Cathepsin S Activity Assay Kit (ab65307) is a fluorescence-based assay that uses the preferred cathepsin-S substrate sequence VVR labeled with AFC (amino-4-trifluoromethyl coumarin).
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Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules and MHC class II antigen presentation (PubMed:30612035). The bond-specificity of this proteinase is in part similar to the specificities of cathepsin L.
Cathepsin S, CTSS
Cathepsin S Activity Assay Kit (ab65307) is a fluorescence-based assay that uses the preferred cathepsin-S substrate sequence VVR labeled with AFC (amino-4-trifluoromethyl coumarin).
Cathepsin S Activity Assay Kit (ab65307) is a fluorescence-based assay that uses the preferred cathepsin-S substrate sequence VVR labeled with AFC (amino-4-trifluoromethyl coumarin). Cell lysates or other samples that contain cathepsin-S will cleave the synthetic substrate VVR-AFC to release free AFC. The released AFC can easily be quantified using a fluorometer or fluorescence plate reader.
This product is manufactured by BioVision, an Abcam company and was previously called K144 Cathepsin S Activity Fluorometric Assay Kit. K144-100 is the same size as the 100 test size of ab65307.
Apoptosis can be mediated by mechanisms other than the traditional caspase-mediated cleavage cascade. There is growing recognition that alternative proteolytic enzymes such as the lysosomal cathepsin proteases may initiate or propagate proapoptotic signals. Cathepsins are lysosomal enzymes that are also used as sensitive markers in various toxicological investigations.
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Cathepsin S sometimes referred to as CTSS is a cysteine protease enzyme weighing about 24-29 kDa part of the papain family. It occurs mainly in lysosomes and is expressed in a variety of cells including antigen-presenting cells like macrophages dendritic cells and B lymphocytes. Cathepsin S functions to cleave proteins at lysines playing a central role in protein degradation and antigen processing. It distinguishes itself from other cathepsins by maintaining activity in an alkaline environment and is essential for the processing of invariant chain (Ii) in MHC class II molecules.
Cathepsin S participates in immune system modulation and matrix degradation. It stands out in its role in the immune response cleaving antigenic proteins for presentation by MHC class II therefore influencing T-cell activation. Although synonymous with lysosomal activity it also operates extracellularly contributing to tissue remodeling and inflammation. Cathepsin S is not part of a larger complex but interacts with MHC class II impacting antigen presentation.
This protease is critical in the immune system and extracellular matrix degradation pathways. In the context of the immune pathway CTSS interacts with other proteases such as Cathepsin L and Cathepsin B to perform antigen trimming and processing. Moreover CTSS supports the activation of T lymphocytes by ensuring the correct presentation of peptide fragments on MHC class II molecules. In matrix degradation CTSS indirectly influences collagen breakdown and interaction with other matrix metalloproteinases.
Cathepsin S is associated with autoimmune diseases like rheumatoid arthritis where it contributes to tissue inflammation and joint damage. It also relates to atherosclerosis promoting instability in atherosclerotic plaques which could result in heart disease. In rheumatoid arthritis interactions with cytokines like TNF-alpha amplify inflammatory responses while in atherosclerosis CTSS links with other proteases to degrade extracellular matrix components leading to vulnerable lesions.
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Cathepsin S Activity measured in tissue lysates (each with protein concentration of 4 mg/mL) after 1 hour of incubation.
Cathepsin S Activity measured in cell lysates (each with cells concentration of 4e7 cells/mL) after 1 hour of incubation with and without inhibitor (I).
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