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anti-Human ATP7B Antikörper:
anti-Mouse (Murine) ATP7B Antikörper:
anti-Rat (Rattus) ATP7B Antikörper:
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Human Polyclonal ATP7B Primary Antibody für ICC, IF - ABIN151824
Safaei, Otani, Larson, Rasmussen, Howell: Transport of cisplatin by the copper efflux transporter ATP7B. in Molecular pharmacology 2008
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Human Polyclonal ATP7B Primary Antibody für ICC, IF - ABIN151825
Guo, Nyasae, Braiterman, Hubbard: NH2-terminal signals in ATP7B Cu-ATPase mediate its Cu-dependent anterograde traffic in polarized hepatic cells. in American journal of physiology. Gastrointestinal and liver physiology 2005
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Human Polyclonal ATP7B Primary Antibody für IHC (p), WB - ABIN3042569
Wu, Yi, Sui, Jiang, Jiang, Zhao: Expression of ATP7B in human gastric cardiac carcinomas in comparison with distal gastric carcinomas. in World journal of gastroenterology 2006
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Human Polyclonal ATP7B Primary Antibody für IF (p), IHC (p) - ABIN733433
Wang, Zhu, Zhao, Wang: miR-133a enhances the sensitivity of Hep-2 cells and vincristine-resistant Hep-2v cells to cisplatin by downregulating ATP7B expression. in International journal of molecular medicine 2016
Human Monoclonal ATP7B Primary Antibody für ELISA, WB - ABIN560009
Ansede, Wright, St Claire, Hart, Gefroh, Brouwer: Characterization of sandwich-cultured hepatocytes as an in vitro model to assess the hepatobiliary disposition of copper. in Drug metabolism and disposition: the biological fate of chemicals 2009
Cow (Bovine) Monoclonal ATP7B Primary Antibody für FACS - ABIN2477128
McCabe: Antibiotics and endotoxic shock. in Bulletin of the New York Academy of Medicine 1976
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Cow (Bovine) Monoclonal ATP7B Primary Antibody für IHC (fro), IP - ABIN2477125
: Prazosin (Minipress) for hypertension. in The Medical letter on drugs and therapeutics 1977
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Cow (Bovine) Monoclonal ATP7B Primary Antibody für FACS - ABIN2477130
Mackay, Maddox, Brandon: A monoclonal antibody to the p220 component of sheep LCA identifies B cells and a unique lymphocyte subset. in Cellular immunology 1987
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Cow (Bovine) Monoclonal ATP7B Primary Antibody für FACS - ABIN2477127
Wijngaard, Metzelaar, MacHugh, Morrison, Clevers: Molecular characterization of the WC1 antigen expressed specifically on bovine CD4-CD8- gamma delta T lymphocytes. in Journal of immunology (Baltimore, Md. : 1950) 1992
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Our findings imply that reduced stability and enhanced dynamics of MBD1 (zeige DPEP1 Antikörper) or MBD6 (zeige MBD6 Antikörper) is the origin of ATP7B dysfunction in Wilson disease patients with the G85V or G591D mutation.
single nucleotide polymorphisms in ATP7B gene is associated with copper dysmetabolism in Alzheimer's disease.
Mutation in ATP7B gene is associated with copper dysmetabolism in Wilson disease.
We here demonstrate that ATP7B confers multidrug resistance by facilitating nuclear drug efflux and late endosomal drug sequestration.
Data suggest that N-terminal segment of metal-binding domains (MBDs) 1-3 of ATOX1 (zeige ATOX1 Antikörper) interact with nucleotide-binding domain of ATP7B, thus physically coupling the domains involved in copper binding and those involved in ATP hydrolysis; interactions with MBDs 1-3 of ATOX1 (zeige ATOX1 Antikörper) activate ATP7B ATP hydrolysis. (ATOX1 (zeige ATOX1 Antikörper) = copper transport protein ATOX1 (zeige ATOX1 Antikörper); ATP7B = Cu-binding P type ATPase (zeige ATP7A Antikörper) ATP7B)
11 single-nucleotide polymorphisms (SNPs) in CTR1 (zeige SLC31A1 Antikörper), CTR2 (zeige SLC31A2 Antikörper), ATP7A (zeige ATP7A Antikörper), and ATP7B were genotyped in these patients.
Wilson's disease results from mutations that cause absent or markedly diminished levels of ATP7B that can be determined in dried blood spots using a novel immune-SRM (zeige SRM Antikörper) assay.
The P-type copper ATPases ATP7A (zeige ATP7A Antikörper) and ATP7B provide an important system for acquisition, active transport, distribution and elimination of copper. Relevance of copper metabolism to human diseases and therapy is already known. It is quite certain that further studies will reveal detailed and useful information on biochemical mechanisms and relevance to diseases
the mechanism of copper-dependent regulation of ATP7B and ATP7A (zeige ATP7A Antikörper), the roles of individual MBDs, and the relationship between the regulatory and catalytic copper binding are still unknown. We describe the structure and dynamics of the MBDs, review the current knowledge about their functional roles and propose a mechanism of regulation of ATP7B by copper-dependent changes in the dynamics and conformation of the MBD (zeige DPEP1 Antikörper) chain.
