Mouse Recombinant CTSD protein, His Tag (V2LY-0526-LY7923)

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Basic Information

Expressed Host
HEK293 Cells
Protein Species
Mouse
Tag
His Tag
Protein Construction
This product is Mouse Recombinant CTSD protein, His Tag consist of Amino Acid: 1-410 and predicts a molecular mass of 44.4 kDa.
Molecule Mass
44.4 kDa
Sequence
Amino Acid: 1-410
Species
Mouse

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

Purity
≥90% 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 PBS
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 D
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.

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