Human Recombinant CTSC protein, His Tag (V2LY-0526-LY2605)

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Basic Information

Expressed Host
HEK293 Cells
Protein Species
Human
Tag
His Tag
Protein Construction
This product is Human Recombinant CTSC protein, His Tag consist of Amino Acid: 1-463 and predicts a molecular mass of 51 kDa.
Molecule Mass
51 kDa
Sequence
Amino Acid: 1-463
Species
Human

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

Purity
>92% as determined by SDS-PAGE
Endotoxin
Please contact us for more information.
Format
Lyophilized
Reconstitution
Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.
Buffer
Lyophilized from sterile Tris, NaCl, Glycerol, Triton
Preservative
None
Storage
Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
More Infomation

Target

Full Name
Cathepsin C
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.

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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