ATP-dependent copper transfer in ATP7A (zeige ATP7A Antikörper)/B is not affected by varying the pH, suggesting that net proton counter-transport may not occur in copper ATPases. Platinum anticancer drugs activate ATP7A (zeige ATP7A Antikörper)/B and are subjected to ATP-dependent vectorial displacement with a mechanism analogous to that of copper
This study showed that knockout of Atp7b led to altered lipid metabolism and liver steatosis in the absence of inflammation.
ATP7B is transported from the trans-Golgi network (TGN (zeige TG Antikörper)) to the bile canaliculus by basolateral sorting and endocytosis, and microtubule-mediated transcytosis through the subapical compartment.
Data indicate that the copper-transporting ATPase (zeige DNAH8 Antikörper) gene (Atp7b) knockout mice showed a drastic, time-dependent accumulation of hepatic copper.
The aim of this study was to identify copper disturbances according to various brain compartments and further dissect the causal relationship between copper storage and neuronal damage using Atp7b(-/-) mice.
DKWSLLL sequence is essential for ATP7b sorting at the TGN (zeige TG Antikörper), transport from the TGN (zeige TG Antikörper) to the PM, endocytosis, and recycling to the TGN (zeige TG Antikörper) and PM.
Ligand-activated nuclear receptors FXR/NR1H4 (zeige NR1H4 Antikörper) and GR/NR3C1 (zeige NR3C1 Antikörper) and nuclear receptor interacting partners are less abundant in Atp7b(-/-) hepatocyte nuclei.
By performing dynamic PET, authors obtained the first real-time measurements of 64Cu distribution in the organs or tissues of Atp7b -/- mice.
Clusterin (zeige CLU Antikörper) and COMMD1 (zeige COMMD1 Antikörper) independently regulate degradation of the mammalian copper ATPases ATP7A (zeige ATP7A Antikörper) and ATP7B.
Neuroinflammatory and behavioural changes in the Atp7B mutant mouse model of Wilson's disease.
The Jackson toxic milk mouse as a model for copper loading
Data show that CD4 (zeige CD4 Antikörper)(+) and WC1(+) gammadelta T-cells were induced to produce IL-17 (zeige IL17A Antikörper) termed Th17 and gammadelta17 cells.
The endocytosis and signaling of the gamma-delta T cell coreceptor WC1 are regulated by a dileucine motif.
WC1 is a hybrid gamma-delta TCR coreceptor and pattern recognition receptor for pathogenic bacteria.
Identification of differences in the signal transduction through the endodomains of WC1 contributes to understanding the functional role of the WC1 coreceptors in the gammadelta T cell responses.
Specific receptors in the WC1 family directly participate in Leptospira recognition and/or activation of gamma-delta T cells.
These findings revealed that despite the existence of a distinct bovine CD4 (zeige CD4 Antikörper)(+)CD25 (zeige IL2RA Antikörper)(high) T cell population, which showed Foxp3 (zeige FOXP3 Antikörper) transcription/expression, natural regulatory activity did not reside in this cell population
Sudies demonstrate that WC1 molecules are encoded by a large, multi-gene family whose transcripts undergo extensive alternative splicing.
A copper-dependent ATPase (zeige DNAH8 Antikörper) hydrolysis in a native Golgi-enriched preparation from liver, was characterized.
This gene is a member of the P-type cation transport ATPase family and encodes a protein with several membrane-spanning domains, an ATPase consensus sequence, a hinge domain, a phosphorylation site, and at least 2 putative copper-binding sites. This protein functions as a monomer, exporting copper out of the cells, such as the efflux of hepatic copper into the bile. Alternate transcriptional splice variants, encoding different isoforms with distinct cellular localizations, have been characterized. Mutations in this gene have been associated with Wilson disease (WD).
ATPase, Cu(2+)- transporting, beta polypeptide
, Wilson disease-associated protein
, copper pump 2
, copper-transporting ATPase 2
, Wilson protein
, toxic milk
, wilson disease-associated protein homolog
, ATPase, Cu++ transporting, beta polypeptide (same as Wilson disease)
, PINA gene, promoter
, pineal night-specific ATPase
, ATPase, Cu++ transporting, beta polypeptide
, copper-transporting ATPase beta subunit
, ATPase 7B protein
, ATPase, Cu++ transporting, beta polypeptide (Wilson disease)
, Wilson's disease protein
, copper-transporting ATPase
, ATPase, Cu(2+)-transporting, beta polypeptide
, copper-transporting ATPase 2-like
, scavenger receptor cysteine-rich type 1 protein M160
, scavenger-receptor protein