CD11a (LFA-1 alpha) together with CD18 constitute leukocyte function-associated antigen 1 (LFA-1), the alphaLbeta2 integrin. CD11a is implicated in activation of LFA-1 complex. LFA-1 is expressed on the plasma membrane of leukocytes in a low-affinity conformation. Cell stimulation by chemokines or other signals leads to induction the high-affinity conformation, which supports tight binding of LFA-1 to its ligands, the intercellular adhesion molecules ICAM-1, -2, -3. LFA-1 is thus involved in interaction of various immune cells and in their tissue-specific settlement, but participates also in control of cell differentiation and proliferation and of T-cell effector functions. Blocking of LFA-1 function by specific antibodies or small molecules has become an important therapeutic approach in treatment of multiple inflammatory diseases. For example, humanized anti-LFA-1 antibody Efalizumab (Raptiva) is being used to interfere with T cell migration to sites of inflammation, binding of cholesterol-lowering drug simvastatin to CD11a allosteric site leads to immunomodulation and increase in lymphocytic cholinergic activity.
Clonality:
Monoclonal
Concentration:
1 mg/ml
Clone Designation:
[MEM-83]
Isotype:
Mouse IgG1
Buffer:
Phosphate buffered saline (PBS), pH 7.4
Storage:
2°C to 8°C
Target:
CD11a
Antibody Type:
Monoclonal Antibody
Application Notes:
Functional application: The antibody MEM-83 directly induces the binding of T cells to purified ICAM-1. Using an in vitro-translated CDlla cDNA deletion series, the MEM-83 activation epitope was mapped to the I domain of the LFA-1 alpha subunit. The studies have therefore identified a novel LFA-1 activation epitope mapping to the I domain of LFA-1, which could play a role in the regulation of LFA-1 binding to ICAM-1. Flow cytometry: Recommended dilution: 1 µg/ml.
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