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.
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Clone
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CBRM1/5
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Format: |
SAFIRE Purified
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Applications
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FC, FA
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Reactivity
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Human
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Isotype:
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Mouse IgG1, kappa
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Preperation:
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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.
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Formulation:
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Phosphate-buffered aqueous solution, ph7.2.
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References:
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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. |