IL 32A Human

IL-32 exists in several splicing variants, with the alpha isoform (IL-32 alpha) being one of them. The alpha isoform lacks a portion of the putative signal peptide and 57 amino acids from the C-terminal region . This makes IL-32 alpha less potent than other isoforms like IL-32 beta, gamma, or delta in inducing the expression of proinflammatory molecules in peripheral blood mononuclear cells (PBMC) .

IL-32 alpha has been shown to induce the production of proinflammatory cytokines such as IL-8, TNF-alpha, and macrophage inflammatory protein-2 (MIP-2) from human and mouse macrophage cell lines . It is upregulated in activated T cells, NK cells, and interferon-gamma (IFN-gamma)-treated epithelial cells . The activity of IL-32 alpha is measured by its ability to induce TNF-alpha secretion by RAW 264.7 mouse monocyte/macrophage cells under serum-free conditions in the presence of muramyl dipeptide (MDP) .

Recombinant human IL-32 alpha is typically produced in Escherichia coli (E. coli) and is purified to a high degree of purity, often greater than 85% as determined by SDS-PAGE . The recombinant protein is lyophilized from a filtered solution and can be reconstituted in phosphate-buffered saline (PBS) for use in various applications .

Recombinant IL-32 alpha is used in research to study its role in inflammation and immune response. It is also utilized to investigate the signaling pathways involved in the production of other cytokines and to explore potential therapeutic applications in inflammatory diseases .

The recombinant protein is typically stored at -20 to -70°C and should be handled under sterile conditions to maintain its stability. It is recommended to avoid repeated freeze-thaw cycles to preserve its activity .