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Mouse Anti-CTSC Recombinant Antibody (CBYCD-135) (V2LY-0125-LY403)


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Published Data
V2LY-0125-LY403-1
Mouse Anti-CTSC Recombinant Antibody (CBYCD-135) (V2LY-0125-LY403) in WB
HT-29 cells were fractionated into cytosol and membrane fractions after DMSO or T/S/Z treatment for 4 h, followed by Western blotting with the indicated antibodies. The mature active cathepsins were shown. LDH (lactate dehydrogenase) and LAMP1 served as cytosol and membrane markers respectively. Antibody p-MLKL recognizes phospho-S358 of MLKL. ...View More
Liu, S., Perez, P., Sun, X., Chen, K., Fatirkhorani, R., Mammadova, J., & Wang, Z. (2024). MLKL polymerization-induced lysosomal membrane permeabilization promotes necroptosis. Cell Death & Differentiation, 31(1), 40-52. Distributed under Open Access license CC BY 4.0, without modification.
V2LY-0125-LY403-2
Mouse Anti-CTSC Recombinant Antibody (CBYCD-135) (V2LY-0125-LY403) in WB
Colors represent different UMAP clusters indicating genetically distinct NK cell subsets. Western blot of protein expression of granzyme B, cathepsin C, and perforin-1 in sNK vs. IL-2 treated primary NK cells derived from the same donor. ...View More
Kaur, K., Chen, P. C., Ko, M. W., Mei, A., Senjor, E., Malarkannan, S., ... & Jewett, A. (2023). Sequential therapy with supercharged NK cells with either chemotherapy drug cisplatin or anti-PD-1 antibody decreases the tumor size and significantly enhances the NK function in Hu-BLT mice. Frontiers in Immunology, 14, 1132807. Distributed under Open Access license CC BY 4.0, without modification.
V2LY-0125-LY403-3
Mouse Anti-CTSC Recombinant Antibody (CBYCD-135) (V2LY-0125-LY403) in WB
Reduced CTSC expression by HA1. Western blot bands were measured using Image J software (n = 3). ...View More
Kim, S., Lee, K. H., Choi, H. J., Kim, E., Kang, S., Han, M., ... & Lee, H. J. (2023). Hederacolchiside A1 suppresses autophagy by inhibiting cathepsin C and reduces the growth of colon cancer. Cancers, 15(4), 1272. Distributed under Open Access license CC BY 4.0, without modification.
V2LY-0125-LY403-4
Mouse Anti-CTSC Recombinant Antibody (CBYCD-135) (V2LY-0125-LY403) in Immunoblotting
Immunoblots for mitochondrial proteins in BMM WT, CtsB KO, CtsL KO and CtsS KO stimulated with 0.5 mM LLOMe for 1 h. (repeated three times with similar results). ...View More
Bussi, C., Heunis, T., Pellegrino, E., Bernard, E. M., Bah, N., Dos Santos, M. S., ... & Gutierrez, M. G. (2022). Lysosomal damage drives mitochondrial proteome remodelling and reprograms macrophage immunometabolism. Nature Communications, 13(1), 7338. Distributed under Open Access license CC BY 4.0, without modification.

Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat
Clone
CBYCD-135
Antibody Isotype
IgG1, κ
Application
WB, IP, IF, ELISA, IHC-P

Basic Information

Immunogen
Amino acids 251-394 mapping mapping to the heavy chain of human cathepsin C.
Host Species
Mouse
Specificity
Human, Mouse, Rat
Antibody Isotype
IgG1, κ
Clonality
Monoclonal Antibody
Application Notes
ApplicationNote
WB1:100-1:1,000
IP1-2 μg per 100-500 μg of total protein (1 mL of cell lysate)
IF(ICC)1:50-1:500
ELISA1:100-1:1,000
IHC-P1:50-1:500

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

Format
Liquid
Buffer
Gelatin & PBS
Preservative
Sodium Azide
Concentration
0.2 mg/mL
Purity
>95% as determined by analysis by SDS-PAGE
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
Cathepsin C
Entrez Gene ID
1075
UniProt ID
P53634
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
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.
More Infomation

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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