Greater than 95.0% as determined by SDS-PAGE.
The lyophilization of IL37 was carried out from a 0.2 µM filtered solution containing 20mM PB (phosphate buffer), 150mM NaCl (sodium chloride), and 2mM DTT (dithiothreitol) at a pH of 7.4.
The purity of the IL37 is greater than 95.0%, as determined by SDS-PAGE analysis.
Interleukin-37, formerly known as Interleukin-1 Family Member 7, is a member of the Interleukin-1 family of cytokines. It is a newly discovered cytokine that plays a crucial role in suppressing innate inflammation and acquired immune responses. Interleukin-37 has five isoforms, designated as Interleukin-37a through Interleukin-37e, with Interleukin-37b being the most studied and longest isoform .
Interleukin-37 functions as a natural inhibitor of inflammatory and immune responses. It has been shown to suppress the production of pro-inflammatory cytokines such as Interleukin-1 alpha, Interleukin-1 beta, and Tumor Necrosis Factor alpha. Overexpression of Interleukin-37 in epithelial cells or macrophages almost completely suppresses the production of these cytokines, whereas silencing of endogenous Interleukin-37 increases their abundance in human blood cells .
Due to its potent anti-inflammatory properties, Interleukin-37 holds significant potential for treating a wide array of human inflammatory and autoimmune disorders. Studies have shown that administration of recombinant Interleukin-37 can ameliorate experimental psoriasis, alleviate rheumatoid arthritis, and reduce bleomycin-induced lung injury and fibrosis. It has also been found to decrease renal ischemia-reperfusion injury and inhibit the growth of cancer cells .
Recombinant Interleukin-37 can be produced using various expression systems, including bacterial, yeast, insect, and mammalian cells. Recently, plants have emerged as a novel expression platform for the production of human Interleukin-37. Transgenic plants have been developed to produce different forms of Interleukin-37b, including the unprocessed full-length precursor form and the mature form. The expression of these forms is driven by a strong constitutive promoter, and the resulting proteins are biologically active .