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Basiliximab recognises the human IL-2R and binds to the epitope (116)ERIYHFV(122) within the extracellular domain of the CD25 subunit - binding is abolished when 2 or more residues within the epitope are mutated. This epitope overlaps with the interaction site of CD25 and IL-2. CD25 is found in the high-affinity IL-2R ( alpha Beta Gammac) - T cells only express CD25 upon activation. IL-2 binding to IL-2R on T cells modulates proliferation and differentiation.
A recombinant chimeric (murine/human) monoclonal antibody (IgG1k) that functions as an immunosuppressive agent, specifically binding to and blocking the interleukin-2 receptor a-chain (IL-2R alpha, also known as CD25 antigen) on the surface of activated T-lymphocytes. It is a 144 kDa glycoprotein obtained from fermentation of an established mouse myeloma cell line genetically engineered to express plasmids containing the human heavy and light chain constant region genes and mouse heavy and light chain variable region genes encoding the RFT5 antibody that binds selectively to the IL-2R alpha. Basiliximab binds with high-affinity to the alpha-subunit (CD25) of the high-affinity IL-2 receptor. This inhibits IL-2 binding, which inhibits T-cell activation and prevents the body from mounting an immune response against the foreign kidney.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein Aliases: CHI621
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