophil adhesion to ICAM-1 and fibrinogen. The Journal of cell biology, 120(2), 545-556.
Shimaoka, M., Shifman, J. M., Jing, H., Takagi, J., Mayo, S. L., & Springer, T. A. (2000). Computational design of an integrin I domain stabilized in the open high affinity conformation. Nature Structural & Molecular Biology, 7(8), 674-678.