|Detection of Human IL‑16 by Western Blot. Western blot shows lysate of human tonsil tissue. PVDF membrane was probed with 2 µg/mL of Mouse Anti-Human IL‑16 Monoclonal Antibody (Catalog # MAB316) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF018). Specific bands were detected for IL‑16 at approximately 45-55 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
Detection of Human IL‑16 by Simple WesternTM. Simple Western lane view shows lysates of human tonsil tissue, loaded at 0.2 mg/mL. A specific band was detected for IL‑16 at approximately 50 kDa (as indicated) using 20 µg/mL of Mouse Anti-Human IL‑16 Monoclonal Antibody (Catalog # MAB316). This experiment was conducted under reducing conditions and using the |
12-230 kDa separation system.
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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