Invitrogen™ CD11a (LFA-1alpha) Monoclonal Antibody (HI111), eBioscience™, Invitrogen™

Description

Description: The HI111 monoclonal antibody reacts with human CD11a, the 180 kDa integrin alphaL, also known as the lymphocyte function associated antigen-1 (LFA-1) alpha chain. LFA-1, formed by non-covalent association of CD11a with CD18 (integrin beta2), serves as an important adhesion molecule involved in lymphocyte and granulocyte function. CD54 (ICAM-1), CD102 (ICAM-2), and CD50 (ICAM-3) are ligands for LFA-1. CD11a is expressed by all leukocytes. Applications Reported: This HI111 antibody has been reported for use in flow cytometric analysis, and immunohistology staining of frozen tissue sections. It has also been reported in blocking of CD11a function in mixed lymphocyte reactions. (Please use Functional Grade purified HI111, cat. 16-0119, in functional assays.). Applications Tested: The HI111 antibody has been tested by flow cytometric analysis of normal human peripheral blood cells. This can be used at less than or equal to 1 μg per test. A test is defined as the amount (μg) of antibody that will stain a cell sample in a final volume of 100 μL. Cell number should be determined empirically but can range from 10^5 to 10^8 cells/test. It is recommended that the antibody be carefully titrated for optimal performance in the assay of interest. Purity: Greater than 90%, as determined by SDS-PAGE. Aggregation: Less than 10%, as determined by HPLC. Filtration: 0.2 μm post-manufacturing filtered.

CD11a (LFA-1 alpha, ITGAL) together with CD18 constitute leukocyte function-associated antigen 1 (LFA-1), the alphaLbeta2 integrin. CD11a is implicated in activation of LFA-1 complex. CD11a plays a central role in leukocyte intercellular adhesion through interactions with its ligands, ICAMs 1-3 (intercellular adhesion molecules 1 through 3), and also functions in lymphocyte costimulatory signaling. CD11a 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 CD11a to its ligands, the intercellular adhesion molecules ICAM-1, -2, -3. CD11a 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 CD11a function by specific antibodies or small molecules has become an important therapeutic approach in treatment of multiple inflammatory diseases. For example, humanized anti- CD11a 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. Two transcript variants encoding different isoforms of CD11a have been found. Diseases associated with CD11a dysfunction include benign cephalic histiocytosis and leukocyte adhesion deficiency.