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anti-Human Cathepsin D Antikörper:
anti-Mouse (Murine) Cathepsin D Antikörper:
anti-Rat (Rattus) Cathepsin D Antikörper:
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Human Monoclonal Cathepsin D Primary Antibody für IF, IP - ABIN968183
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
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Human Monoclonal Cathepsin D Primary Antibody für IF, IP - ABIN968184
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 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
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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
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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
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Human Monoclonal Cathepsin D Primary Antibody für 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 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
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 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 für 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
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.
apoptosis is accompanied by degradation of the cysteine cathepsin inhibitor stefin B (StfB (zeige CSTB Antikörper)). 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 (zeige PSAP Antikörper) precursor into saposins A-D. Myc (zeige MYC Antikörper)-CLN3 (zeige CLN3 Antikörper) colocalized with CTSD and activity of CTSD decreased as myc (zeige MYC Antikörper)-CLN3 (zeige CLN3 Antikörper) expression increased, and clearly decreased under hyperosmotic conditions
Study demonstrate that PGRN (zeige GRN Antikörper) interacts with the lysosomal protease CTSD and maintains its proper activity in vivo. Therefore, by regulating CTSD activity, PGRN (zeige GRN Antikörper) may modulate protein homeostasis. This could potentially explain the TDP-43 (zeige TARDBP Antikörper) aggregation observed in frontotemporal lobar degeneration with GRN (zeige GRN Antikörper) mutations.
The S-nitrosation of a non-catalytic cysteine residue in the lysosomal aspartyl protease cathepsin D (CTSD) inhibited proteolytic activation.
Secreted PGRN (zeige GRN Antikörper) is incorporated into cells via sortilin (zeige SORT1 Antikörper) or cation-independent mannose 6-phosphate receptor (zeige IGF2R Antikörper), and facilitated the acidification of lysosomes and degradation of CTSDmat. Moreover, the change of PGRN (zeige GRN Antikörper) levels led to a cell-type-specific increase of insoluble TDP-43 (zeige TARDBP Antikörper). In the brain tissue of FTLD-TDP patients with PGRN (zeige GRN Antikörper) deficiency, CTSD and phosphorylated TDP-43 (zeige TARDBP Antikörper) 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 (zeige CASP8 Antikörper) and Bid (zeige BID Antikörper) 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 (zeige FLNA Antikörper)% and cathepsin D levels. Cathepsin D, which is known to be associated with atherosclerosis, may play a role in the proce
Serum CTSB (zeige CTSB Antikörper) and CTSD concentrations were found to have a diagnostic value in NPC (zeige NPC1 Antikörper). However, the CTSB (zeige CTSB Antikörper) and CTSD serum levels had no prognostic role for the outcome in nasopharyngeal carcinoma patients.
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 (zeige DNAJC5 Antikörper)-dependent cathepsins B and L, but not the Asp (zeige C3 Antikörper)-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 (zeige ALMS1 Antikörper).
Mouse prolactin (zeige PRL Antikörper) was proteolytically cleaved by Cath D between amino acids 148 and 149. N-terminal prolactin (zeige PRL Antikörper) fragment and Cath D expression increased during mammary gland involution.
Association of polymorphisms in calpain 1 (zeige CAPN1 Antikörper), (mu/I) large subunit, calpastatin (zeige CAST Antikörper), 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