Cathepsin S, human

Cathepsin S, human (CTSS) mediates invariant chain cleavage to enable MHC-II maturation and antigen presentation, and enhances the migration of dendritic cells; these processes occur in human antigen-presenting cells including dendritic cells, monocytes, lymphocytes and splenocytes^[1].
Cathepsin S, human activates PAR2 via a unique cleavage site, thereby triggering calcium mobilization, ERK1/2 activation, β-arrestin recruitment and endocytosis, and drives inflammatory responses in human cells expressing PAR2^[1].
Cathepsin S, human promotes NF-κB-dependent inflammatory responses in the liver by degrading SIRT1, whereas inhibition of CTSS stabilizes SIRT1 and thereby suppresses NF-κB in human hepatocytes^[1].
Cathepsin S, human regulates the activity of various human protein substrates with distinct physiological and pathological functions via proteolytic cleavage^[2].
Cathepsin S, human promotes adipogenic differentiation of preadipocytes, whereas inhibition of Cathepsin S reduces lipid content and the expression of adipocyte markers in differentiated adipocytes^[3].
Cathepsin S, human cleaves Myelin basic protein (HY-P1821) in vitro^[3].
Cathepsin S, human cleaves secretory leukocyte protease inhibitor in vitro^[3].
Cathepsin S, human degrades defensins in vitro^[3].
Cathepsin S, human degrades surfactant protein A in vitro^[3].
Cathepsin S, human proteolytically processes Amiloride (HY-B0285)-sensitive epithelial sodium channels in vitro^[3].
Cathepsin S, human releases the pro-angiogenic γ2 peptide from laminin-5 in vitro^[3].
Cathepsin S, human releases endostatin from type XVII collagen in vitro^[3].
Cathepsin S, human (0.4 μM; 2 h) potently degrades the Ii-p10 fragment in the cell membrane of HeLa-CIITA cells, whereas human cathepsin L fails to effectively degrade Ii-p10 even at a concentration 10 times higher^[5].
When expressed in transfected COS-7 cells, human Cathepsin S retains 25% of its maximum elastinolytic activity at pH 7, and all activity at pH 7 is completely inhibited by 1 μM E-64 (HY-15282)^[4].
Cathepsin S, human (24 h) efficiently degrades the Ii-p10 and Ii-p22 fragments, and reduces the accumulation of lysosomal Ii chains in HeLa-CIITA cells^[5].
Cathepsin S, human (24 h) effectively degrades the Ii-p10 fragment and reduces the accumulation of lysosomal Ii chains in MelJuSo cells, whereas the degradation of Ii-p22 in these cells does not require Cathepsin S^[5].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.