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Summary This antibody recognizes membrane-bound form of HLA-G (full-length HLA-G1), but not soluble forms.
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Summary The monoclonal antibody HM102 recognizes the extracellular part of membrane-bound TNF-RII as well as the soluble form of TNF-RII which is generated by proteolytic cleavage of the extracellular domain. The soluble form can still bind TNF-alpha with high affinity and functions as a TNF-alpha antagonist. The antibody is a agonistic receptor modulating antibody. It enhances in vitro TNF alpha responses by increasing the affinity of the soluble form of TNF-alpha for TNF-RII.

Summary The antibody binds to the beta chain, recognising an epitope that is dependent upon expression of both CD8 alpha and CD8 beta.

Summary The CRA1 (AER37) monoclonal antibody reacts with the Fc epsilon R1 alpha subunit on a region that does not overlap the region of the IgE binding site, thus it does not compete withIgE for the receptor binding. Since the CRA2 (AER24) monoclonal antibody reacts with the IgE binding site on Fc epsilon R1 alpha, it competes with IgE for the receptor binding. Combining the two antibodies, one can quantitatively measure the amounts of the IgE-bound Fc epsilon R1 alpha.

Summary This antibody recognizes a determinant on thymocytes and peripheral T-cells but it does not bind to B cells or peritoneal macrophages.