Mouse Copper-Transporting ATPase1 Monoclonal Antibody | anti-ATP7A antibody

Copper Transporting ATPase 1 Antibody: ATTO 594

Cat. Num. AAA800627

• Gene Names: ATP7A; MK; MNK; DSMAX; SMAX3
• Reactivity: Human, Mouse, Rat
• Applications: Immunohistochemistry, Western Blot, Immunoprecipitation
• Synonyms: Copper-Transporting ATPase1; Monoclonal Antibody; Copper Transporting ATPase 1 Antibody: ATTO 594; ATP7A; ATP 7A; ATPase Cu transporting; DSMAX; FLJ17790; MC1; MC 1; MK; MNK; OHS; Copper pump 1; Menke; OTTHUMP00000062077; SMAX3; ATPase copper transporting alpha polypeptide; ATPase Cu++ transporting alpha polypeptide (Menkes syndrome); anti-ATP7A antibody

• Host: Mouse
• Reactivity: Human, Mouse, Rat
• Clonality: Monoclonal
• Isotype: IgG2b
• Clone Number: S60-4
• Form/Format: Protein G Purified
• Concentration: 1mg/mL (varies by lot)
• Sequence Length: 1500

• Applicable Applications for anti-ATP7A antibody: Immunohistochemistry (IHC), Western Blot (WB), Immunoprecipitation (IP)
• Application Notes: 1:1000 (WB)
• Conjugate: ATTO 594
• Storage Buffer: PBS pH7.2, 50% glycerol, 0.09% sodium azide
• Preparation and Storage: -20 degree C

Immunocytochemistry (ICC)

(Immunocytochemistry/Immunofluorescence analysis using Mouse Anti-Copper Transporting ATPase 1 Monoclonal Antibody, Clone S60-4 . Tissue: NIH 3T3 (NIH 3T3). Species: Mouse. Fixation: 4% Formaldehyde for 15 min at RT. Primary Antibody: Mouse Anti-Copper Transporting ATPase 1 Monoclonal Antibody at 1:100 for 60 min at RT. Secondary Antibody: Goat Anti-Mouse ATTO 488 at 1:200 for 60 min at RT. Counterstain: Phalloidin Texas Red F-Actin stain; DAPI (blue) nuclear stain at 1:1000, 1:5000 for 60 min at RT, 5 min at RT. Localization: Endoplasmic Reticulum, Cytoplasm, Golgi Apparatus, Trans-Golgi Network Membrane, Cell Membrane. Magnification: 60X. (A) DAPI (blue) nuclear stain. (B) Phalloidin Texas Red F-Actin stain. (C) Copper Transporting ATPase 1 Antibody. (D) Composite.)

Western Blot (WB)

(Western Blot analysis of Human SH-SY5Y showing detection of Copper Transporting ATPase 1 protein using Mouse Anti-Copper Transporting ATPase 1 Monoclonal Antibody, Clone S60-4 . Lane 1: MW Ladder. Lane 2: 10 ug SH-SY5Y. Load: 10 ug. Block: 5% Skim Milk powder in TBST. Primary Antibody: Mouse Anti-Copper Transporting ATPase 1 Monoclonal Antibody at 1:500 for 2 hours at RT with shaking. Secondary Antibody: Goat anti-mouse IgG:HRP at 1:4000 for 1 hour at RT with shaking. Color Development: Chemiluminescent for HRP (Moss) for 5 min in RT.)

Related Product Information for anti-ATP7A antibody

Background Info: Detects ~180kDa in rat brain membrane preparations.

Scientific Background: The copper efflux transporters ATP7A and ATP7B sequester intracellular copper into the vesicular secretory pathway for export from the cell. ATP7A (also known as Copper-transporting ATPase 1) functions as a transmembrane copper-trans locating P-type ATPase and plays a vital role in systemic copper absorption in the gut and copper reabsorption in the kidney. Polarized epithelial cells such as Madin-Darby canine kidney cells are a physiologically relevant model for systemic copper absorption and reabsorption in vivo. Although ATP7A is not detectable in most normal tissues, it is expressed in a considerable fraction of many common tumor types. Increased expression of ATP7A renders cells resistant to cisplatin and carboplatin. Mutations in the ATP7A gene result in Menkes disease, which is fatal in early childhood. Mutations in the ATP7B gene lead to the autosomal recessive disorder, Wilson disease, characterized by neurological symptoms and hepatic damage.

