Use your antibodies-online credentials, if available.
Keine Produkte auf Ihrer Vergleichsliste.
Ihr Warenkorb ist leer.
Alle Spezies anzeigen
Weitere Synonyme anzeigen
Wählen Sie die Spezies und Applikation aus
anti-Human Cathepsin D Antikörper:
anti-Mouse (Murine) Cathepsin D Antikörper:
anti-Rat (Rattus) Cathepsin D Antikörper:
Sie gelangen zu unserer vorgefilterten Suche.
Human Monoclonal Cathepsin D Primary Antibody für WB - ABIN1882228
Burkard, Planyavsky, Kaupe, Breitwieser, Bürckstümmer, Bennett, Superti-Furga, Colinge: Initial characterization of the human central proteome. in BMC systems biology 2011
Show all 5 Pubmed References
Human Monoclonal Cathepsin D Primary Antibody für ELISA, EM - ABIN316063
Miyamoto, Kitamura, Nakamura, Futamura, Miyamoto, Yoshida, Ono, Ichinose, Arakawa: Possible existence of lysosome-like organella within mitochondria and its role in mitochondrial quality control. in PLoS ONE 2011
Show all 4 Pubmed References
Human Monoclonal Cathepsin D Primary Antibody für ELISA, EM - ABIN269482
Kitamura, Nakamura, Miyamoto, Miyamoto, Kabu, Yoshida, Futamura, Ichinose, Arakawa: Mieap, a p53-inducible protein, controls mitochondrial quality by repairing or eliminating unhealthy mitochondria. in PLoS ONE 2011
Show all 4 Pubmed References
Human Polyclonal Cathepsin D Primary Antibody für WB - ABIN541107
Liaudet-Coopman, Beaujouin, Derocq, Garcia, Glondu-Lassis, Laurent-Matha, Prébois, Rochefort, Vignon: Cathepsin D: newly discovered functions of a long-standing aspartic protease in cancer and apoptosis. in Cancer letters 2006
Show all 3 Pubmed References
Human Monoclonal Cathepsin D Primary Antibody für ELISA, WB - ABIN534419
Zaidi, Maurer, Nieke, Kalbacher: Cathepsin D: a cellular roadmap. in Biochemical and biophysical research communications 2008
Show all 2 Pubmed References
Human Polyclonal Cathepsin D Primary Antibody für ELISA, IF (cc) - ABIN732098
Liao, Li, Li, Liu: Organellar proteome analyses of ricin toxin-treated HeLa cells. in Toxicology and industrial health 2014
Human Polyclonal Cathepsin D Primary Antibody für IHC, ELISA - ABIN238943
Ahlemeyer, Halupczok, Rodenberg-Frank, Valerius, Baumgart-Vogt: Endogenous Murine Amyloid-β Peptide Assembles into Aggregates in the Aged C57BL/6J Mouse Suggesting These Animals as a Model to Study Pathogenesis of Amyloid-β Plaque Formation. in Journal of Alzheimer's disease : JAD 2017
Mouse (Murine) Polyclonal Cathepsin D Primary Antibody für IHC (p), WB - ABIN3042775
Zheng, Li, Wang, Wang, Liao, Hu, Fan, Kang, Zeng, Wu, Wu, Zhang, Wang, He et al.: Inhibition of autophagosome-lysosome fusion by ginsenoside Ro via the ESR2-NCF1-ROS pathway sensitizes esophageal cancer cells to 5-fluorouracil-induced cell death via the CHEK1-mediated DNA damage ... in Autophagy 2017
Human Monoclonal Cathepsin D Primary Antibody für IHC (p), IP - ABIN560534
Kam, Hennessy, Chua, Gan, Philp, Hon, Lai, Chan, Ong, Wong, Lim, Ling, Tan, Tan, Ho, Kon: Characterization of the human gastric fluid proteome reveals distinct pH-dependent protein profiles: implications for biomarker studies. in Journal of proteome research 2011
This is the first report showing a congenital myopathy caused by CD deficiency in a vertebrate experimental animal model.
phenotypic description of the lack of CD expression during zebrafish (Danio rerio) development
These results suggest that this 33 bp region could function as a promoter element in the tissue-specificity expression of BmCatD
These results suggest that the ecdysone response elements are vital for activation of the promoter by 20-hydroxyecdysone (20E) in the larval fat body and further support the crucial role of ecdysone signaling to control cathepsin D gene transcription.
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.
Newly diagnosed type 2 diabetes demonstrated significantly higher circulating cathepsin D concentrations than controls.
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.
Study results suggest that the CTSD rs17571 variant may not be associated with risk of Parkinson's disease, amyotrophic lateral sclerosis in Han Chinese.
VPS52 activated the apoptotic pathway through cathepsin D in gastric cancer cells.
