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Mouse Anti-CTSC Recombinant Antibody (CBCNC-472) (CBMAB-C3116-CN)

This product is a Mouse antibody that recognizes CTSC. The antibody CBCNC-472 can be used for immunoassay techniques such as: ELISA, WB, IHC-P.
See all CTSC antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBCNC-472
Antibody Isotype
IgG2b
Application
ELISA, WB, IHC-P

Basic Information

Immunogen
Recombinant protein
Specificity
Human
Antibody Isotype
IgG2b
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Buffer
Citrate-Tris-HCl buffer, pH 7.0
Preservative
0.02% Proclin 300

Target

Full Name
Cathepsin C
Introduction
CTSC (Cathepsin C) is a Protein Coding gene. Diseases associated with CTSC include Papillon-Lefevre Syndrome and Haim-Munk Syndrome. Among its related pathways are Metabolism of proteins and Transport to the Golgi and subsequent modification. Gene Ontology (GO) annotations related to this gene include identical protein binding and cysteine-type peptidase activity. An important paralog of this gene is TINAG.
Entrez Gene ID
1075
UniProt ID
P53634
Alternative Names
Cathepsin C; Dipeptidyl Peptidase 1; Dipeptidyl Transferase; Cathepsin J; EC 3.4.14.1; DPP-I; CPPI; DPPI; Dipeptidyl-Peptidase I;
Function
Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII.
Biological Process
Aging Source: Ensembl
COPII vesicle coating Source: Reactome
Endoplasmic reticulum to Golgi vesicle-mediated transport Source: Reactome
Immune response Source: ProtInc
Negative regulation of myelination Source: Ensembl
Neutrophil degranulation Source: Reactome
Positive regulation of apoptotic signaling pathway Source: Ensembl
Positive regulation of microglial cell activation Source: Ensembl
Positive regulation of proteolysis involved in cellular protein catabolic process Source: ParkinsonsUK-UCL
Proteolysis Source: UniProtKB
Proteolysis involved in cellular protein catabolic process Source: GO_Central
Response to organic substance Source: Ensembl
T cell mediated cytotoxicity Source: Ensembl
Cellular Location
Lysosome
Involvement in disease
Papillon-Lefevre syndrome (PLS):
An autosomal recessive disorder characterized by palmoplantar keratosis and severe periodontitis affecting deciduous and permanent dentitions and resulting in premature tooth loss. The palmoplantar keratotic phenotype vary from mild psoriasiform scaly skin to overt hyperkeratosis. Keratosis also affects other sites such as elbows and knees.
Haim-Munk syndrome (HMS):
An autosomal recessive disorder characterized by palmoplantar keratosis, onychogryphosis and periodontitis. Additional features are pes planus, arachnodactyly, and acroosteolysis.
Periodontititis, aggressive, 1 (AP1):
A disease characterized by severe and protracted gingival infections, generalized or localized, leading to tooth loss. Amounts of microbial deposits are generally inconsistent with the severity of periodontal tissue destruction and the progression of attachment and bone loss may be self arresting.
PTM
N-glycosylated. While glycosylation at Asn-53, Asn-119 and Asn-276 is mediated by STT3A-containing complexes, glycosylation at Asn-29 is mediated STT3B-containing complexes.
In approximately 50% of the complexes the exclusion domain is cleaved at position 58 or 61. The two parts of the exclusion domain are held together by a disulfide bond.

Xiao, Y., Cong, M., Li, J., He, D., Wu, Q., Tian, P., ... & Hu, G. (2021). Cathepsin C promotes breast cancer lung metastasis by modulating neutrophil infiltration and neutrophil extracellular trap formation. Cancer Cell, 39(3), 423-437.

Ghanei, M., Abbaszadegan, M. R., Forghanifard, M. M., Aarabi, A., & Arab, H. (2021). A novel mutation in the cathepsin C (CTSC) gene in Iranian family with Papillon‐Lefevre syndrome. Clinical and Experimental Dental Research, 7(4), 568-573.

Zhang, G. P., Yue, X., & Li, S. Q. (2020). Cathepsin C interacts with TNF-α/p38 MAPK signaling pathway to promote proliferation and metastasis in hepatocellular carcinoma. Cancer Research and Treatment: Official Journal of Korean Cancer Association, 52(1), 10.

Khaket, T. P., Singh, M. P., Khan, I., & Kang, S. C. (2020). In vitro and in vivo studies on potentiation of curcumin-induced lysosomal-dependent apoptosis upon silencing of cathepsin C in colorectal cancer cells. Pharmacological research, 161, 105156.

John, D. S., Aschenbach, J., Krüger, B., Sendler, M., Weiss, F. U., Mayerle, J., ... & Aghdassi, A. A. (2019). Deficiency of cathepsin C ameliorates severity of acute pancreatitis by reduction of neutrophil elastase activation and cleavage of E-cadherin. Journal of Biological Chemistry, 294(2), 697-707.

Chiang, K. C., Lai, C. Y., Chiou, H. L., Lin, C. L., Chen, Y. S., Kao, S. H., & Hsieh, Y. H. (2019). Timosaponin AIII inhibits metastasis of renal carcinoma cells through suppressing cathepsin C expression by AKT/miR‐129‐5p axis. Journal of Cellular Physiology, 234(8), 13332-13341.

Alam, S., Liu, Q., Liu, S., Liu, Y., Zhang, Y., Yang, X., ... & Ma, J. (2019). Up-regulated cathepsin C induces macrophage M1 polarization through FAK-triggered p38 MAPK/NF-κB pathway. Experimental Cell Research, 382(2), 111472.

Gang Liu, Y., Teng, Y. S., Cheng, P., Kong, H., Lv, P. Y., Mao, F. Y., ... & Zhuang, A. Y. (2019). Abrogation of cathepsin C by Helicobacter pylori impairs neutrophil activation to promote gastric infection. The FASEB Journal, 33(4), 5018-5033.

Khaket, T. P., Singh, M. P., Khan, I., Bhardwaj, M., & Kang, S. C. (2018). Targeting of cathepsin C induces autophagic dysregulation that directs ER stress mediated cellular cytotoxicity in colorectal cancer cells. Cellular Signalling, 46, 92-102.

Miller, B. E., Mayer, R. J., Goyal, N., Bal, J., Dallow, N., Boyce, M., ... & Lazaar, A. L. (2017). Epithelial desquamation observed in a phase I study of an oral cathepsin C inhibitor (GSK2793660). British journal of clinical pharmacology, 83(12), 2813-2820.

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For research use only. Not intended for any clinical use.

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