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anti-Human ATP7A Antikörper:
anti-Mouse (Murine) ATP7A Antikörper:
anti-Rat (Rattus) ATP7A Antikörper:
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Human Polyclonal ATP7A Primary Antibody für IF (p), IHC (p) - ABIN731513
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 Polyclonal ATP7A Primary Antibody für ELISA - ABIN449703
Schlief, West, Craig, Holtzman, Gitlin: Role of the Menkes copper-transporting ATPase in NMDA receptor-mediated neuronal toxicity. in Proceedings of the National Academy of Sciences of the United States of America 2006
Mouse (Murine) Polyclonal ATP7A Primary Antibody für FACS, IHC (p) - ABIN2192174
Steveson, Ciccotosto, Ma, Mueller, Mains, Eipper: Menkes protein contributes to the function of peptidylglycine alpha-amidating monooxygenase. in Endocrinology 2002
A hierarchic gene expression of copper homeostatic genes was demonstrated between atp7a, sp1 (zeige SP1 Antikörper) and sod1 (zeige SOD1 Antikörper) in zebrafish.
The investigators interrogated a genetic screen for embryos phenocopied by copper deficiency, identifying calamity, a mutant defective in the zebrafish ortholog of the Menkes disease gene (atp7a).
Mutation in ATP7A gene is associated with X-linked distal hereditary motor neuropathy.
MNK orchestrates counterbalancing forces that regulate mTORC1 enzymatic activity.
11 single-nucleotide polymorphisms (SNPs) in CTR1 (zeige SLC31A1 Antikörper), CTR2 (zeige SLC31A2 Antikörper), ATP7A, and ATP7B (zeige ATP7B Antikörper) were genotyped in these patients.
The P-type copper ATPases ATP7A and ATP7B (zeige ATP7B Antikörper) 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 (zeige ATP7B Antikörper) and ATP7A, 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 (zeige ATP7B Antikörper) by copper-dependent changes in the dynamics and conformation of the MBD (zeige DPEP1 Antikörper) chain.
Deletion spanning exons 8 to 12 of the ATP7A gene is associated with a family affected with Menkes disease.
ATP-dependent copper transfer in ATP7A/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/B and are subjected to ATP-dependent vectorial displacement with a mechanism analogous to that of copper
studies show that merestinib effectively blocks eIF4E (zeige EIF4E Antikörper) phosphorylation in AML (zeige RUNX1 Antikörper) cells and suppresses primitive leukemic progenitors from AML (zeige RUNX1 Antikörper) patients in vitro and in an AML (zeige RUNX1 Antikörper) xenograft model in vivo.
It has been demonstrated in ovarian cancer cells that cisplatin resistance and uptake correlates with reduced CTR1 (zeige SLC31A1 Antikörper) and LRRC8A (zeige LRRC8A Antikörper) protein expression/activity and a concomitant upregulation in cisplatin exporting transporters (ATP7A, ATP7B (zeige ATP7B Antikörper)), which implies that the resistant cells have a reduced ability to accumulate cisplatin and activate proapoptotic transporters for osmolytes.
Thus, ATP7A activity protects mitochondria from excessive copper entry, which is deleterious to redox buffers. Mitochondrial redox misbalance could significantly contribute to pathologies associated with ATP7A inactivation in tissues with paradoxical accumulation of copper
Atp7a(T985I/Y) mice have reduced Atp7a protein levels and recapitulate the defective trafficking and altered post-translational regulatory mechanisms observed in the human ATP7A(T994I) patient fibroblasts
Cu chaperone function of Atox1 (zeige ATOX1 Antikörper) mediated through Cu transporter ATP7A is required for VEGF (zeige VEGFA Antikörper)-induced angiogenesis via activation of Cu enzyme lysyl oxidase (zeige LOX Antikörper).
CTR1 (zeige SLC31A1 Antikörper), ATP7A, and lysyl oxidase (zeige LOX Antikörper) were upregulated in the lung tissues and pulmonary arteries of mice with hypoxia-induced pulmonary hypertension and pulmonary arterial smooth muscle cells.
study characterized the Mottled-dappled deletion in C3H101H carrier females
Results from experiments in mouse model of Menkes disease harboring ATP5a (zeige ATP5G1 Antikörper) mutation, show increase expression of SOD1 (zeige SOD1 Antikörper) and induction of HO-1 (zeige HMOX1 Antikörper) causing iron metabolism disruption and hemolysis due to copper deficiency.
The MPhi ATP7A selectively regulates LPS (zeige TLR4 Antikörper)-induced inflammatory mediators, in part, via modulation of cellular copper availability, whereas neocuproine generally inhibits the production of inflammatory mediators.
a decrease in ATP7A protein expression contributes to impaired SOD3 (zeige SOD3 Antikörper) activity, resulting in O2(*-) overproduction and endothelial dysfunction in blood vessels of type 1 diabetes mellitus.
ATP7A mutations leading to Menkes disease and occipital horn syndrome in human and animal models [Review]
These studies demonstrate the essential role of the Atp7a gene in mouse embryonic development and establish a powerful model for understanding the tissue-specific roles of ATP7A in copper metabolism and disease.
This gene encodes a transmembrane protein that functions in copper transport across membranes. This protein is localized to the trans-Golgi network, where it is predicted to supply copper to copper-dependent enzymes in the secretory pathway. It relocalizes to the plasma membrane under conditions of elevated extracellular copper, and functions in the efflux of copper from cells. Mutations in this gene are associated with Menkes disease, X-linked cutis laxa, and occipital horn syndrome.
ATPase, Cu++ transporting, alpha polypeptide (Menkes syndrome)
, ATPase, Cu++ transporting, alpha polypeptide
, Menkes disease ATPase
, copper-transporting ATPase 1
, copper-transporting P-type ATPase
, copper-transporting ATPase
, ATPase protein
, Copper-transporting ATPase 1
, copper-transporting ATPase 1-like
, Cu++-transporting P-type ATPase
, Menkes disease-associated protein
, copper pump 1
, Menkes protein
, menkes disease-associated protein homolog
, copper transporting ATPase