Plasma cathepsin D correlates with histological classifications of fatty liver disease in adults.
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.
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.
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.
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.
apoptosis is accompanied by degradation of the cysteine cathepsin inhibitor stefin B (StfB). CatD did not exhibit a crucial role in this step. However, this degradation was partially prevented through pre-incubation with the antioxidant N-acetyl cysteine
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
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.
The S-nitrosation of a non-catalytic cysteine residue in the lysosomal aspartyl protease cathepsin D (CTSD) inhibited proteolytic activation.
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
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.
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.
Gene expression level of CTSD is significantly higher in AD patients when compared to normal controls.
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
Serum CTSB and CTSD concentrations were found to have a diagnostic value in NPC. However, the CTSB and CTSD serum levels had no prognostic role for the outcome in nasopharyngeal carcinoma patients.
Study shows that cathepsin D regulates lipid metabolism in murine steatohepatitis. These data demonstrate for the first time a key regulatory role for cathepsin D in lipid metabolism in the development of non-alcoholic steatohepatitis.
Acid ceramidase inhibitor LCL521 targets lysosomes to activate cathepsin B and cathepsin D, resulting in interrupted autophagy and ER stress that culminates in myeloid-suppressor cell death.
These results suggested that Purkinje cells (PCs) were more vulnerable to CTSD deficiency in lysosomes than to autophagy impairment, and this vulnerability does not depend on the severity of axonal swelling.
Exposure of J774A.1 cells to HOCl or HOSCN resulted in a significant decrease in the activity of the Cys-dependent cathepsins B and L, but not the Asp-dependent cathepsin D.
the cytosolic Cat D level and Cat D activity was significantly upregulated in response to oxygen-glucose deprivation/reperfusion exposure.
these results suggest that inhibition of lysosomal proteases, such as CtsD, could be a new therapeutic approach to reduce renal fibrosis and slow progression of chronic kidney disease.
The neuroectoderm specific cathepsin D (Ctsd) knock-out mice survived about 5.5 days longer.
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).
We therefore conclude that CD in pancreatic acinar cells is implicated in CB and CL degradation but not in autophagic activity.
This study demonistrated that Mice heterozygous for cathepsin D deficiency exhibit mania-related behavior and stress-induced depression.
A proteolytic cascade, involving cathepsins C and D, controls LLOMe-mediated necrosis.
Post-translational modifications drive CatD into the nucleus to cleave Histone 3 in the involuting mammary gland.
Increased lysosomal storage in CatD KO mice causes oxidative damage in brain pericytes, subsequently resulting in an increased vessel diameter and enhanced permeability of the BBB.
Mouse prolactin was proteolytically cleaved by Cath D between amino acids 148 and 149. N-terminal prolactin fragment and Cath D expression increased during mammary gland involution.
Cathepsin D was not inherent to sperm themselves, but rather of epididymal origin and was presumably transported to the sperm surface via epididymosomes.
TGase 2 may regulate the balance between cell survival and cell death through the modulation of CTSD levels.
These results suggest that increased release/activation of cathepsin D can trigger neurodegeneration and possibly development of Niemann-Pick type C disease pathology.
Relative position of thyroglobulin (Tg)peptide epitopes are identified based on homology to known Ctsd cleavage sites in rabbit Tg.
Three cathepsin D-specific cleavage sites in Bid, Phe24, Trp48, and Phe183, were identified.
Association of polymorphisms in calpain 1, (mu/I) large subunit, calpastatin, and cathepsin D genes with meat quality traits in double-muscled Piemontese cattle.
findings strongly suggest a link between the lysosomal dysfunction of cathepsin D and the etiology of Alzheimer's disease
g.70G>A polymorphism affects fatness and muscle deposition on SSC2p
Polymorphisms were discovered in several pig breeds, mostly in intron 4 and 5, including missense mutations, synonymous mutations, and intronic subsitutions.
The effect of heavy metal cations on the activity of cathepsin D, was studied.
This gene encodes a lysosomal aspartyl protease composed of a dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. This proteinase, which is a member of the peptidase C1 family, has a specificity similar to but narrower than that of pepsin A. Transcription of this gene is initiated from several sites, including one which is a start site for an estrogen-regulated transcript. Mutations in this gene are involved in the pathogenesis of several diseases, including breast cancer and possibly Alzheimer disease.
, cathepsin D
, aspartic protease
, cathepsin d
, preprocathepsin D
, ceroid-lipofuscinosis, neuronal 10
, lysosomal aspartyl peptidase
, lysosomal aspartyl protease
, cathepsin D (lysosomal aspartyl peptidase)
, cathepsin D (lysosomal aspartyl protease)
, prepro-cathepsin D, prepro-CD