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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.

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Enzyme Commission number:

Quality Level

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.

UniProt accession no.

shipped in

wet ice

storage temp.

−70°C

Gene Information

human ... CTSS(1520)

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This Item
219461218725342001
recombinant

expressed in E. coli

recombinant

expressed in E. coli

recombinant

expressed in E. coli

recombinant

expressed in E. coli

assay

≥90% (SDS-PAGE)

assay

≥95% (SDS-PAGE)

assay

≥80% (SDS-PAGE)

assay

≥95% (SDS-PAGE)

form

liquid

form

liquid

form

liquid

form

liquid

specific activity

≥30,000 mU/mg protein

specific activity

≥900 mU/mg protein

specific activity

≥100,000 units/mg protein

specific activity

≥1000 mU/mg protein

storage condition

OK to freeze, avoid repeated freeze/thaw cycles

storage condition

OK to freeze, avoid repeated freeze/thaw cycles

storage condition

OK to freeze, avoid repeated freeze/thaw cycles

storage condition

OK to freeze, avoid repeated freeze/thaw cycles

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.

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.

Warning

Toxicity: Harmful (C)

Unit Definition

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 potassium phosphate, 35 mM Sodium acetate, 2 mM DTT, 2 mM EDTA, 50% ethylene glycol, pH 6.5.

Reconstitution

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

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.

Legal Information

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

Pictograms

Exclamation markHealth hazard

Signal Word

Warning

Hazard Statements

Hazard Classifications

Acute Tox. 4 Oral - STOT RE 2 Oral

Target Organs

Kidney

Storage Class Code

10 - Combustible liquids

WGK

WGK 1


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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)
Cathepsin S activity regulates antigen presentation and immunity
Riese RJ, et al.
The Journal of Clinical Investigation, 101(11), 2351-2363 (1998)
Cathepsin S: therapeutic, diagnostic, and prognostic potential
Wilkinson RDA, et al.
Biological Chemistry, 396(8), 867-882 (2015)
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

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