Recombinant Human Cathepsin S (CTSS) Protein (His)

Name: Recombinant Human Cathepsin S (CTSS) Protein (His)
Brand: Beta LifeScience
SKU: BLC-03574P
Price: 418.4 USD
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: Enzymes, Featured enzyme molecules, Protease, Recombinant proteins

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Product Overview

Description	Recombinant Human Cathepsin S (CTSS) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P25774
Target Symbol	CTSS
Synonyms	Cathepsin S; CathepsinS; CATS_HUMAN; Ctss
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	LPDSVDWREKGCVTEVKYQGSCGACWAFSAVGALEAQLKLKTGKLVSLSAQNLVDCSTEKYGNKGCNGGFMTTAFQYIIDNKGIDSDASYPYKAMDQKCQYDSKYRAATCSKYTELPYGREDVLKEAVANKGPVSVGVDARHPSFFLYRSGVYYEPSCTQNVNHGVLVVGYGDLNGKEYWLVKNSWGHNFGEEGYIRMARNKGNHCGIASFPSYPEI
Expression Range	115-331aa
Protein Length	Full Length of Mature Protein
Mol. Weight	28.0kDa
Research Area	Immunology
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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	HGNC: 2545 OMIM: 116845 KEGG: hsa:1520 STRING: 9606.ENSP00000357981 UniGene: Hs.181301

