Recombinant Human proCathepsin D Protein

Beta LifeScience SKU/CAT #: BLA-7302P

Recombinant Human proCathepsin D Protein

Beta LifeScience SKU/CAT #: BLA-7302P
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Host Species Human
Accession P07339
Synonym CATD_HUMAN Cathepsin D cathepsin D (lysosomal aspartyl protease) Cathepsin D heavy chain Ceroid-lipofuscinosis, neuronal 10 CLN10 CPSD ctsd EC 3.4.23 EC Lysosomal aspartyl peptidase Lysosomal aspartyl protease MGC2311 OTTHUMP00000042282 OTTHUMP00000196039 OTTHUMP00000198692
Description Recombinant Human proCathepsin D Protein was expressed in HEK293. It is a Full length protein
Source HEK293
Molecular Weight 44 kDa including tags
Purity Greater than 95% SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Formulation Liquid Solution
Stability The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution See related COA
Unit Definition For Research Use Only
Storage Buffer Shipped at 4°C. Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

Target Details

Target 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. Involved in the pathogenesis of several diseases such as breast cancer and possibly Alzheimer disease.
Subcellular Location Lysosome. Melanosome. Secreted, extracellular space.
Protein Families Peptidase A1 family
Database References
Associated Diseases Ceroid lipofuscinosis, neuronal, 10 (CLN10)
Tissue Specificity Expressed in the aorta extracellular space (at protein level). Expressed in liver (at protein level).

