SLPI Protein, Mouse (HEK293, Fc)

The jGranzyme B/GZMB protein is an abundant protease found in the cytosolic granules of cytotoxic T-cells and NK-cells. It plays a crucial role in various cellular processes. When delivered into the target cell through the immunological synapse, Granzyme B/GZMB activates caspase-independent pyroptosis, leading to target cell death. It achieves this by cleaving after Asp and catalyzing the cleavage of gasdermin-E (GSDME), releasing the pore-forming component of GSDME, which triggers pyroptosis. Granzyme B/GZMB is also involved in the activation cascade of caspases, including caspase-3, -9, and -7, which are responsible for apoptosis execution and plasma membrane repair in response to bacterial infection. Moreover, the Acid-stable proteinase inhibitor SLPI Protein exhibits strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G. It modulates the innate immune response after bacterial infection and contributes to regulating the inflammatory and immune responses to the intracellular parasite L.major. SLPI Protein also down-regulates responses to bacterial lipopolysaccharide (LPS) and plays a role in regulating the activation of NF-kappa-B and inflammatory responses. Additionally, it has antimicrobial activity against mycobacteria, contributes to normal resistance against infection by M.tuberculosis, and is required for normal resistance to L.major. SLPI Protein is also involved in wound healing by preventing tissue damage through limiting protease activity. It interacts with GRN and this interaction protects progranulin from proteolysis.