CTSS Proteins

CTSS (Cathepsin S) is a Protein Coding gene. Diseases associated with CTSS include Dacryoadenitis. Among its related pathways are Innate Immune System and G-protein signaling N-RAS regulation pathway. Gene Ontology (GO) annotations related to this gene include peptidase activity and cysteine-type peptidase activity. An important paralog of this gene is CTSK.

CUSABIO has five systems (E. coli, In vitro E.coli, Yeast, Insect Baculovirus, Mammalian) from prokaryotic to eukaryotic to express the recombinant protein, and a very strict QC system so that the quality can be guaranteed. And the following CTSS proteins are produced under the system.
CTSS proteins produced by CUSABIO are featured with high purity, low endotoxin, multi-Sources & tags, animal-free, etc. And you will have many choices on sizes from μg to mg. In addition, CTSS custom service is also available for research with more specific needs.

CTSS Proteins Catalog

CTSS Proteins for Rattus norvegicus (Rat)

CTSS Proteins for Homo sapiens (Human)

CTSS Proteins for Bos taurus (Bovine)

CTSS Proteins for Mus musculus (Mouse)

CTSS Proteins for Canis lupus familiaris (Dog) (Canis familiaris)

CTSS Proteins for Saimiri boliviensis boliviensis (Bolivian squirrel monkey)

CTSS Background

Cathepsin S (CTSS) is one of the lysosomal cysteine endopeptidases. CTSS is synthesized as a 331 amino acid pre-proenzyme containing a signal domain (16 amino acids), pro-peptide domain (98 amino acids), and mature domain (217 amino acids) [1]. The propeptide domain occludes the active site, rendering the protease inactive [2]. Procathepsin S can be autocatalytically activated ac pH 4.5 [3]. And active CTSS is overexpressed and secreted by human chondrocytes upon stimulation from pro-inflammatory cytokines interleukin 1α (IL-1α) and tumor necrosis factor α (TNF α) [13]. CTSS has a high endopeptidase activity against different proteins including elastin and collagen. Its substrate specificity is similar to cathepsin L, but it differs distinctly in its S2 subsite specificity [4]. Biochemically, cathepsin S is different from other cysteine cathepsins in its ability to retain activity at a neutral pH [5]. CTSS is predominantly expressed in the spleen and professional antigen-presenting cells, including B lymphocytes, macrophages, and other class II-positive cells [6][7]. The restricted tissue distribution of CTSS is consistent with its function in the major histocompatibility complex (MHC) class II antigen-presenting pathway in antigen-presenting cells derived from bone marrow [8]. CTSS is essential in B cells for effective Ii chain proteolysis necessary to make class II molecules competent to bind peptides [9]. And CTSS is also involved in lysosomal rupture-induced apoptosis. CTSS was shown to play novel roles in cancer cell migration and invasion, such as colorectal carcinomas [10], gastric cancer [11], and hepatocellular carcinoma [12]. Silencing CTSS expression inhibited the migration and invasion of gastric cancer cells in vitro. Flannery T et al. demonstrated that CTSS may act as a prognostic indicator and potential target for noninvasive therapy [14].

[1] Lecaille, F., Kaleta, J., et al. Human and parasitic papain-like cysteine proteases: their role in physiology and pathology and recent developments in inhibitor design [J]. Chem. 2002, Rev. 102, 4459-4488.
[2] Dickinson, D.P. Cysteine peptidases of mammals: their biological roles and potential effects in the oral cavity and other tissues in health and disease [J]. Crit Rev Oral Biol Med, 2002, 13 (3), 238-75.
[3] Bonneau, P.R., Lachance, P., et al. Functional expression of human cathepsin s in Saccharomvces cerevisiae. Purification and characterization of the recombinant enzyme [J]. J. Biol. Chem. 1993, 268 (7), 4832-4838.
[4] Xin, X-Q., Gunesekera, et al. The specificity and elastinolytic activities of bovine cathepsins S and H [J]. Arch. Bioc.hem. Biophys. 1992, 299, 334-339.
[5] Chapman, H.A., Riese, R.J., et al. Emerging roles for cysteine proteases in human biology [J]. Annu. Rev. Physiol. 1997, 59, 63-88.
[6] Shi GP, Munger JS, et al. Molecular cloning and expression of human alveolar macrophage cathepsin S, an elastinolytic cysteine p4otease [J]. J Biol Chem. 1992 Apr 15; 267(11):7258-62.
[7] Shi GP, Webb AC, et al. Human cathepsin S: chromosomal localization, gene structure, and tissue distribution [J]. J Biol Chem. 1994 Apr 15; 269(15):11530-6.
[8] Honey, K., and Rudensky, A. Y. Lysosomal cysteine proteases regulate antigen presentation [J]. Nat. Rev. Immunol. 2003, 3, 472 - 482.
[9] ERiese RJ, Wolf PR, et al. sential role for cathepsin S in MHC class II-associated invariant chain processing and peptide loading [J]. Immunity. 1996 Apr; 4(4):357-66.
[10] Burden RE, Gormley JA, et al. Inhibition of Cathepsin S by Fsn0503 enhances the efficacy of chemotherapy in colorectal carcinomas [J]. Biochimie. 2012 Feb; 94(2):487-93.
[11] Yang Y, Lim SK, et al. Cathepsin S mediates gastric cancer cell migration and invasion via a putative network of metastasis-associated proteins [J]. J Proteome Res. 2010 Sep 3; 9(9):4767-78.
[12] Fan Q, Wang X, et al. Silencing cathepsin S gene expression inhibits growth, invasion, and angiogenesis of human hepatocellular carcinoma in vitro [J]. Biochem Biophys Res Commun. 2012 Sep 7; 425(4):703-10.
[13] Cagliˇc, D.; Repnik, U.; et al. The proinflammatory cytokines interleukin-1α and tumor necrosis factorα promote the expression and secretion of proteolytically active cathepsin S from human chondrocytes [J]. Biol. Chem. 2013, 394, 307-316.
[14] Flannery T, McQuaid S, et al. Cathepsin S expression: An independent prognostic factor in glioblastoma tumours--A pilot study [J]. Int J Cancer. 2006 Aug 15; 119(4):854-60.

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