Gene Functions References

  1. CatD plays a major role in intracellular advanced glycation end products (AGEs) degradation. Decreased CatD expression and activity impairs intracellular AGEs degradation in photoaged fibroblasts. PMID: 29501392
  2. Newly diagnosed type 2 diabetes demonstrated significantly higher circulating cathepsin D concentrations than controls. PMID: 29375176
  3. This work identifies PGRN as an activator of lysosomal cathepsin D activity, and suggests that decreased cathepsin D activity due to loss of PGRN contributes to both FTD and NCL pathology in a dose-dependent manner. PMID: 29036611
  4. Study results suggest that the CTSD rs17571 variant may not be associated with risk of Parkinson's disease, amyotrophic lateral sclerosis in Han Chinese. PMID: 28917980
  5. VPS52 activated the apoptotic pathway through cathepsin D in gastric cancer cells. PMID: 28791438
  6. Plasma cathepsin D correlates with histological classifications of fatty liver disease in adults. PMID: 27922112
  7. Study shows that CtsD expression was upregulated in damaged tubular cells in nephrotoxic and ischemia reperfusion induced acute kidney injury (AKI) models. Also, the results provide compelling evidence for CtsD as an important mediator for apoptotic cell death during AKI. PMID: 27271556
  8. Epithelial ovarian (EOC) cancer secreted Cathepsin D acts as an extracellular ligand and may play an important pro-angiogenic, and thus pro-metastatic, role by activating the omental microvasculature during EOC metastasis to the omentum. PMID: 29024694
  9. Results show that lowering endogenous cathepsin D abundance induced senescence in HeLa cells, leading to reduced cell proliferation, impaired tumorigenesis in a mouse model, and increased permeability of lysosomal membrane and reactive oxygen species accumulation. These results suggest that CTSD is involved in cancer cells in maintaining lysosomal integrity, redox balance, and Nrf2 activity, thus promoting tumorigenesis. PMID: 26657266
  10. Data suggest that, compared to control individuals, serum cathepsin-D levels are up-regulated in patients with T2DM-Y (young onset type 2 diabetes) with and without diabetic retinopathy. This study was conducted in India. PMID: 28336215
  11. The lysosomal enzyme cathepsin D (CTSD) mediates the proteolytic cleavage of PSAP precursor into saposins A-D. Myc-CLN3 colocalized with CTSD and activity of CTSD decreased as myc-CLN3 expression increased, and clearly decreased under hyperosmotic conditions PMID: 28390177
  12. Study demonstrate that PGRN interacts with the lysosomal protease CTSD and maintains its proper activity in vivo. Therefore, by regulating CTSD activity, PGRN may modulate protein homeostasis. This could potentially explain the TDP-43 aggregation observed in frontotemporal lobar degeneration with GRN mutations. PMID: 28493053
  13. The S-nitrosation of a non-catalytic cysteine residue in the lysosomal aspartyl protease cathepsin D (CTSD) inhibited proteolytic activation. PMID: 27291402
  14. Secreted PGRN is incorporated into cells via sortilin or cation-independent mannose 6-phosphate receptor, and facilitated the acidification of lysosomes and degradation of CTSDmat. Moreover, the change of PGRN levels led to a cell-type-specific increase of insoluble TDP-43. In the brain tissue of FTLD-TDP patients with PGRN deficiency, CTSD and phosphorylated TDP-43 accumulated in neurons PMID: 28073925
  15. CTSD, in need of its catalytic activity, may promote proliferation in advanced glycation end products-treated human umbilical vein endothelial cells independent of the autophagy-lysosome pathway. PMID: 28218663
  16. Cathepsin D facilitates the TRAIL-induced apoptosis of MDA-MB-231 breast cancer cells in enzymatic activity-dependent manner. Caspase-8 and Bid proteins are the CD targets. The modulatory role of CD in cell response to TRAIL was also confirmed in another breast cancer cell line SKBR3. PMID: 26867770
  17. Gene expression level of CTSD is significantly higher in AD patients when compared to normal controls. PMID: 26943237
  18. There was a significant difference between groups with and without endothelial dysfunction in terms of cathepsin D levels, and negative and significant correlations were found between brachial artery FMD% and cathepsin D levels. Cathepsin D, which is known to be associated with atherosclerosis, may play a role in the proce PMID: 25611836
  19. Fibroblasts from Niemann-Pick type C (NPC) disease patients with low levels of NPC1 protein have high amounts of procathepsin D but reduced quantities of the mature protein, thus showing a diminished cathepsin D activity. PMID: 26507101
  20. Data indicate that cathepsin D (CD) protein is elevated in the retinas of diabetic mice and serum of human patients with diabetic macular edema (DME). PMID: 26718887
  21. Data show that co-silencing of tricho-rhino-phalangeal-syndrome (TRPS1) and cathepsin D (Cath-D) in breast cancer cells (BCC) affects the transcription of cell cycle and proliferation. PMID: 26183398
  22. Transcellular transmission of alpha-synuclein aggregates is increased in CTSD mutated cells. PMID: 26448324
  23. Serum CatD activity as a marker of healthy endogenous phagocytosis and remodeling was impaired in patients with new-onset cardiac dysfunction. PMID: 25911051
  24. study provides evidence that hTERT overexpression is responsible for the upregulation of the cysteine protease cathepsin D by regulating EGR-1 to activate invasiveness in cancer progression PMID: 26519755
  25. A proteomics workflow identified CTSD as an over-expressed protein in osteosarcomas and pulmonary metastases and may thus serve as a new biomarker for individualized treatment regimes for patients with osteosarcomas, even at metastastic stage. PMID: 26203049
  26. the clues provided by the yeast model unveiled a novel CatD function in the degradation of damaged mitochondria when autophagy is impaired, which protects colorectal cancer cells from acetate-induced apoptosis. PMID: 26086961
  27. Fenhexamid and cyprodinil can promote ovarian cancer metastasis by increasing the protein expression of cathepsin D via an estrogen receptor dependent pathway. PMID: 26344002
  28. Variations in CTSD and MnSOD showed no association with the development of Alzheimer's Disease, whereas the presence of the Ala224Val polymorphism in CTSD had a positive association with the development of AD PMID: 26351775
  29. Human Herpesvirus 8-encoded viral interleukin-6 promotes endoplasmic reticulum-associated degradation of procathepsin D. PMID: 26018151
  30. NOS-3 overexpression resulted in an increased sensitivity to anti-Fas induced cell death, independently of AR expression and CatD activity. PMID: 25712867
  31. These results suggest that decreased expression of cathepsin D in the peripheral monocytes is a potential signature of Alzheimer disease,and that this decreased expression is involved in Abeta degradation and Alzheimer disease pathogenesis. PMID: 24898658
  32. No differences in Cathepsin D were observed in the study when comparing male breast cancer tissues to those of female patients. PMID: 24656773
  33. T-carrying genotype is associated with a 2.5-fold increased risk for developing Alzheimer disease compared to C/C genotype. There was also a synergistic interaction with APOE epsilon4 leading to a 6.25-fold increased risk of the disease. PMID: 24281128
  34. CTSD, FKBP10, and SLC2A1 are novel genes that participate in the acquisition and maintenance of the adriamycin-resistant phenotype in leukemia cells. PMID: 24467213
  35. Knockdown of cathepsin D (CD) expression mediated by siRNA significantly inhibited the in vitro invasion of two hepatocellular carcinoma cell lines, SNU449 and SNU473, which normally secrete high-levels of CD. PMID: 24259486
  36. In this meta-analysis no association is found betweeen cathepsin D C224T polymorphism and the risk of Alzheimer's disease. PMID: 24423188
  37. Cathepsin D levels are reduced in patients with preeclampsia in Korean population.Cathepsin D level is an important factor that may contribute to the pathogenesis of preeclampsia. PMID: 23954850
  38. These data provide a better understanding of Cathepsin D behavior in tumor microenvironment conditions and this knowledge can be used to develop more specific tools for diagnosis and drug delivery. PMID: 23871913
  39. Determination of cathepsin D status in breast cancer might identify patients at different risk for relapse PMID: 24044567
  40. These data point to an evident correlation between cathepsins S and D expression and clinical stage of relapsing-remitting multiple sclerosis PMID: 23439581
  41. Upregulation of cathepsin D may be critically involved in the malignant transformation and progression of melanocytic tumors. PMID: 24511668
  42. Human herpesvirus 8 IL6 contributes to primary effusion lymphoma cell viability via suppression of cathepsin D interaction with VKORC1v2. PMID: 24198402
  43. Cathepsin D release from lysosomes and subsequent Bid cleavage is mediated by exposure of cells to an HSP70 inhibitor. PMID: 23868063
  44. Substrate specificities and proteolytic cleavage characterisitics of human cathepsin D. PMID: 23840360
  45. A Cathepsin D variant co-segregating with PSEN1 mutation was linked to cerebellar dysfunction and dementia. PMID: 23415546
  46. Quantification of immunohistochemistry showed that there is no difference in the global expression of CTSD, CTSH and CTSK between asthmatics and non-asthmatics. PMID: 23483898
  47. The beta-hairpin loop of human pro-cathepsin D, absent in the zebrafish protein, acts as recognition peptide for the enzymes involved in post translational processing. PMID: 23107604
  48. a model of Aven activation by which its N-terminal inhibitory domain is removed by CathD-mediated proteolysis, thereby unleashing its cytoprotective function. PMID: 22388353
  49. Cathepsin D activity was decreased in ATP13A2-knockdown cells that displayed lysosome-like bodies characterized by fingerprint-like structures PMID: 23499937
  50. Data indicate that a serum biomarker panel consisting of CA19-9, cathepsin D, and MMP-7 may provide the most effective screening test currently feasible for Pancreatic ductal adenocarcinoma. PMID: 23065739


Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

Recently viewed