Recombinant Human Cathepsin D (CTSD) Protein (GST)

Name: Recombinant Human Cathepsin D (CTSD) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-07884P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Cathepsin D (CTSD) Protein (GST) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P07339
Target Symbol	CTSD
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	IPEVLKNYMDAQYYGEIGIGTPPQCFTVVFDTGSSNLWVPSIHCKLLDIACWIHHKYNSDKSSTYVKNGTSFDIHYGSGSLSGYLSQDTVSVPCQSASSASALGGVKVERQVFGEATKQPGITFIAAKFDGILGMAYPRISVNNVLPVFDNLMQQKLVDQNIFSFYLSRDPDAQPGGELMLGGTDSKYYKGSLSYLNVTRKAYWQVHLDQVEVASGLTLCKEGCEAIVDTGTSLMVGPVDEVRELQKAIGAVPLIQGEYMIPCEKVSTLPAITLKLGGKGYKLSPEDYTLKVSQAGKTLCLSGFMGMDIPPPSGPLWILGDVFIGRYYTVFDRDNNR
Expression Range	67-403aa
Protein Length	Partial
Mol. Weight	63.8 kDa
Research Area	Neuroscience
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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	HGNC: 2529 OMIM: 116840 KEGG: hsa:1509 STRING: 9606.ENSP00000236671 UniGene: PMID: 29501392 Newly diagnosed type 2 diabetes demonstrated significantly higher circulating cathepsin D concentrations than controls. PMID: 29375176 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 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 VPS52 activated the apoptotic pathway through cathepsin D in gastric cancer cells. PMID: 28791438 Plasma cathepsin D correlates with histological classifications of fatty liver disease in adults. PMID: 27922112 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 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 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 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 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 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 The S-nitrosation of a non-catalytic cysteine residue in the lysosomal aspartyl protease cathepsin D (CTSD) inhibited proteolytic activation. PMID: 27291402 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 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 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 Gene expression level of CTSD is significantly higher in AD patients when compared to normal controls. PMID: 26943237 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 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 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 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 Transcellular transmission of alpha-synuclein aggregates is increased in CTSD mutated cells. PMID: 26448324 Serum CatD activity as a marker of healthy endogenous phagocytosis and remodeling was impaired in patients with new-onset cardiac dysfunction. PMID: 25911051 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 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 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 Fenhexamid and cyprodinil can promote ovarian cancer metastasis by increasing the protein expression of cathepsin D via an estrogen receptor dependent pathway. PMID: 26344002 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 Human Herpesvirus 8-encoded viral interleukin-6 promotes endoplasmic reticulum-associated degradation of procathepsin D. PMID: 26018151 NOS-3 overexpression resulted in an increased sensitivity to anti-Fas induced cell death, independently of AR expression and CatD activity. PMID: 25712867 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 No differences in Cathepsin D were observed in the study when comparing male breast cancer tissues to those of female patients. PMID: 24656773 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 CTSD, FKBP10, and SLC2A1 are novel genes that participate in the acquisition and maintenance of the adriamycin-resistant phenotype in leukemia cells. PMID: 24467213 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 In this meta-analysis no association is found betweeen cathepsin D C224T polymorphism and the risk of Alzheimer's disease. PMID: 24423188 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 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 Determination of cathepsin D status in breast cancer might identify patients at different risk for relapse PMID: 24044567 These data point to an evident correlation between cathepsins S and D expression and clinical stage of relapsing-remitting multiple sclerosis PMID: 23439581 Upregulation of cathepsin D may be critically involved in the malignant transformation and progression of melanocytic tumors. PMID: 24511668 Human herpesvirus 8 IL6 contributes to primary effusion lymphoma cell viability via suppression of cathepsin D interaction with VKORC1v2. PMID: 24198402 Cathepsin D release from lysosomes and subsequent Bid cleavage is mediated by exposure of cells to an HSP70 inhibitor. PMID: 23868063 Substrate specificities and proteolytic cleavage characterisitics of human cathepsin D. PMID: 23840360 A Cathepsin D variant co-segregating with PSEN1 mutation was linked to cerebellar dysfunction and dementia. PMID: 23415546 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 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 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 Cathepsin D activity was decreased in ATP13A2-knockdown cells that displayed lysosome-like bodies characterized by fingerprint-like structures PMID: 23499937 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

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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.

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