Mouse Anti-CTSD Recombinant Antibody (P0252) (V2LY-0125-LY415)

Name: Mouse Anti-CTSD Recombinant Antibody (P0252)
SKU: V2LY-0125-LY415
Rating: 5 (1 reviews)

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Published Data

Mouse Anti-CTSD Recombinant Antibody (P0252) (V2LY-0125-LY415) in WB

The effect of aerobic training and Vitamin D3 supplementation on protein expression involved in autophagy in left ventricle. Quantification graphs of Cathepsin D proteins relative to B-actin. ...View More

Golpasandi, H., Rahimi, M. R., Ahmadi, S., Łubkowska, B., & Cięszczyk, P. (2023). Effects of vitamin D3 supplementation and aerobic training on autophagy signaling proteins in a rat model type 2 diabetes induced by high-fat diet and streptozotocin. Nutrients, 15(18), 4024. Distributed under Open Access license CC BY 4.0, without modification.

Mouse Anti-CTSD Recombinant Antibody (P0252) (V2LY-0125-LY415) in IF

Confocal immunofluorescence images of LAMP-1/2 (green; scale bar: 15 µm) and cathepsin D (green, scale bar: 10 µm) in RPTEC/TERT1 and NRK-52E cells treated with polymyxin B for 24 h. ...View More

Jarzina, S., Di Fiore, S., Ellinger, B., Reiser, P., Frank, S., Glaser, M., ... & Mally, A. (2022). Application of the adverse outcome pathway concept to in vitro nephrotoxicity assessment: kidney injury due to receptor-mediated endocytosis and lysosomal overload as a case study. Frontiers in Toxicology, 4, 864441. Distributed under Open Access license CC BY 4.0, without modification.

Mouse Anti-CTSD Recombinant Antibody (P0252) (V2LY-0125-LY415) in WB

Role of cathepsins in iota-toxin-induced cytotoxicity in MDCK cells. Small interfering RNAs (siRNAs) were used to reduce (A) cathepsin B (siCTSB), (B) cathepsin L (siCTSL), and (C) cathepsin D (siCTsD). Non-silencing siRNA was utilized as control siRNA (Con-siRNA). Western blots were used to evaluate decreased levels of cathepsins B, L, and D. Data are representative of three independent experiments. siRNA-transfected cells were treated with Ia (200 ng/mL) and Ib (500 ng/mL) for 4 h at 37 °C. About 100 MDCK cells were observed on microscopic pictures, and percentage of rounded cells was calculated. Data from five experiments are expressed as mean ± SD. One-way analysis of variance was used to assess significance. * P < 0.01, significant difference compared with intact plus iota-toxin. ...View More

Nagahama, M., Kobayashi, K., & Takehara, M. (2021). Cathepsin release from lysosomes promotes endocytosis of Clostridium perfringens iota-toxin. Toxins, 13(10), 721. Distributed under Open Access license CC BY 4.0, without modification.

Mouse Anti-CTSD Recombinant Antibody (P0252) (V2LY-0125-LY415) in WB

Western blots of lysosomal enzymes, CTSB, CTSD, GAA, and lysosomal transport protein M6PR. Represented images from 3 different experiments are on the top, and the quantifications are on the bottom. Mean ± SEM, unpaired two-tailed t test, *p< 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001. ...View More

Kilinc, S., Paisner, R., Camarda, R., Gupta, S., Momcilovic, O., Kohnz, R. A., ... & Goga, A. (2021). Oncogene-regulated release of extracellular vesicles. Developmental cell, 56(13), 1989-2006. Distributed under Open Access license CC BY 4.0, without modification.

Datasheet

SDS

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Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Host Animal

Mouse

Clone

P0252

Application

WB, IP, IF, ELISA, IHC-P

Immunogen

Amino acids 171-189 within an internal region of human cathepsin D.

Host Species

Mouse

Specificity

Human, Mouse, Rat

Antibody Isotype

IgG2b, κ

Clonality

Monoclonal Antibody

Application Notes

Application	Note
WB	1:100-1:1,000
IP	1-2 μg per 100-500 μg of total protein (1 mL of cell lysate)
IF(ICC)	1:50-1:500
ELISA	1:100-1:1,000
IHC-P	1:50-1:500

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

Format

Liquid

Buffer

Gelatin & PBS

Preservative

Sodium Azide

Concentration

0.2 mg/mL

Purity

>95% as determined by analysis by SDS-PAGE

Storage

Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

More Infomation

Target

Full Name

Cathepsin D

Entrez Gene ID

Human	1509
Mouse	13033
Rat	171293

UniProt ID

Human	P07339
Mouse	P18242
Rat	P24268

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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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme-Linked Immunospot (ELISpot)
Proteogenomics
Other Protocols

Antibody Pairs

CTSD Matched Antibody Pair (318) (CAT#: APMAB-318LY)

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Isotype control

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

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