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anti-Human ATOX1 Antibodies:
anti-Mouse (Murine) ATOX1 Antibodies:
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Human Polyclonal ATOX1 Primary Antibody for ICC, IF - ABIN438544
Palm, Weise, Lundin, Wingsle, Nygren, Björn, Naredi, Wolf-Watz, Wittung-Stafshede: Cisplatin binds human copper chaperone Atox1 and promotes unfolding in vitro. in Proceedings of the National Academy of Sciences of the United States of America 2011
Show all 3 Pubmed References
Copper chaperone Atox-1 is involved in the induction of SOD3 in a monocyte cell line.
Since full occupancy of the tetrahedral cavity is a common feature of all Atox1 dimeric structures obtained with other metal ions (Cu(+), Cd(2+), and Hg(2+)), we propose that in the case of platinum, where the occupancy is only 0.4, the remaining cavities are occupied by Cu(+) ions
Data suggest that N-terminal segment of metal-binding domains (MBDs) 1-3 of ATOX1 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 activate ATP7B ATP hydrolysis. (ATOX1 = copper transport protein ATOX1; ATP7B = Cu-binding P type ATPase ATP7B)
It show that copper(I) and glutathione form large polymers with a molecular mass of approximately 8 kDa, which can transfer copper to Atox1.
Highlighted in this review are unique redox properties of Atox1 and other copper chaperones. Also, summarized are the redox nodes in the cytosol which potentially play dominant roles in the redox regulation of copper chaperones
The structural flexibility of the human copper chaperone Atox1 has been reported based on insights from combined pulsed EPR studies and computations.
Cu chaperone Atox1 has a role in breast cancer cell migration
Multiple genetic models identified genetic associations with systolic blood pressure and ATOX1.
In addition to Atox1, the human cytoplasm also contains Cu chaperones for loading of superoxide dismutase 1 (i.e. CCS) and cytochrome c oxidase in mitochondria (i.e. Cox17). [review]
results suggest the possibility of a therapy with copper-chelating or ionophore drugs in subtypes of tumors showing specific alterations in ATOX1 expression
C-Terminus of Human Copper Importer Ctr1 Acts as a Binding Site and Transfers Copper to Atox1
Cu chaperone function of Atox1 mediated through Cu transporter ATP7A is required for VEGF-induced angiogenesis via activation of Cu enzyme lysyl oxidase.
Upon neuronal differentiation, transitions in redox states upregulates expression of ATOX1 and its partner ATP7A, producing higher flux of copper through the secretory pathway.
To identify new interactions partners of Atox1, a yeast two-hybrid screen with a large human placenta library of cDNA fragments using Atox1 as bait, was performed.
Studied the localization of Atox1 in HeLa cells using fluorescence imaging in combination with in vitro binding experiments to fluorescently labeled DNA duplexes harboring the proposed promotor sequence.
Human cytoplasmic copper chaperones Atox1 and CCS exchange copper ions in vitro
Cisplatin is one of the most used anticancer drugs. Its cellular influx and delivery to target DNA may involve the copper chaperone Atox1 protein.
The data collected here shows that the Atox1 keeps its dimer nature also in the presence of the CTR1 c-terminal domain; however, two geometrical states are assumed by the Atox1.
The Cu-binding motif in Atox1, as well as in target Cu-binding domains of ATP7A/B, consists of a MX1CXXC motif where X1 = T.
Human Grx1 can catalyse reduction of Atox1 by glutathione but only in the presence of Cu(I).
Transduced Tat-ATOX1 markedly suppressed inflammatory responses in LPS-exposed Raw 264.7 cells and in a TPA-induced animal model by inhibition of pro-inflammatory mediator proteins, as well as activated NF-B and MAPK, suggesting that Tat-ATOX1 may contribute to the development of therapeutic proteins for the treatment of skin inflammation.
ATOX1 appeared ubiquitously expressed throughout the cells until compaction; in subsequent embryo stages, ATOX1 relocalized to cytoplasmic perinuclear domains in the inner cell mass. Silencing of Oct4 did not affect Atox1 expression, but silencing of Atox1 at the 2-cell stage strongly diminished Oct4 expression in 16-cell embryos.
Atox1 is involved in neointimal formation after vascular injury through promoting vascular smooth muscle cell migration and inflammatory cell recruitment in injured vessels
Atox1 functions to prevent Ang II-induced endothelial dysfunction and hypercontraction in resistant vessels, as well as hypertension.
the importance of Atox1, not only as a metallochaperone for delivering Cu to cuproenzymes, but also as a key player in maintaining the proper distribution and organization of Cu at the cellular level
ATOX1 is a cytoplasmic copper chaperone that interacts with the copper-binding domain of the membrane copper transporters ATP7A and ATP7B
Atox1 has a role in establishing the threshold for copper-dependent movement of the copper-transporting ATPases within the secretory compartment
Atox1 functions not only as a copper chaperone for SOD3 but also as a positive regulator for SOD3 transcription and may have an important role in modulating oxidative stress in the cardiovascular system.
Atox1 functions as a novel transcription factor that, when activated by copper, undergoes nuclear translocation, DNA binding, and transactivation, thereby contributing to cell proliferation.
both the copper chaperone and the transcription factor functions are required for the activity of antioxidant enzyme, superoxide dismutase (SOD3)
Atox1 is required for the polyubiquitination of Ctr1 and the Ctr1-mediated uptake of CDDP.
Although Cu concentration in metallothionein (MT)-knockout cells was increased by the knockdown of the copper chaperone, Atox1, the concentrations of 2 other copper metabolizing proteins were paradoxically increased.
Atox1 upregulates prion protein expression.
results clearly reveal a distorted copper homeostasis in Atox1-deficient Drosophila
This gene encodes a copper chaperone that plays a role in copper homeostasis by binding and transporting cytosolic copper to ATPase proteins in the trans-Golgi network for later incorporation to the ceruloplasmin. This protein also functions as an antioxidant against superoxide and hydrogen peroxide, and therefore, may play a significant role in cancer carcinogenesis. Because of its cytogenetic location, this gene represents a candidate gene for 5q-syndrome.
ATX1 antioxidant protein 1 homolog
, copper transport protein ATOX1
, metal transport protein ATX1
, copper chaperone
, Copper transport protein ATOX1
, ATX1 (antioxidant protein 1) homolog 1
, ATX1 homolog protein Rah1
, copper chaperone SAH
, ATX1 antioxidant protein 1 homolog (yeast)
, antioxidant protein 1 homolog