- Functional Application
The antibody MEM-115 blocks binding of HIV gp120 to CD4 molecule and it also strongly inhibits CD4-MHC Class II interactions.
- Flow Cytometry
Recommended dilution:3 μg/ml
Although it has not been tested rigorously, following data suggest that the antibody MEM-115 is a low-affinity antibody: its binding to T cells increases at elevated temperature; monovalent Fab fragments essentially do not bind to T cells.
Indicated dilutions are recommended starting points for use of this product. Working concentrations should be determined by the investigator.
*Millan J, Cerny J, Horejsi V, Alonso MA: CD4 segregates into specific detergent-resistant T-cell membrane microdomains. Tissue Antigens. 1999 Jan;53(1):33-40. [Abstract]
*Foti M, Phelouzat MA, Holm A, Rasmusson BJ, Carpentier JL: p56Lck anchors CD4 to distinct microdomains on microvilli. Proc Natl Acad Sci U S A. 2002 Feb 19;99(4):2008-13. [Abstract] [Full Text]
Clapham PR, McKnight A.: Cell surface receptors, virus entry and tropism of primate lentiviruses. J Gen Virol. 2002 Aug;83(Pt 8):1809-29. [Abstract] [Full Text]
Product Specific References
*Leukocyte Typing V., Schlossman S. et al. (Eds.), Oxford University Press (1995).
*Brdicková N, Brdicka T, Angelisová P, Horváth O, Spicka J, Hilgert I, Paces J, Simeoni L, Kliche S, Merten C, Schraven B, Horejsí V: LIME: a new membrane Raft-associated adaptor protein involved in CD4 and CD8 coreceptor signaling. J Exp Med. 2003 Nov 17;198(10):1453-62. [Abstract] [Full Text]
*Bosze S, Caccamo N, Majer Z, Mezo G, Dieli F, Hudecz F: In vitro T-cell immunogenicity of oligopeptides derived from the region 92-110 of the 16-kDa protein of Mycobacterium tuberculosis. Biopolymers. 2004;76(6):467-76. [Abstract]
*Singer II, Scott S, Kawka DW, Chin J, Daugherty BL, DeMartino JA, DiSalvo J, Gould SL, Lineberger JE, Malkowitz L, Miller MD, Mitnaul L, Siciliano SJ, Staruch MJ, Williams HR, Zweerink HJ, Springer MS: CCR5, CXCR4, and CD4 are clustered and closely apposed on microvilli of human
macrophages and T cells. [Abstract] [Full Text]