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.
Preparation and Storage
Reconstitute at 0.5 mg/mL in sterile PBS.
Reconstitution Buffer Available
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
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.
Cruikshank, W.W. et al. (1994) Proc. Natl. Acad. Sci. USA 91:5109.
Baier, M. et al. (1997) Proc. Natl. Acad. Sci. USA 94:5273.
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