Interleukin 16, also named lymphocyte chemoattractant factor (LCF), was originally identified as a CD8+ T-cell-derived chemoattractant for CD4+ cells. The biologically active form of IL-16 was originally proposed to be a homotetramer of 14 kDa chains containing 130 amino acid residue subunits. The complete pro-IL-16 cDNA was subsequently cloned and shown to encode a 631 amino acid residue hydrophilic protein that lacked a signal peptide. The original 130 amino acid residue polypeptide is now believed to have been derived from the C terminus of the precursor. IL-16 precursor protein has been detected in the lysates of various cells including mitogen stimulated PBMCs. The biologically active and secreted natural IL-16 is assumed to be a proteolytic cleavage product of pro-IL-16 generated by proteases present in or on activated CD8+ cells. A likely cleavage site was proposed to be at aspartate residue 510. This would yield a 121 amino acid residue protein, smaller than the 130 aa residue protein first described. The expression of IL-16 precursor mRNA has been detected in various tissues including spleen, thymus, lymph nodes, peripheral leukocytes, bone marrow, and cerebellum. The gene for IL-16 precursor has been localized to chromosome 15. The biological activities ascribed to IL-16 are reported to be dependent on the cell surface expression of CD4, suggesting that IL-16 is a CD4 ligand. Besides its chemotactic properties, IL-16 has also been shown to suppress HIV-1 replication in vitro. Recombinant E. coli-derived IL-16 produced at R&D Systems is present mostly as a monomer, exhibits chemotactic activity for lymphocytes at high concentrations, lacks chemotactic activites for monocytes, and binds the extracellular domain of CD4 with low affinity.
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Zhou, A. et al. (1997) Nature Medicine 3:659.
Bazan, J.F. and T.J. Schall (1996) Nature 381:29.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
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