Recombinant Mouse Cathepsin S Protein (His Tag)

Name: Recombinant Mouse Cathepsin S Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-0608
Availability: InStock

Collections: Enzymes, Protease, Recombinant proteins

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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	KEGG: mmu:13040 STRING: 10090.ENSMUSP00000112006 UniGene: Mm.3619
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

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
CatS(-/-) mice exhibited impaired social interaction and social novelty recognition in the three-chamber test. PMID: 28623134
Cathepsin S activity controls injury-related vascular remodeling via TLR2/p38MAPK/PI3K/Akt/p-HDAC6 signaling pathway. PMID: 27365406
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
Fluorogen substrate, Mca-GRWPPMGLPWE-Lys(Dnp)-DArg-NH2 can detect CTSS activities in mouse antigen presenting cells. PMID: 26899824
Data show that cathepsins S (CatS) regulates CCL2 chemokine expression by modulation of CD74 antigen processing. PMID: 26358505
Cathepsin S activates MrgprC11 and evokes receptor-dependent scratching in mice. PMID: 26216096
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
results identify Cat-S as a biased agonist of PAR2 that causes PAR2- and TRPV4-dependent inflammation and pain. PMID: 25118282
Cathepsin S contributes to macrophage migration via degradation of elastic fibre integrity to facilitate neointima formation of vein grafts PMID: 24319016
CatS also reduced myocardial Smad2 and Smad3 activation and extra domain A fibronectin expression PMID: 23771947
CatS is involved in the secondary injury after traumatic brain injury PMID: 24282339
Disruption of CatS therefore induces hyperlocomotor activity due to failure to downscale the synaptic strength. PMID: 24067868
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
High cathepsin S promotes cancer growth and neovascularization. PMID: 23629809
Provide direct evidence that Cat S plays an important role in abdominal aortic aneurysm formation in apoE-deficient mice. PMID: 22871592
GILT expression decreased the proteolysis of a CatS selective substrate. PMID: 23012103
Cathepsin S deficiency results in abnormal accumulation of autophagosomes in macrophages and enhances Ang II-induced cardiac inflammation. PMID: 22558139
Overexpression of cathepsin S induces chronic atopic dermatitis in mice. PMID: 22170489
Cat-S activates nociceptors to induce visceral pain via protease-activated receptor-2. PMID: 21802389
only prophylactic Cat S inhibitor dosing blocked lung inflammation, consistent with our findings in Cat S knockout mice. PMID: 20855652
Cathepsin S inhibition prevented the formation of lung granulomas in a mouse model of sarcoidosis. PMID: 21251246
Cat S derived from macrophages is involved in the mechanisms of atherosclerotic plaque vulnerability in apoE-deficient mice PMID: 20079903
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
regulation of the phagosomal CatS, CatL, CatB and CatZ contents during dendritic cell activation PMID: 12186844
cathepsin S contributes to angiogenesis by microvascular endothelial cells. PMID: 12600886
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
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
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
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
Cathepsin S has a unique role in determining the morphology of class II MHC-positive endosomal compartments PMID: 16094690
interleukin-6-signal transducer and activator of transcription 3 -mediated increase of cathepsin S activity PMID: 16286017
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
plays an important role in atherosclerotic plaque destabilization and rupture PMID: 16410454
Plays role in migration and activation of microglia to protect facial motoneurons against axotomy-induced injury. PMID: 17539023
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
Upregulation of elastase proteins results in aortic dilatation in mucopolysaccharidosis I mice. PMID: 18479957
CAT S participates in inflammatory processes accompanying aging and pathologies of the central nervous system PMID: 18694734
Leukocyte cathepsin S is a potent regulator of both cell and matrix turnover in advanced atherosclerosis. PMID: 19095996
catS-induced elastolysis accelerates arterial and aortic valve calcification in chronic renal disease PMID: 19307473
The active form of cathepsin S was identified as being significantly up-regulated in poorly differentiated TRAMP tumours. PMID: 19487544

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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.

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