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anti-Human ATOX1 Antibodies:
anti-Mouse (Murine) ATOX1 Antibodies:
anti-Rat (Rattus) 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 (show SOD3 Antibodies) 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 (show CD2 Antibodies)+), 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 (show ATP7B Antibodies), thus physically coupling the domains involved in copper binding and those involved in ATP hydrolysis; interactions with MBDs 1-3 of ATOX1 activate ATP7B (show ATP7B Antibodies) ATP hydrolysis. (ATOX1 = copper transport protein ATOX1; ATP7B (show ATP7B Antibodies) = Cu-binding P type ATPase (show ATP7A Antibodies) ATP7B (show ATP7B Antibodies))
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 (show EREG Antibodies) 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 (show SOD1 Antibodies) (i.e. CCS (show CCS Antibodies)) and cytochrome c (show CYCS Antibodies) oxidase in mitochondria (i.e. Cox17 (show COX17 Antibodies)). [review]
results suggest the possibility of a therapy with copper-chelating or ionophore drugs in subtypes of tumors showing specific alterations in ATOX1 expression
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 (show POU5F1 Antibodies) did not affect Atox1 expression, but silencing of Atox1 at the 2-cell stage strongly diminished Oct4 (show POU5F1 Antibodies) expression in 16-cell embryos.
Cu chaperone function of Atox1 mediated through Cu transporter ATP7A (show ATP7A Antibodies) is required for VEGF (show VEGFA Antibodies)-induced angiogenesis via activation of Cu enzyme lysyl oxidase (show LOX Antibodies).
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 (show AGT Antibodies)-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 (show ATP7A Antibodies) and ATP7B (show ATP7B Antibodies)
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 (show SOD3 Antibodies) but also as a positive regulator for SOD3 (show SOD3 Antibodies) 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 (show SOD3 Antibodies))
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