Cathepsin S Antibody #25084
Filter:
- WB
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 25, 37 |
| SOURCE | Rabbit |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Simple Western™ | 1:50 - 1:250 |
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.
Protocol
Specificity / Sensitivity
Cathepsin S Antibody recognizes endogenous levels of total cathepsin S protein. The antibody detects the full-length pro-protein (37 kDa), and proteolytically activated cathepsin S (25 kDa). In some cell extracts, the antibody weakly detects a 70 kDa protein of unknown identity.
Species Reactivity:
Human
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Gly233 of human cathepsin S protein. Antibodies are purified by peptide affinity chromatography.
Background
Cathepsin S (CTSS) is a cysteine protease belonging to the cathepsin family (1). It is synthesized as a 37 kDa pro-protein, which is proteolytically processed to remove the amino terminal activation peptide, yielding the mature (active) cathepsin S protein (2). The protein is localized to the lysosomal or endosomal compartments of antigen-presenting cells such as B cells, macrophages, and dendritic cells, where it plays an important role in immune response activation (3,4). Specifically, cathepsin S proteolytically removes the self-associated invariant chain (CD74) from MHC class II, and promotes MHC-exogenous antigenic peptide loading (5). Cathepsin S may also be secreted by cells to the extracellular matrix, where its proteolytic degradation of matrix proteins and cytokines (e.g., collagens, elastin, PAR2) has been shown to influence cell signaling (1). Aberrant expression and activity of cathepsin S have been associated with various disease states, including atherosclerosis, fibrosis and inflammation, autoimmune disease, and cancer (6-10), making it a potential biomarker and a promising therapeutic target.
- Wilkinson, R.D. et al. (2015) Biol Chem 396, 867-82.
- Huang, C.C. et al. (2016) Sci Rep 6, 29256.
- Villadangos, J.A. et al. (1999) Immunol Rev 172, 109-20.
- Nakagawa, T.Y. and Rudensky, A.Y. (1999) Immunol Rev 172, 121-9.
- Riese, R.J. et al. (1996) Immunity 4, 357-66.
- Wu, H. et al. (2018) J Atheroscler Thromb 25, 111-123.
- Kehlet, S.N. et al. (2017) BMC Pulm Med 17, 110.
- Sena, B.F. et al. (2017) Front Cardiovasc Med 4, 88.
- Clark, A.K. and Malcangio, M. (2012) Exp Neurol 234, 283-92.
- McDowell, S.H. et al. (2020) Biochim Biophys Acta Mol Cell Res 1867, 118781.
限制使用
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KARPAS cell line source: Dr. Abraham Karpas at the University of Cambridge.
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