IL 16 Rhesus Macaque

Recombinant Rhesus Macaque Interleukin-16 (rrmIL-16) is a form of IL-16 that has been produced using recombinant DNA technology. This involves inserting the gene encoding IL-16 into a host organism, such as Escherichia coli (E. coli), to produce the protein in large quantities . The recombinant protein is then purified using various chromatographic techniques to ensure high purity and biological activity .

The recombinant rhesus macaque IL-16 is a single, non-glycosylated polypeptide chain containing 121 amino acids and has a molecular weight of approximately 12.5 kDa . The amino acid sequence of rrmIL-16 shares 85% to 95% identity with human and murine IL-16, making it a valuable tool for comparative studies and research .

The protein is typically lyophilized (freeze-dried) for stability and can be reconstituted in sterile distilled water or an aqueous buffer containing 0.1% bovine serum albumin (BSA) to a concentration of 0.1-1.0 mg/mL . Upon reconstitution, the preparation is stable for up to one week at 2-8°C and for long-term storage at -20°C to -80°C .

Recombinant rhesus macaque IL-16 is fully biologically active when compared to the standard IL-16. Its biological activity is determined by a chemotaxis bioassay using human peripheral T lymphocytes, with an effective concentration range of 1.0-100 ng/mL . The protein signals through the CD4 receptor, similar to its human counterpart .

Recombinant IL-16 is used extensively in immunological research to study its role in immune responses and its potential therapeutic applications. It is particularly useful in studying the mechanisms of T-cell activation, chemotaxis, and the suppression of viral replication . Additionally, due to its high sequence identity with human IL-16, rrmIL-16 serves as a valuable model for understanding the function and regulation of IL-16 in humans .