Description
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.
Product Properties
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Synonyms |
Interleukin-16 isoform 2, Lymphocyte chemoattractant factor, LCF |
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Accession |
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GeneID |
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Source |
E.coli-derived human IL-16 protein,Met1203-Ser1332,with an N-terminal Met. |
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Molecular Weight |
Approximately 13.4 kDa. |
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AA Sequence |
MPDLNSSTDS AASASAASDV SVESTAEATV CTVTLEKMSA GLGFSLEGGK GSLHGDKPLT INRIFKGAAS EQSETVQPGD EILQLGGTAM QGLTRFEAWN IIKALPDGPV TIVIRRKSLQ SKETTAAGDS |
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Tag |
None |
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Physical Appearance |
Sterile Filtered White lyophilized (freeze-dried) powder. |
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Purity |
> 95% by SDS-PAGE and HPLC analyses. |
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Biological Activity |
Fully biologically active when compared to standard. The biological activity determined by a chemotaxis bioassay using human CD4+ T Lymphocytes is in a concentration range of 1.0-100 ng/ml. |
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Endotoxin |
< 1.0 EU per 1μg of the protein by the LAL method. |
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Formulation |
Lyophilized from a 0.2 µm filtered concentrated solution in 20 mM Tris, 150 mM NaCl, pH 7.0. |
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Reconstitution |
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions. |
Shipping and Storage
The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year.
Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.
Cautions
1. Avoid repeated freeze-thaw cycles.
2. For your safety and health, please wear lab coats and disposable gloves for operation.
3. For research use only.
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