219343

Cathepsin S, Human, Recombinant, E. coli

Name: Cathepsin S, Human, Recombinant, <i>E. coli</i>
Brand: MM

Cathepsin S, Human, Recombinant, E. coli, is prepared without a tag or fusion protein. A major lysosomal cysteine proteinase with high specific activity.

Synonym(s):

Cathepsin S Protein

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About This Item

EC Number:

3.4.22.27 (BRENDA, IUBMB)

NACRES:

NA.77

UNSPSC Code:

12352202

Product Name

Cathepsin S, Human, Recombinant, E. coli, Cathepsin S, Human, Recombinant, E. coli, is prepared without a tag or fusion protein. A major lysosomal cysteine proteinase with high specific activity.

biological source

human

recombinant

expressed in E. coli

assay

≥90% (SDS-PAGE)

form

liquid

specific activity

≥30,000 mU/mg protein

manufacturer/tradename

Calbiochem^®

storage condition

OK to freeze
avoid repeated freeze/thaw cycles

technique(s)

cell based assay: suitable

Protein ID accession no.

AAC37592
AAH02642

UniProt accession no.

P25774

shipped in

wet ice

storage temp.

−70°C

Quality Level

100

Gene Information

human ... CTSS(1520)

Application

Cathepsin S, Human, Recombinant, E. coli has been used in cathepsin digestion reactions.

Biochem/physiol Actions

Cathepsin S is a cysteine protease that plays a role in degradation of class II complexes in human B lymphocytes. It possesses endoproteolytic activity and aids in processing and presenting antigens to immune cells, thereby influencing the immune response. Cathepsin S is involved in facilitating the degradation of damaged or unwanted proteins within the endo-lysosomal pathway. Dysregulation of Cathepsin S activity leads to the development of various diseases such as arthritis, cancer, and cardiovascular diseases.

Disclaimer

Toxicity: Harmful (C)

General description

Note: 1 mU = 1 milliunit.

Research area: Cell Signaling

Recombinant, human cathepsin S expressed in E. coli without a tag or fusion protein. A major lysosomal cysteine proteinase that is preferentially expressed in macrophages and microglia. Shown to be involved in the processing of antigenic peptides for presentation by MHC Class II molecules on the surface of antigen-presenting cells by mediating invariant (Ii) chain degradation. Inhibition of cathepsin S results in impaired antigen-presentation.

Other Notes

Liuzzo, J.P., et al. 1999. Mol. Med.5, 334.
Riese, R.J., et al. 1998. J. Clin. Invest.101, 2351.
Sukhova, G.K., et al. 1998. J. Clin. Invest.102, 576.
Kirschke, H., and Wiederanders, B. 1994. Methods Enzymol.244, 500.
Xin, X.Q., et al. 1992. Arch. Biochem. Biophys.299, 334.
Kirschke, H., et al. 1989. Biochem. J.264, 467.

One unit is defined as the amount of enzyme that will hydrolyze 1.0 µmol Z-VVR-AMC per min at 37°C, pH 6.5. Note: 1 mU = 1 milliunit.

Physical form

In 35 mM MES, 35 mM sodium acetate, 2 mM DTT, 2 mM EDTA, 50% ethylene glycol, pH 6.4.

Preparation Note

Following initial thaw, aliquot and freeze (-70°C).

Legal Information

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

pictograms

GHS08,GHS07

signalword

Warning

hcodes

H302,H373

pcodes

P260 - P264 - P270 - P301 + P312 - P314 - P501

Hazard Classifications

Acute Tox. 4 Oral - STOT RE 2 Oral

target_organs

Kidney

Storage Class

10 - Combustible liquids

wgk

WGK 1

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Cathepsin S: therapeutic, diagnostic, and prognostic potential

Wilkinson RDA, et al.

Biological Chemistry, 396(8), 867-882 (2015)

Cathepsin S: therapeutic, diagnostic, and prognostic potential

Wilkinson RD, et al.

Applied Biological Chemistry, 396(8), 867-882 (2015)

Cathepsin S activity regulates antigen presentation and immunity

Riese R J, et al.

The Journal of Clinical Investigation, 2351-2363 (1998)

Design, synthesis and biological evaluation of inhibitors of cathepsin K on dedifferentiated chondrocytes.

Xiao-Yu Yuan et al.

Bioorganic & medicinal chemistry, 27(6), 1034-1042 (2019-02-19)

Selective proteinase inhibitors have demonstrated utility in the investigation of cartilage degeneration mechanisms and may have clinical use in the management of osteoarthritis. The cysteine protease cathepsin K (CatK) is an attractive target for arthritis therapy. Here we report the