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Cathepsin S (human), (recombinant)

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Highly active

Cathepsin S, a member of the papain family of lysosomal cysteine proteases, functions in the immune system.

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Application Notes	Useful to study enzyme kinetics, cleave target substrates, and screen for inhibitors.
Formulation	Liquid. In 100 mM MES, pH 6.5, containing 1 mM EDTA, 50 mM L-cysteine, 10 mM DTT, 0.5% Triton^® X-100, 30% glycerol.
MW	26 kDa
Purity	≥95% (SDS-PAGE)
Purity Detail	Purified by multi-step chromatography.
Source	Produced in insect cells. Recombinant active cathepsin S cloned from human cDNA as full length proenzyme, auto-activated by incubation in pH 4.5 acetate buffer, and purified. Produced in a baculovirus expression system.
Specific Activity	≥20 U/mg protein. One unit will hydrolyze one µmole Z-Val-Val-Arg-AMC substrate (Prod. No. BML-P199, 40 µM) per minute at 37°C.
UniProt ID	P25774

Long Term Storage	-80°C
Shipping	Dry Ice

Regulatory Status	RUO – Research Use Only

An Unusual Two-Domain Thyropin from Tick Saliva: NMR Solution Structure and Highly Selective Inhibition of Cysteine Cathepsins Modulated by Glycosaminoglycans: Z. Matoušková, et al.; Int. J. Mol. Sci. 25, 2240 (2024), Abstract
An evolutionary molecular adaptation of an unusual stefin from the liver fluke Fasciola hepatica redefines the cystatin superfamily: M. Busa, et al.; J. Biol. Chem. 299, 102970 (2023), Abstract
Two Tags in One Probe: Combining Fluorescence- and Biotin-based Detection of the Trypanosomal Cysteine Protease Rhodesain: C. Lemke, et al.; Chemistry 28, e202201636 (2022), Abstract
Multiple sites on SARS-CoV-2 spike protein are susceptible to proteolysis by cathepsins B, K, L, S, and V: K. Bollavaram, et al.; Protein Sci. 30, 1131 (2021), Abstract
Cell penetrable, clickable and tagless activity-based probe of human cathepsin L: D. Dana, et al.; Bioorg. Chem. 85, 505 (2019), Application(s): Activity assay, Abstract
Development of a highly potent, selective, and cell-active Inhibitor of cysteine cathepsin L-A hybrid design approach: D. Dana, et al.; Chem. Commun. (Camb.) 50, 10875 (2014), Abstract
Development of cell-active non-peptidyl inhibitors of cysteine cathepsins: D. Dana, et al.; Bioorg. Med. Chem. 21, 2975 (2013), Abstract

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