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Human Monoclonal Cathepsin D Primary Antibody for 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
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Human Monoclonal Cathepsin D Primary Antibody for 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 4 Pubmed References
Human Monoclonal Cathepsin D Primary Antibody for 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 3 Pubmed References
Human Monoclonal Cathepsin D Primary Antibody for 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
Human Polyclonal Cathepsin D Primary Antibody for ELISA, IF (cc) - ABIN732098
Liao, Li, Li, Liu: Organellar proteome analyses of ricin toxin-treated HeLa cells. in Toxicology and industrial health 2014
Cow (Bovine) Polyclonal Cathepsin D Primary Antibody for WB - ABIN2776841
Gambarte Tudela, Capmany, Romao, Quintero, Miserey-Lenkei, Raposo, Goud, Damiani: The late endocytic Rab39a GTPase regulates the interaction between multivesicular bodies and chlamydial inclusions. in Journal of cell science 2015
Human Polyclonal Cathepsin D Primary Antibody for IP, WB - ABIN4288228
Sethna, Chamakkala, Gu, Thompson, Cao, Elliott, Finnemann: Regulation of Phagolysosomal Digestion by Caveolin-1 of the Retinal Pigment Epithelium Is Essential for Vision. in The Journal of biological chemistry 2016
Human Polyclonal Cathepsin D Primary Antibody for IHC, IHC (p) - ABIN4288229
Ahmad, Boisvert, Lundberg, Uhlen, Lamond: Systematic analysis of protein pools, isoforms, and modifications affecting turnover and subcellular localization. in Molecular & cellular proteomics : MCP 2012
Human Monoclonal Cathepsin D Primary Antibody for ELISA, WB - ABIN1582516
Zhang, Zhang, Shea, Xu, Tobin, Knapton, Sharron, Rouse: Autophagy in pancreatic acinar cells in caerulein-treated mice: immunolocalization of related proteins and their potential as markers of pancreatitis. in Toxicologic pathology 2014
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.
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 (show VPS52 Antibodies) 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 (show GABPA Antibodies) 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 (show CSTB Antibodies)). 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 (show PSAP Antibodies) precursor into saposins A-D. Myc (show MYC Antibodies)-CLN3 (show CLN3 Antibodies) colocalized with CTSD and activity of CTSD decreased as myc (show MYC Antibodies)-CLN3 (show CLN3 Antibodies) expression increased, and clearly decreased under hyperosmotic conditions
Study demonstrate that PGRN (show GRN Antibodies) interacts with the lysosomal protease CTSD and maintains its proper activity in vivo. Therefore, by regulating CTSD activity, PGRN (show GRN Antibodies) may modulate protein homeostasis. This could potentially explain the TDP-43 (show TARDBP Antibodies) aggregation observed in frontotemporal lobar degeneration with GRN (show GRN Antibodies) mutations.
Acid ceramidase (show ASAH1 Antibodies) inhibitor LCL521 targets lysosomes to activate cathepsin B (show CTSB Antibodies) 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 (show DNAJC5 Antibodies)-dependent cathepsins B and L, but not the Asp (show C3 Antibodies)-dependent cathepsin D.
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).
This study demonistrated that Mice heterozygous for cathepsin D deficiency exhibit mania-related behavior and stress-induced depression.
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 (show ALMS1 Antibodies).
Association of polymorphisms in calpain 1 (show CAPN1 Antibodies), (mu/I) large subunit, calpastatin (show CAST Antibodies), 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
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