Phosphate-buffered solution, pH 7.2, containing no preservative. 0.2 μm filter sterilized. Endotoxin level is < 0.1 EU/μg of the protein (< 0.01 ng/μg of the protein) as determined by the LAL test.
Preparation:
The LEAF™ (Low Endotoxin, Azide-Free) antibody was purified by affinity chromatography.
Storage & Handling:
The antibody solution should be stored undiluted at 4 °C. This LEAF™ solution contains no preservative; handle under aseptic conditions.
Application:
FC - Quality tested IP*, Blocking*, Depletion*, IHC(Frozen)*, IF* - *Reported in the literature.
Recommended Usage:
Each lot of this antibody is quality control tested by immunofluorescent staining with flow cytometric analysis. For immunofluorescent staining, the suggested use of this reagent is ≤ 0.25 µg per 106 cells in 100 µl volume. It is recommended that the reagent be titrated for optimal performance for each application.
Application Notes:
Additional reported applications (for relevant formats of this clone) include:immunoprecipitation1, 4, in vitro blocking3, 9, 12, depletion2, 8,immunofluorescence microscopy6, 7, 10 and immunohistochemistry of acetone-fixed frozen sections5, 11-13.
Application References:
1. Springer, T., et al., 1978. Eur. J. Immunol. 8:539. (IP) 2. Ault, K., Springer, T., 1981. J. Immunol. 126:359. (Deplete) 3. Springer, T.A., et al., 1982. Immunol. Rev. 68:171. (Block) 4. Ho, MK., Springer, TA., 1983. J Biol Chem. 258:2766. (IP) 5. Flotte, T.J., et al., 1983. Am. J. Pathol. 111:112. (IHC) 6. Noel GJ et al 1990 J Clin Invest. 85:208. (IF) 7. Allen, LA., Aderem, A., 1996. J Exp Med. 184:627 (IF) 8. D'Amico, A., Wu, L., 2003. J. Exp. Med. 198:293. (Deplete) 9. Brickson, SJ., et al., 2003. Appl Physiol. 95:969. (Block) 10. Clatworthy MR, Smith KG. 2004. J Exp Med. 199:717. (IF) 11. Hata, H., et al., 2004. J. Clin. Invest. 114:582. (IHC) 12. Zhang, Y., et al., 2002. J. Immunol. 168: 3088. (IHC) 13. Iwasaki, A., Kelsall, BL., 2001. J Immunol 166:4884 (IHC, FC) 14. Tailleux L 2003 J Exp Med 197:121. (Block, FC) 15. Olver, S., et al., 2006. Cancer Research 66:571. (FC) 16. Tan, SL., et al., 2006. J. Immunol. 176:2872. (FC) PubMed 17. Ponomarev, E. D., et al., 2006. J. Immunol. 176:1402. (FC) 18. Dzhagalov, I., et al., 2007. Blood 109:1620. (FC) 19. Fazilleau, N., et al., 2007. Nature Immunol. 8:753. 20. Rasmussen, J.W., et al., 2006. Infect. Immun.74:6590. PubMed 21. Napimoga, MH.,et al., 2008. J. Immunol. 180:609. PubMed 22. Elqaraz-Carmon, V., et al., 2008. J Lipid Res. PubMed 23. Kim DD., et al. 2008. Blood.PubMed 24. Guo, Y., et al., 2008. Blood. 112:480. PubMed 25. Norian, LA., et al., 2009. Cancer Res. 69:3086. (FC) PubMed 26. Baumgartner, C.K., et al., 2010. J. Immunol. 184:573. PubMed 27. Charles, N., et al., 2010. Nat. Med. 16:701. (FC) PubMed
C57BL/6 mouse bone marrow cells stained with LEAF™ purified M1/70, followed by anti-rat IgGs FITC
Description:
CD11b is a 170 kD glycoprotein, also known as αM integrin, Mac-1 α subunit, Mol, CR3, or Ly-40. CD11b is a member of the integrin family, primarily expressed on granulocytes, monocytes/macrophages, NK cells, and some T and B cells. CD11b non-covalently associates with CD18 (β2 integrin) to form Mac-1. Mac-1 plays an important role in cell-cell interaction by binding its ligands ICAM-1 (CD54), ICAM-2 (CD102), ICAM-4 (CD242), iC3b, and fibrinogen. The M1/70 antibody can block CD11b-mediated cellular adhesion. This antibody is also cross-reactive with human CD11b.
Other Names:
αM integrin, Mac-1, Mo1, CR3, Ly-40, C3biR
Structure:
Integrin family, associates with integrin ß2 (CD18), 170 kD
Distribution:
Granulocytes, monocytes, NK cells, some T and B cells
