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Mouse Anti-CTSD Recombinant Antibody (MM0127-6K22) (CBMAB-C11314-LY)


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Summary

Host Animal
Mouse
Specificity
Human
Clone
MM0127-6K22
Antibody Isotype
IgG1
Application
WB

Basic Information

Immunogen
AA 21-412
Specificity
Human
Antibody Isotype
IgG1
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!]

Format
Lyophilized
Concentration
0.5 mg/mL
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 D
Introduction
CTSD (Cathepsin D) is a Protein Coding gene. Diseases associated with CTSD include Ceroid Lipofuscinosis, Neuronal, 10 and Neuronal Ceroid Lipofuscinosis. Among its related pathways are Peptide hormone metabolism and Innate Immune System. Gene Ontology (GO) annotations related to this gene include aspartic-type endopeptidase activity. An important paralog of this gene is ENSG00000250644.
Entrez Gene ID
1509
UniProt ID
P07339
Alternative Names
Cathepsin D; Ceroid-Lipofuscinosis, Neuronal 10; EC 3.4.23.5; CPSD; Epididymis Secretory Sperm Binding Protein Li 130P; Cathepsin D (Lysosomal Aspartyl Protease);
Function
Acid protease active in intracellular protein breakdown. Plays a role in APP processing following cleavage and activation by ADAM30 which leads to APP degradation (PubMed:27333034).

Involved in the pathogenesis of several diseases such as breast cancer and possibly Alzheimer disease.
Biological Process
Antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
Collagen catabolic process Source: Reactome
Lipoprotein catabolic process Source: ARUK-UCL
Neutrophil degranulation Source: Reactome
Positive regulation of apoptotic process Source: ARUK-UCL
Positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: ARUK-UCL
Proteolysis Source: ARUK-UCL
Regulation of establishment of protein localization Source: ARUK-UCL
Cellular Location
Extracellular space; Lysosome; Melanosome. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. In aortic samples, detected as an extracellular protein loosely bound to the matrix (PubMed:20551380).
Involvement in disease
Ceroid lipofuscinosis, neuronal, 10 (CLN10):
A form of neuronal ceroid lipofuscinosis with onset at birth or early childhood. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material, and clinically by seizures, dementia, visual loss, and/or cerebral atrophy.
PTM
N- and O-glycosylated.
Undergoes proteolytic cleavage and activation by ADAM30.
As well as the major heavy chain which starts at Leu-169, 2 minor forms starting at Gly-170 and Gly-171 have been identified (PubMed:1426530). An additional form starting at Ala-168 has also been identified (PubMed:27333034).
More Infomation

Hossain, M. I., Marcus, J. M., Lee, J. H., Garcia, P. L., Singh, V., Shacka, J. J., ... & Andrabi, S. A. (2021). Restoration of CTSD (cathepsin D) and lysosomal function in stroke is neuroprotective. Autophagy, 17(6), 1330-1348.

Di, Y. Q., Han, X. L., Kang, X. L., Wang, D., Chen, C. H., Wang, J. X., & Zhao, X. F. (2021). Autophagy triggers CTSD (cathepsin D) maturation and localization inside cells to promote apoptosis. Autophagy, 17(5), 1170-1192.

Mijanovic, O., Petushkova, A. I., Brankovic, A., Turk, B., Solovieva, A. B., Nikitina, A. I., ... & Zamyatnin, A. A. (2021). Cathepsin D—Managing the Delicate Balance. Pharmaceutics, 13(6), 837.

Marques, A. R., Di Spiezio, A., Thießen, N., Schmidt, L., Grötzinger, J., Lüllmann-Rauch, R., ... & Saftig, P. (2020). Enzyme replacement therapy with recombinant pro-CTSD (cathepsin D) corrects defective proteolysis and autophagy in neuronal ceroid lipofuscinosis. Autophagy, 16(5), 811-825.

Zheng, W., Chen, Q., Wang, C., Yao, D., Zhu, L., Pan, Y., ... & Shao, C. (2020). Inhibition of Cathepsin D (CTSD) enhances radiosensitivity of glioblastoma cells by attenuating autophagy. Molecular Carcinogenesis, 59(6), 651-660.

Basu, S., Cheriyamundath, S., Gavert, N., Brabletz, T., Haase, G., & Ben-Ze’ev, A. (2019). Increased expression of cathepsin D is required for L1-mediated colon cancer progression. Oncotarget, 10(50), 5217.

Aghdassi, A. A., John, D. S., Sendler, M., Weiss, F. U., Reinheckel, T., Mayerle, J., & Lerch, M. M. (2018). Cathepsin D regulates cathepsin B activation and disease severity predominantly in inflammatory cells during experimental pancreatitis. Journal of Biological Chemistry, 293(3), 1018-1029.

Houben, T., Oligschlaeger, Y., Hendrikx, T., Bitorina, A. V., Walenbergh, S., van Gorp, P. J., ... & Shiri-Sverdlov, R. (2017). Cathepsin D regulates lipid metabolism in murine steatohepatitis. Scientific reports, 7(1), 1-10.

Zhou, X., Paushter, D. H., Feng, T., Pardon, C. M., Mendoza, C. S., & Hu, F. (2017). Regulation of cathepsin D activity by the FTLD protein progranulin. Acta neuropathologica, 134(1), 151-153.

Beel, S., Moisse, M., Damme, M., De Muynck, L., Robberecht, W., Van Den Bosch, L., ... & Van Damme, P. (2017). Progranulin functions as a cathepsin D chaperone to stimulate axonal outgrowth in vivo. Human molecular genetics, 26(15), 2850-2863.

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

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