Recombinant Mouse Cathepsin S Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-0608

Recombinant Mouse Cathepsin S Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-0608
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Tag His
Host Species Mouse
Accession AAB94925.1
Synonym Cat S, Cats
Background Cathepsin S (CTSS), one of the lysosomal proteinases, has many important physiological functions in the nervous system, especially in process of extracellular matrix degradation and endocellular antigen presentation. CTSS is synthesized as inactive precursor of 331 amino acids consisting of a 15-aa signal peptide, a propeptide of 99 aa, and a mature polypeptide of 217 aa. It is activated in the lysosomes by a proteolytic cleavage of the propeptide. Cathepsin S is expressed in the lysosome of antigen presenting cells, primarily dendritic cells, B-cells and macrophages. Compared with other lysosomal cysteine proteases, cathepsin S has displayed some unique characteristics. Cathepsin S is most well known for its critical function in the proteolytic digestion of the invariant chain chaperone molecules, thus controlling antigen presentation to CD4+ T-cells by major histocompatibility complex (MHC) class II molecules or to NK1.1+ T-cells via CD1 molecules. Cathepsin S also appears to participate in direct processing of exogenous antigens for presentation by MHC class II to CD4+ T-cells, or in cross-presentation by MHC class I molecules to CD8+ T-cells. In addition, although direct evidence is still lacking, in its secreted form cathepsin S is implicated in degradation of the extracellular matrix, which may contribute to the pathology of a number of diseases, including arthritis, atherosclerosis, neurological diseases and chronic obstructive pulmonary disease.
Description A DNA sequence encoding the full length of mouse CTSS (AAB94925.1) (Met 1-Ile 340) was expressed, with a C-terminal His tag.
Source HEK293
Predicted N Terminal Val 18
AA Sequence Met 1-Ile 340
Molecular Weight The recombinant mouse CTSS consists of 334 a.a. and predicts a molecular mass of 37.6 KDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rmCTSS is approximately 33-38 KDa.
Purity >90% as determined by SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity Measured by its ability to cleave the fluorogenic peptide substrate, Mca-RPKPVENval-WRK (Dnp)-NH2, AnaSpec, Catalog # 27114.The specific activity is >300 pmoles/min/ug.(Activation description: The enzyme achieves its activity under acidic pH)
Formulation Lyophilized from sterile PBS, pH 7.4.
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules and MHC class II antigen presentation. The bond-specificity of this proteinase is in part similar to the specificities of cathepsin L.
Subcellular Location Lysosome. Secreted. Cytoplasmic vesicle, phagosome.
Protein Families Peptidase C1 family
Database References
Tissue Specificity Widely expressed with highest expression found in non-skeletal tissues. Relatively high levels found in skeletal tissues. Expressed in spleen, B cells, dendritic cells and macrophages.