Gene Functions References

Plasma apoA-I proteolysis is augmented in aortic valve stenosis and cathepsin S exerts the most deleterious effects on apoA-I integrity in humans. PMID: 29915952
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
High expression of CTSS was independently associated with lymph node metastasis (OR, 2.015; 95% CI, 1.225-3.315; P=0.006). Therefore, CTSS may serve as a predictive risk marker for the progression and prognosis of papillary thyroid cancer . PMID: 29749483
Authors show a significant increase of circulating CS levels in healthy female subjects induced by long-term physical activity. PMID: 29181829
This study therefore considerably improves our understanding of the molecular mechanism responsible for cathepsin S inhibition and facilitates the identification of potential novel selective inhibitors of cathepsin S. PMID: 28236030
cathepsin S is increased in periodontal cells and tissues under inflammatory and infectious conditions, suggesting a critical role of this autophagy-associated molecule in the pathogenesis of periodontitis. PMID: 29362520
Elevated cathepsin S activity was associated with collagen I degradation and thus might be involved in the progression of abdominal aortic aneurysms. PMID: 29624112
Cathepsin S was identified as the major IL-36gamma-activating protease expressed in epithelial cells. PMID: 28289191
Our results indicate that autophagy is essential for decreasing CTSS activity to inhibit tumor metastasis by hispolon treatment in cervical cancer; this finding provides a new perspective on molecular regulation. PMID: 28981104
These results revealed that CTSS can regulate EGFR signalling by facilitating EGF-mediated EGFR degradation. PMID: 27387133
This study suggested serum Cat S may be a potential biomarker for the diagnosis and prognosis of gastric cancer PMID: 27058412
Overall, these results indicate that exploitation of the cathepsin S activity in MPS tissues can be utilized to substantially lower non-target accumulation, suggesting this is a promising approach for the development of diagnostic and radiotherapeutic nanomedicine platforms. PMID: 27372424
polymorphism of rs7534124 and rs1136774 in cathepsin S promoter may decrease the susceptibility of asthma in a Chinese Han population PMID: 27249607
cathepsin S mRNA (CTSS), which encodes a cysteine protease associated with angiogenesis and atherosclerosis, is highly edited in human endothelial cells. RNA editing enables the recruitment of the stabilizing RNA-binding protein human antigen R (HuR; encoded by ELAVL1) to the 3' UTR of the CTSS transcript, thereby controlling CTSS mRNA stability and expression. PMID: 27595325
the essential role of autophagy-regulated early ROS in triggering late apoptotic signaling PMID: 26029922
Cathepsin S cleaves near the N-terminus of PAR2 to expose a novel tethered ligand, KVDGTS. PMID: 24964046
Increased plasma CTSS concentration is associated with atherogenesis. PMID: 24727728
potential marker of pruritus in dandruff/seborrhoeic dermatitis PMID: 24690038
results identify Cat-S as a biased agonist of PAR2 that causes PAR2- and TRPV4-dependent inflammation and pain. PMID: 25118282
Its stability at neutral pH and potent proteolytic activity on extracellular matrix components mean that cathepsin S may contribute significantly to cartilage degradation and may thus be considered a potential drug target in joint diseases. PMID: 23152404
High cathepsin S expression at the primary site correlates with decreased brain metastasis-free survival in breast cancer patients. PMID: 25086747
cathepsin S and chemerin only correlated positively with insulin resistance and inflammation PMID: 24390241
Cat S-mediated autophagic flux is an important mechanism for inducing M2-type polarization of tumor-associated macrophages, which leads to tumor development PMID: 24580730
Cathepsin S plays an important role in the regulation of autophagy and apoptosis in human glioblastoma cells. PMID: 24875536
Suppression of CD47 by morpholino approach suppressed growth of hepatocellular carcinoma in vivo and exerted a chemosensitization effect through blockade of CTSS/PAR2 signaling. PMID: 24523067
The miR-31/IRF-1/CTSS pathway may play a functional role in the pathogenesis of cystic fibrosis lung disease. PMID: 24940638
Markedly high levels of tear CTSS activity are suggestive of Sjogren syndrome. PMID: 24644101
This study reveals a noncanonical molecular pathway in which, after the inhibition of cathepsin S, autophagy induces early reactive oxygen species production for oxidative DNA damage and cell death through xanthine oxidase. PMID: 23892358
Amyloid-beta can regulate the proinflammatory state of human macrophages by inducing MMP-2/MMP-9/cathepsin S levels and by reducing TGF-beta1 secretion. PMID: 24335416
Cat S may participate in the pathophysiology of cystic fibrosis by weakening the antibacterial activity of SP-A. PMID: 23707200
the genetic polymorphisms of CTSS were associated with metabolic disorders in a Chinese Han population PMID: 23747398
Cathepsin S activity appears to be involved in the early dysregulation of glucose and insulin metabolism. PMID: 22923671
Cleavage of nidogen-1 by cathepsin S impairs its binding to basement membrane partners PMID: 22952693
The present study was designed to determine the role of Cat S in human hepatocellular carcinoma cell growth, invasion and angiogenesis, using RNA interference technology. PMID: 22796222
CTSS variants seem to be nominally associated to obesity related traits and this association may be modified by dietary protein intake PMID: 22844403
HCV has an inhibitory role on cathepsin S-mediated major histocompatibility complex (MHC) class II maturation, which may contribute to weak immunogenicity of viral antigens in chronic infections. PMID: 22761382
Cathepsin S therefore appears to be an important factor that influences selection of autoreactive T cells. PMID: 22424724
Cathepsin S specificity profile appears to be pH-independent. PMID: 21967108
Cathepsin S plays an important role in the regulation of cell autophagy through interference with the EGFR-ERK/MAPK-signaling pathway. PMID: 22101325
results signify that CatS may be an important prognostic biomarker and predictive of response to adjuvant fluoruracil/folinic acid in colorectal carcinoma PMID: 21989182
The cathepsin S deserves further evaluation as therapeutic targets to develop disease modifying drugs to treat Alzheimer's disease. PMID: 21585286
Serum cathepsin S showed significantly lower values 4 days after surgery PMID: 21250859
Among elderly individuals in 2 independent cohorts, higher serum cathepsin S levels were associated with increased mortality risk PMID: 21878432
results suggest that CTSS mediated atherogenesis may be associated with a CD40 mediated inflammatory and immune response. Further invasive atheroma analysis is reasonable PMID: 21223957
Cathepsin S activity in human whole blood was dependent on the time of blood collection, suggesting that cathepsin S activity is subject to circadian variations. PMID: 21094118
Our data provide first evidence that Cathepsin S expression is selectively induced in psoriatic keratinocytes. PMID: 19849712
Down-regulation of cathepsin S was found in inverted papilloma tissues as compared with its expression level in normal sinus mucosa tissues. PMID: 21038029
the immunosuppressive effects of IL-10-STAT3 on MHC-II antigen presentation may occur via the inhibition of cathepsin S expres PMID: 20356901
The researchers found no evidence of an association between the CTSS -25G/A polymorphism and the presence of coronary artery disease in a Chinese population. PMID: 19593952
cathepsin S was found to be significantly elevated in rheumatoid arthritis and osteoarthritis synovial fluid. PMID: 20180636

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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.

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