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anti-Human Cathepsin D Antibodies:
anti-Mouse (Murine) Cathepsin D Antibodies:
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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 - 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 Monoclonal Cathepsin D Primary Antibody for IF, IP - ABIN968184
Erickson, Conner, Blobel: Biosynthesis of a lysosomal enzyme. Partial structure of two transient and functionally distinct NH2-terminal sequences in cathepsin D. in The Journal of biological chemistry 1981
Show all 4 Pubmed References
Human Monoclonal Cathepsin D Primary Antibody for IF, IP - ABIN968183
Faust, Kornfeld, Chirgwin: Cloning and sequence analysis of cDNA for human cathepsin D. in Proceedings of the National Academy of Sciences of the United States of America 1985
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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 2 Pubmed References
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 ELISA, IF (cc) - ABIN732098
Liao, Li, Li, Liu: Organellar proteome analyses of ricin toxin-treated HeLa cells. in Toxicology and industrial health 2014
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
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
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
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.
Secreted PGRN (show GRN Antibodies) is incorporated into cells via sortilin (show SORT1 Antibodies) or cation-independent mannose 6-phosphate receptor (show IGF2R Antibodies), and facilitated the acidification of lysosomes and degradation of CTSDmat. Moreover, the change of PGRN (show GRN Antibodies) levels led to a cell-type-specific increase of insoluble TDP-43 (show TARDBP Antibodies). In the brain tissue of FTLD-TDP patients with PGRN (show GRN Antibodies) deficiency, CTSD and phosphorylated TDP-43 (show TARDBP Antibodies) 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 (show CASP8 Antibodies) and Bid (show BID Antibodies) 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 (show FLNA Antibodies)% and cathepsin D levels. Cathepsin D, which is known to be associated with atherosclerosis, may play a role in the proce
Serum CTSB (show CTSB Antibodies) and CTSD concentrations were found to have a diagnostic value in NPC (show NPC1 Antibodies). However, the CTSB (show CTSB Antibodies) and CTSD serum levels had no prognostic role for the outcome in nasopharyngeal carcinoma patients.
Fibroblasts from Niemann-Pick type C (NPC (show NPC1 Antibodies)) disease patients with low levels of NPC1 (show NPC1 Antibodies) protein have high amounts of procathepsin D but reduced quantities of the mature protein, thus showing a diminished cathepsin D activity.
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).
Data show that co-silencing of tricho-rhino-phalangeal-syndrome (TRPS1 (show TRPS1 Antibodies)) and cathepsin D (Cath-D) in breast cancer cells (BCC) affects the transcription of cell cycle and proliferation.
Transcellular transmission of alpha-synuclein (show SNCA Antibodies) aggregates is increased in CTSD mutated cells.
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.
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).
Mouse prolactin (show PRL Antibodies) was proteolytically cleaved by Cath D between amino acids 148 and 149. N-terminal prolactin (show PRL Antibodies) 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.
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