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ATP7A Antibody (internal region)

Peptide-affinity purified goat antibody

     
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Product Information
Application
  • Applications Legend:
  • WB=Western Blot
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin-embedded Sections)
  • IHC-F=Immunohistochemistry (Frozen Sections)
  • IF=Immunofluorescence
  • FC=Flow Cytopmetry
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • E=ELISA
  • IP=Immunoprecipitation
  • DB=Dot Blot
  • CHIP=Chromatin Immunoprecipitation
  • FA=Fluorescence Assay
  • IEM=Immuno electron microscopy
  • EIA=Enzyme Immunoassay
E
Primary Accession Q04656
Other Accession NP_000043.3, 538
Predicted Human
Host Goat
Clonality Polyclonal
Concentration 0.5 mg/ml
Isotype IgG
Calculated MW 163373 Da
Additional Information
Gene ID 538
Other Names Copper-transporting ATPase 1, 3.6.3.54, Copper pump 1, Menkes disease-associated protein, ATP7A, MC1, MNK
Format 0.5 mg/ml in Tris saline, 0.02% sodium azide, pH7.3 with 0.5% bovine serum albumin
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsATP7A Antibody (internal region) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name ATP7A {ECO:0000303|PubMed:28389643, ECO:0000312|HGNC:HGNC:869}
Function ATP-driven copper (Cu(+)) ion pump that plays an important role in intracellular copper ion homeostasis (PubMed:10419525, PubMed:11092760, PubMed:28389643). Within a catalytic cycle, acquires Cu(+) ion from donor protein on the cytoplasmic side of the membrane and delivers it to acceptor protein on the lumenal side. The transfer of Cu(+) ion across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation that shifts the pump conformation from inward-facing to outward-facing state (PubMed:10419525, PubMed:19453293, PubMed:19917612, PubMed:28389643, PubMed:31283225). Under physiological conditions, at low cytosolic copper concentration, it is localized at the trans-Golgi network (TGN) where it transfers Cu(+) ions to cuproenzymes of the secretory pathway (PubMed:11092760, PubMed:28389643). Upon elevated cytosolic copper concentrations, it relocalizes to the plasma membrane where it is responsible for the export of excess Cu(+) ions (PubMed:10419525, PubMed:28389643). May play a dual role in neuron function and survival by regulating cooper efflux and neuronal transmission at the synapse as well as by supplying Cu(+) ions to enzymes such as PAM, TYR and SOD3 (By similarity) (PubMed:28389643). In the melanosomes of pigmented cells, provides copper cofactor to TYR to form an active TYR holoenzyme for melanin biosynthesis (By similarity).
Cellular Location Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein Melanosome membrane {ECO:0000250|UniProtKB:Q64430}; Multi-pass membrane protein. Early endosome membrane {ECO:0000250|UniProtKB:Q64430}; Multi-pass membrane protein. Cell projection, axon {ECO:0000250|UniProtKB:P70705} Cell projection, dendrite {ECO:0000250|UniProtKB:P70705}. Postsynaptic density {ECO:0000250|UniProtKB:P70705}. Note=Cycles constitutively between the TGN and the plasma membrane (PubMed:9147644). Predominantly found in the TGN and relocalized to the plasma membrane in response to elevated copper levels. Targeting into melanosomes is regulated by BLOC-1 complex (By similarity). In response to glutamate, translocates to neuron processes with a minor fraction at extrasynaptic sites (By similarity). {ECO:0000250|UniProtKB:P70705, ECO:0000250|UniProtKB:Q64430, ECO:0000269|PubMed:9147644} [Isoform 5]: Endoplasmic reticulum
Tissue Location Widely expressed including in heart, brain, lung, muscle, kidney, pancreas, and to a lesser extent placenta (PubMed:8490646, PubMed:8490659). Expressed in fibroblasts, aortic smooth muscle cells, aortic endothelial cells and umbilical vein endothelial cells (at protein level) (PubMed:16371425)
Research Areas
Citations (0)
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References

Role of the Menkes copper-transporting ATPase in NMDA receptor-mediated neuronal toxicity. Schlief ML, West T, Craig AM, Holtzman DM, Gitlin JD. Proc Natl Acad Sci U S A. 2006 Oct 3;103(40):14919-24. Epub 2006 Sep 26. PMID: 17003121

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$ 216.00
Cat# AF2750a
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