Product Categories/Family for anti-ATP7A antibody

Transporters

References

1. Samimi G., et al. (2003) Clin. Cancer Res. 9: 5853-9. 2. Samimi G., et al. (2004) Mol Pharmacol. 66: 25-32. 3. Greenough M., et al. (2004) Am. J. Physiol. Cell Physiol. 287: C1463-71. 4. Song, I.S., et al. (2004) Mol. Cancer Ther. 3: 1543-1549. 5. van Dongen, E.M., et al. (2004) Biochem. Biophys. Res. Commun. 323: 789-795. 6. Samimi, G., et al. (2004) Mol Pharmacol 66: 25-32. 7. Morgan, C.T., et al. (2004) J. Biol. Chem. 279: 36363-36371. 8. Barnes, N., et al. (2005) J. Biol. Chem. [Epub].

NCBI and Uniprot Product Information

• NCBI GI #: 115529486
• NCBI GeneID: 538
• NCBI Accession #: NP_000043.3
• NCBI GenBank Nucleotide #: NM_000052.5
• UniProt Accession #: Q04656; O00227; O00745; Q9BYY8; B1AT72
• Molecular Weight: 11,522 Da
• NCBI Official Full Name: copper-transporting ATPase 1
• NCBI Official Synonym Full Names: ATPase, Cu++ transporting, alpha polypeptide
• NCBI Official Symbol: ATP7A
• NCBI Official Synonym Symbols: MK; MNK; DSMAX; SMAX3
• NCBI Protein Information: copper-transporting ATPase 1; copper pump 1; Cu++-transporting P-type ATPase; Menkes disease-associated protein
• UniProt Protein Name: Copper-transporting ATPase 1
• UniProt Gene Name: ATP7A
• UniProt Synonym Gene Names: MC1; MNK
• UniProt Entry Name: ATP7A_HUMAN

NCBI Description

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 distal spinal muscular atrophy, and occipital horn syndrome. Alternatively-spliced transcript variants have been observed. [provided by RefSeq, Aug 2013]

Uniprot Description

ATP7A: a multi-pass membrane protein and cation transporting ATPase. A copper-transporter that may supply copper to copper-requiring proteins within the secretory pathway when localized in the trans-Golgi network. Cycles between the trans-Golgi network (TGN) and the plasma membrane. Predominantly found in the TGN and relocalizes to the plasma membrane in response to elevated extracellular copper levels where it functions in the efflux of copper from cells. Defects in ATP7A are the cause of Menkes syndrome (MD) and occipital horn syndrome (OHS). Six alternatively spliced isoforms have been described. The longest isoform has 6 transmembrane regions. Isoform 3, lacking all 6 transmembrane regions and 5 heavy-metal-associated (HMA) domains, is probably cytosolic. Isoform 6 lacks all transmembrane regions and 5 heavy-metal-associated (HMA) domains, but has a putative nuclear localization signal attached at the N-terminus.

Protein type: Hydrolase; Chaperone; Membrane protein, integral; Cell development/differentiation; EC 3.6.3.54; Apoptosis; Transporter, ion channel; Membrane protein, multi-pass; Transporter; Vesicle

Chromosomal Location of Human Ortholog: Xq21.1

Cellular Component: Golgi apparatus; neuron projection; brush border membrane; endoplasmic reticulum; basolateral plasma membrane; integral to membrane; trans-Golgi network; cytosol; secretory granule; trans-Golgi network transport vesicle; cell soma; membrane; perinuclear region of cytoplasm; late endosome; plasma membrane

Molecular Function: copper ion transmembrane transporter activity; protein binding; copper ion binding; copper-exporting ATPase activity; superoxide dismutase copper chaperone activity; ATP binding; copper-dependent protein binding

Biological Process: positive regulation of catalytic activity; skin development; extracellular matrix organization and biogenesis; collagen fibril organization; catecholamine metabolic process; dopamine metabolic process; norepinephrine biosynthetic process; plasma membrane copper ion transport; tryptophan metabolic process; negative regulation of neuron apoptosis; positive regulation of oxidoreductase activity; central nervous system neuron development; mitochondrion organization and biogenesis; release of cytochrome c from mitochondria; response to iron(III) ion; dendrite morphogenesis; detoxification of copper ion; ATP metabolic process; elastic fiber assembly; response to reactive oxygen species; regulation of gene expression; response to zinc ion; regulation of oxidative phosphorylation; cerebellar Purkinje cell differentiation; copper ion import; alveolus development; lactation; removal of superoxide radicals; pyramidal neuron development; locomotory behavior; norepinephrine metabolic process; peptidyl-lysine modification; epinephrine metabolic process; transmembrane transport; serotonin metabolic process; blood vessel development; negative regulation of metalloenzyme activity; hair follicle morphogenesis; cellular copper ion homeostasis; T-helper cell differentiation; in utero embryonic development; tyrosine metabolic process; positive regulation of metalloenzyme activity; copper ion transport; elastin biosynthetic process; pigmentation; cartilage development; blood vessel remodeling; copper ion export; neurite morphogenesis

Disease: Occipital Horn Syndrome; Menkes Disease; Spinal Muscular Atrophy, Distal, X-linked 3