SLPI Protein, Human (HEK293, Fc)

SLPI, an acid-stable proteinase inhibitor, exhibits robust affinities for trypsin, chymotrypsin, elastase, and cathepsin G, as demonstrated in various studies. It plays a crucial role in modulating inflammatory and immune responses following bacterial infection, as well as infection by the intracellular parasite L.major. Additionally, SLPI contributes to down-regulating responses to bacterial lipopolysaccharide (LPS) (By similarity) and is involved in regulating the activation of NF-kappa-B, thereby influencing inflammatory responses. Notably, SLPI exhibits antimicrobial activity against mycobacteria but not against salmonella, contributing to normal resistance against infection by M.tuberculosis. It is also essential for normal resistance to infection by L.major and plays a critical role in wound healing, likely by preventing tissue damage through the regulation of protease activity (By similarity). Furthermore, in collaboration with ELANE, SLPI is required for the normal differentiation and proliferation of bone marrow myeloid cells, and it interacts with GRN, protecting progranulin from proteolysis.