Gene Functions References

  1. The present data indicating that Cat-S activity increases with CKD progression suggest that Cat-S might be a therapeutic target to prevent cardiovascular complications in CKD. PMID: 28240259
  2. CatS(-/-) mice exhibited impaired social interaction and social novelty recognition in the three-chamber test. PMID: 28623134
  3. Cathepsin S activity controls injury-related vascular remodeling via TLR2/p38MAPK/PI3K/Akt/p-HDAC6 signaling pathway. PMID: 27365406
  4. Ctss induction during muscular dystrophy is a pathologic event that partially underlies disease pathogenesis, and its inhibition might serve as a new therapeutic strategy in Duchenne muscular dystrophy. PMID: 26966179
  5. Fluorogen substrate, Mca-GRWPPMGLPWE-Lys(Dnp)-DArg-NH2 can detect CTSS activities in mouse antigen presenting cells. PMID: 26899824
  6. Data show that cathepsins S (CatS) regulates CCL2 chemokine expression by modulation of CD74 antigen processing. PMID: 26358505
  7. Cathepsin S activates MrgprC11 and evokes receptor-dependent scratching in mice. PMID: 26216096
  8. cathepsin S deficiency alters the balance between adipocyte and osteoblast differentiation, increases bone turnover, and changes bone microarchitecture. Therefore, bone and fat metabolisms should be monitored when using cathepsin S inhibitors clinically PMID: 24780878
  9. results identify Cat-S as a biased agonist of PAR2 that causes PAR2- and TRPV4-dependent inflammation and pain. PMID: 25118282
  10. Cathepsin S contributes to macrophage migration via degradation of elastic fibre integrity to facilitate neointima formation of vein grafts PMID: 24319016
  11. CatS also reduced myocardial Smad2 and Smad3 activation and extra domain A fibronectin expression PMID: 23771947
  12. CatS is involved in the secondary injury after traumatic brain injury PMID: 24282339
  13. Disruption of CatS therefore induces hyperlocomotor activity due to failure to downscale the synaptic strength. PMID: 24067868
  14. These results show a peripheral pivotal role of CatS in the development of neuropathic pain through the antigen-specific activation of CD4(+) T-cells PMID: 24553941
  15. High cathepsin S promotes cancer growth and neovascularization. PMID: 23629809
  16. Provide direct evidence that Cat S plays an important role in abdominal aortic aneurysm formation in apoE-deficient mice. PMID: 22871592
  17. GILT expression decreased the proteolysis of a CatS selective substrate. PMID: 23012103
  18. Cathepsin S deficiency results in abnormal accumulation of autophagosomes in macrophages and enhances Ang II-induced cardiac inflammation. PMID: 22558139
  19. Overexpression of cathepsin S induces chronic atopic dermatitis in mice. PMID: 22170489
  20. Cat-S activates nociceptors to induce visceral pain via protease-activated receptor-2. PMID: 21802389
  21. only prophylactic Cat S inhibitor dosing blocked lung inflammation, consistent with our findings in Cat S knockout mice. PMID: 20855652
  22. Cathepsin S inhibition prevented the formation of lung granulomas in a mouse model of sarcoidosis. PMID: 21251246
  23. Cat S derived from macrophages is involved in the mechanisms of atherosclerotic plaque vulnerability in apoE-deficient mice PMID: 20079903
  24. For a subset of antigens, epitope generation is critically regulated by cathepsin S, which participates in antigen processing and generates qualitative and quantitative differences in the peptide repertoires displayed by MHC class II molecules. PMID: 11884425
  25. regulation of the phagosomal CatS, CatL, CatB and CatZ contents during dendritic cell activation PMID: 12186844
  26. cathepsin S contributes to angiogenesis by microvascular endothelial cells. PMID: 12600886
  27. In vivo, nonprofessional histocompatibility class (MHC) II-expressing antigen presenting cells of the intestinal epithelium use Cat S, but not Cat L, for MHC class II-mediated antigen presentation. PMID: 15661874
  28. First direct genetic evidence is reported for a key role of cathepsin S in autoimmune responses to acetylcholine receptor and in the pathogenesis of experimental autoimmune myasthenia gravis. PMID: 15661938
  29. Transgenic interferon-gamma induces alveolar epithelial cell DNA injury and apoptosis via a novel murine cathepsin S-dependent pathway, a critical event in the pathogenesis of alveolar remodeling, emphysema and inflammation. PMID: 15944319
  30. The increases in mRNA levels for CatS and GPX3 found in the aging C57BL/6 RPE/choroid appear to represent an increase in both the numbers of cells expressing these messages and an increase in the level of expression in individual cells. PMID: 15947738
  31. Cathepsin S has a unique role in determining the morphology of class II MHC-positive endosomal compartments PMID: 16094690
  32. interleukin-6-signal transducer and activator of transcription 3 -mediated increase of cathepsin S activity PMID: 16286017
  33. Data show that cathepsin S deficiency impairs angiogenesis and tumor cell proliferation, impairing angiogenic islet formation and the growth of solid tumors; while the absence of its endogenous inhibitor cystatin C resulted in opposite phenotypes. PMID: 16365041
  34. plays an important role in atherosclerotic plaque destabilization and rupture PMID: 16410454
  35. Plays role in migration and activation of microglia to protect facial motoneurons against axotomy-induced injury. PMID: 17539023
  36. These results indicate that seizures induced by kainate elicit neurodegeneration, astrogliosis, and microglial activation accompanied by the expression of cathepsin S while those induced by nicotine do not. PMID: 17997037
  37. Upregulation of elastase proteins results in aortic dilatation in mucopolysaccharidosis I mice. PMID: 18479957
  38. CAT S participates in inflammatory processes accompanying aging and pathologies of the central nervous system PMID: 18694734
  39. Leukocyte cathepsin S is a potent regulator of both cell and matrix turnover in advanced atherosclerosis. PMID: 19095996
  40. catS-induced elastolysis accelerates arterial and aortic valve calcification in chronic renal disease PMID: 19307473
  41. The active form of cathepsin S was identified as being significantly up-regulated in poorly differentiated TRAMP tumours. PMID: 19487544


Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

Recently viewed