Description
Research Area: Cell SignalingDipeptidyl peptidase I (DPPI), also known as cathepsin C, is an abundant lysosomal cysteine protease from the papain superfamily with a molecular weight of approximately 200 kDa. It is widely expressed in a variety of mammalian tissues, with the highest levels found in the lungs, kidneys, liver, and spleen, and relatively lower levels in the brain.DPPI is the only member of its family that is functional as a tetramer, consisting of four identical subunits, each composed of an N-terminal fragment, a heavy chain, and a light chain. It is identified as one of the multifaceted protease-processing machines, having been shown to function beyond its role as a non-specific lysosomal protease.ApplicationCathepsin C from bovine spleen has been used for the in vitro enzyme activity assays.[3] It has also been used as a digestion enzyme for in vitro myelin oligodendrocyte glycoprotein (MOG) digestion.Cathepsin C has been used in a study that demonstrated the potential of a proteomics approach to identify novel proteins expressed by extravillous trophoblast and to uncover the mechanisms leading to disease states in pregnancy. Cathepsin C has also been used in a study to evaluate biodegradable thermogels.The enzyme has been used in the activation of granzyme k (Gzmk) precursor from E. coli. Granzymes are granule-stored lymphocyte serine proteases that are implicated in T- and natural killer cell-mediated cytotoxic defense reactions.CautionUnstable. Keep frozen.Physical formLyophilized from a 1 M sodium chloride solution