This CTSG protein is a semi-custom product. There are 5 expression system options: Yeast, E. coli, In Vivo Biotinylation in E. coli, Baculovirus, and Mammalian cell. Your requirements will be given top priority in determining the protein tags. For proteins within 800 aa, risk-free custom service is guaranteed. It means you will not be charged if the protein cannot be delivered.
CTSG is a serine protease primarily found in azurophilic granules of leukocytes, particularly neutrophils [1]. It converts angiotensin I to angiotensin II or cleaves angiotensin II from a plasma protein substrate [4][5]. CTSG plays an important role in inflammation and tissue damage at sites of inflammation [2]. CTSG participates in various physiological processes, including apoptosis and platelet activation [2][3].
Studies have shown that CTSG has a dual trypsin-and chymotrypsin-like specificity and can exert antibacterial effects against pathogens such as Staphylococcus aureus and Pseudomonas aeruginosa [6][7]. Furthermore, CTSG has a potential role in cancer progression as evidence shows that CTSG is associated with cancer stem cells in head and neck cutaneous squamous cell carcinoma and oral tongue squamous cell carcinoma [8][9]. CTSG has been linked to heart failure [10].
References:
[1] E. Glusa and C. Adam, Endothelium‐dependent relaxation induced by cathepsin g in porcine pulmonary arteries, British Journal of Pharmacology, vol. 133, no. 3, p. 422-428, 2001. https://doi.org/10.1038/sj.bjp.0704089
[2] A. Sabri, S. Alcott, H. Elouardighi, E. Pak, C. Derian, P. Andrade‐Gordonet al., Neutrophil cathepsin g promotes detachment-induced cardiomyocyte apoptosis via a protease-activated receptor-independent mechanism, Journal of Biological Chemistry, vol. 278, no. 26, p. 23944-23954, 2003. https://doi.org/10.1074/jbc.m302718200
[3] G. Sambrano, W. Huang, T. Faruqi, S. Mahrus, C. Craik, & S. Coughlin, Cathepsin g activates protease-activated receptor-4 in human platelets, Journal of Biological Chemistry, vol. 275, no. 10, p. 6819-6823, 2000. https://doi.org/10.1074/jbc.275.10.6819
[4] B. Wintroub, L. Klickstein, V. Dzau, & K. Watt, Granulocyte-angiotensin system. identification of angiotensinogen as the plasma protein substrate of leukocyte cathepsin g, Biochemistry, vol. 23, no. 2, p. 227-232, 1984. https://doi.org/10.1021/bi00297a009
[5] M. Tonnesen, M. Klempner, K. Austen, & B. Wintroub, Identification of a human neutrophil angiotension ii-generating protease as cathepsin g., Journal of Clinical Investigation, vol. 69, no. 1, p. 25-30, 1982. https://doi.org/10.1172/jci110437
[6] W. Shafer, M. Shepherd, B. Boltin, L. Wells, & J. Pohl, Synthetic peptides of human lysosomal cathepsin g with potent antipseudomonal activity, Infection and Immunity, vol. 61, no. 5, p. 1900-1908, 1993. https://doi.org/10.1128/iai.61.5.1900-1908.1993
[7] L. Avril, M. Martino-Ferrer, G. Pignède, M. Séman, & F. Gauthier, Identification of the u‐937 membrane‐associated proteinase interacting with the v3 loop of hiv‐1 gp12o as cathepsin g, Febs Letters, vol. 345, no. 1, p. 81-86, 1994. https://doi.org/10.1016/0014-5793(94)00410-2
[8] T. Featherston, H. Brasch, S. Siljee, B. Schaijik, J. Patel, J. Jonghet al., Cancer stem cells in head and neck cutaneous squamous cell carcinoma express cathepsins, Plastic and Reconstructive Surgery Global Open, vol. 8, no. 8, p. e3042, 2020. https://doi.org/10.1097/gox.0000000000003042
[9] T. Featherston, R. Marsh, B. Schaijik, H. Brasch, S. Tan, & T. Itinteang, Expression and localization of cathepsins b, d, and g in two cancer stem cell subpopulations in moderately differentiated oral tongue squamous cell carcinoma, Frontiers in Medicine, vol. 4, 2017. https://doi.org/10.3389/fmed.2017.00100
[10] B. Ilkhanizadeh, A. Shirpoor, M. Ansari, S. Nemati, & Y. Rasmi, Protective effects of ginger (zingiber officinale) extract against diabetes-induced heart abnormality in rats, Diabetes & Metabolism Journal, vol. 40, no. 1, p. 46, 2016. https://doi.org/10.4093/dmj.2016.40.1.46
