IL 16 Human, His

Interleukin-16 Human Recombinant, His Tag, is produced in Escherichia coli (E. coli) as a single, non-glycosylated polypeptide chain. This recombinant protein contains 150 amino acids and has a molecular mass of approximately 15.5 kDa . The IL-16 protein is fused to a 20 amino acid His-Tag at the N-terminus, which facilitates its purification through affinity chromatography .

IL-16 undergoes proteolytic processing, resulting in two functional proteins. The secreted C-terminal peptide is primarily responsible for the cytokine’s functions, while the N-terminal product may play a role in cell cycle control . Caspase 3 is reported to be involved in this proteolytic processing .

IL-16 stimulates a migratory response in CD4+ lymphocytes, monocytes, and eosinophils. It also induces T-lymphocyte expression of the interleukin-2 receptor, which is crucial for T cell proliferation and activation .

Recombinant IL-16 is used extensively in laboratory research to study its role in immune responses and its potential therapeutic applications. The protein is typically stored at 4°C for short-term use (2-4 weeks) and at -20°C for long-term storage to maintain its stability .