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Rat Anti-CTSD Recombinant Antibody (RM0162-7D22) (CBMAB-1487-CN)

This product is a rat antibody that recognizes CTSD of mouse. The antibody RM0162-7D22 can be used for immunoassay techniques such as: WB.
See all CTSD antibodies

Summary

Host Animal
Rat
Specificity
Mouse
Clone
RM0162-7D22
Antibody Isotype
IgG2
Application
WB

Basic Information

Immunogen
Mouse Cathepsin D.
Specificity
Mouse
Antibody Isotype
IgG2
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
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS, Trehalose.
Concentration
LYOPH
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Cathepsin D
Introduction
This gene encodes a member of the A1 family of peptidases. The encoded preproprotein is proteolytically processed to generate multiple protein products. These products include the cathepsin D light and heavy chains, which heterodimerize to form the mature enzyme. This enzyme exhibits pepsin-like activity and plays a role in protein turnover and in the proteolytic activation of hormones and growth factors. This protein plays a role in APP processing following cleavage and activation by ADAM30 which leads to APP degradation.
Entrez Gene ID
UniProt ID
Alternative Names
CD; CatD
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).

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.

Custom Antibody Labeling

We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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