IL 22 Human

Human recombinant IL-22 (hIL-22) is typically produced in human 293 cells. The recombinant protein is often lyophilized from a filtered solution of phosphate-buffered saline (PBS) and can be reconstituted for use in various assays . The molecular weight of nonglycosylated hIL-22 is approximately 16,749 Da, but due to glycosylation, it migrates as a 34 kDa polypeptide in SDS-PAGE .

IL-22 plays a crucial role in mediating proinflammatory responses, driving the production of antimicrobial peptides, and contributing to tissue repair and wound healing . It exerts its effects by binding to a heterodimeric receptor composed of IL-22R1 and IL-10R2 . The IL-22 receptor is predominantly expressed on tissue-resident cells, particularly those of epithelial origin .

Upon binding to its receptor, IL-22 activates several signaling pathways, including the JAK-STAT pathway (primarily STAT3), as well as the MEK-ERK-RSK, JNK-SAPK, and p38 pathways . These signaling cascades lead to various cellular responses, including the production of antimicrobial peptides and the promotion of cell survival and proliferation .

IL-22 has been studied for its potential therapeutic applications, particularly in the context of epithelial repair and protection against tissue injury . It has shown promise in preclinical models of liver, pancreas, gut, kidney, and lung injuries . Additionally, IL-22 plays a role in host defense against bacterial infections .

The therapeutic potential of IL-22 is further highlighted by its minimal side effects, as it specifically targets epithelial cells without affecting immune cells . Clinical studies have explored the use of IL-22-Fc fusion proteins to enhance its stability and efficacy in vivo .