WH0000475M1
Monoclonal Anti-ATOX1 antibody produced in mouse
clone 2E6, purified immunoglobulin, buffered aqueous solution
Synonym(s):
Anti-ATX1, Anti-ATX1 antioxidant protein 1 homolog (yeast), Anti-HAH1, Anti-MGC138453, Anti-MGC138455
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About This Item
UNSPSC Code:
12352203
NACRES:
NA.41
biological source
mouse
Quality Level
conjugate
unconjugated
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
2E6, monoclonal
form
buffered aqueous solution
species reactivity
human
technique(s)
indirect ELISA: suitable
indirect immunofluorescence: suitable
western blot: 1-5 μg/mL
isotype
IgG2aκ
GenBank accession no.
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... ATOX1(475)
General description
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. (provided by RefSeq)
ATOX1 (antioxidant 1 copper chaperone) is a metallochaperone which is also called as HAH1. It is a small cytosolic protein. ATOX1 is located on human chromosome 5q33.
ATOX1 (antioxidant 1 copper chaperone) is a metallochaperone which is also called as HAH1. It is a small cytosolic protein. ATOX1 is located on human chromosome 5q33.
Immunogen
ATOX1 (NP_004036, 1 a.a. ~ 68 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.
Sequence
MPKHEFSVDMTCGGCAEAVSRVLNKLGGVKYDIDLPNKKVCIESEHSMDTLLATLKKTGKTVSYLGLE
Sequence
MPKHEFSVDMTCGGCAEAVSRVLNKLGGVKYDIDLPNKKVCIESEHSMDTLLATLKKTGKTVSYLGLE
Application
Monoclonal Anti-ATOX1 antibody has been used in immunoblot analysis.
Biochem/physiol Actions
ATOX1 (antioxidant 1 copper chaperone) participates in the human copper modulation system. It plays a major role in the migration of breast cancer cells. ATOX1 helps in the transportation of copper to the cell secretory pathway.
Features and Benefits
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Physical form
Solution in phosphate buffered saline, pH 7.4
Legal Information
GenBank is a registered trademark of United States Department of Health and Human Services
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Storage Class Code
10 - Combustible liquids
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
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ATOX1 gene silencing increases susceptibility to anticancer therapy based on copper ionophores or chelating drugs.
Barresi V, et al.
Journal of Inorganic Biochemistry, 156, 145-152 (2016)
Copper chaperone Atox1 plays role in breast cancer cell migration.
Blockhuys S and Wittung-Stafshede P
Biochemical and Biophysical Research Communications, 483(1), 301-304 (2017)
Copper chaperone ATOX1 is required for MAPK signaling and growth in BRAF mutation-positive melanoma.
Ye-Jin Kim et al.
Metallomics : integrated biometal science, 11(8), 1430-1440 (2019-07-19)
Copper (Cu) is a tightly regulated micronutrient that functions as a structural or catalytic cofactor for specific proteins essential for a diverse array of biological processes. While the study of the extremely rare genetic diseases, Menkes and Wilson, has highlighted
Metallochaperone Atox1 transfers copper to the NH2-terminal domain of the Wilson's disease protein and regulates its catalytic activity.
Walker JM, et al.
The Journal of Biological Chemistry, 277(31), 27953-27959 (2002)
The structural flexibility of the human copper chaperone Atox1: Insights from combined pulsed EPR studies and computations.
Levy AR, et al.
Protein Science, 26(8), 1609-1618 (2017)
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