Human IL-16 Alexa Fluor® 405-conjugated Antibody
Human IL-16 Alexa Fluor® 405-conjugated Antibody Summary
Accession # Q14005
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Preparation and Storage
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.
- Zhou, A. et al. (1997) Nature Medicine 3:659.
- Bazan, J.F. and T.J. Schall (1996) Nature 381:29.
Product Specific Notices
This product is provided under an agreement between Life Technologies Corporation and R&D Systems, Inc, and the manufacture, use, sale or import of this product is subject to one or more US patents and corresponding non-US equivalents, owned by Life Technologies Corporation and its affiliates. The purchase of this product conveys to the buyer the non-transferable right to use the purchased amount of the product and components of the product only in research conducted by the buyer (whether the buyer is an academic or for-profit entity). The sale of this product is expressly conditioned on the buyer not using the product or its components (1) in manufacturing; (2) to provide a service, information, or data to an unaffiliated third party for payment; (3) for therapeutic, diagnostic or prophylactic purposes; (4) to resell, sell, or otherwise transfer this product or its components to any third party, or for any other commercial purpose. Life Technologies Corporation will not assert a claim against the buyer of the infringement of the above patents based on the manufacture, use or sale of a commercial product developed in research by the buyer in which this product or its components was employed, provided that neither this product nor any of its components was used in the manufacture of such product. For information on purchasing a license to this product for purposes other than research, contact Life Technologies Corporation, Cell Analysis Business Unit, Business Development, 29851 Willow Creek Road, Eugene, OR 97402, Tel: (541) 465-8300. Fax: (541) 335-0354.
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