Copper Transporting ATPase 1 Antibody
Copper Transporting ATPase 1 Antibody, Clone S60-4
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, IHC, ICC, IP |
---|---|
Primary Accession | Q04656 |
Other Accession | NP_000043.3 |
Host | Mouse |
Isotype | IgG2b |
Reactivity | Human, Mouse, Rat |
Clonality | Monoclonal |
Description | Mouse Anti-Human Copper Transporting ATPase 1 Monoclonal IgG2b |
Target/Specificity | Detects ~180kDa in rat brain membrane preparations. |
Other Names | ATP7A Antibody, ATP 7A Antibody, ATPase Cu transporting Antibody, DSMAX Antibody, FLJ17790 Antibody, MC1 Antibody, MC 1 Antibody, MK Antibody, MNK Antibody, OHS Antibody, Copper pump 1 Antibody, Menke Antibody, OTTHUMP00000062077 Antibody, SMAX3 Antibody, ATPase copper transporting alpha polypeptide Antibody, ATPase Cu++ transporting alpha polypeptide (Menkes syndrome) Antibody, Copper transporting ATPase 1 Antibody, Cu++ transporting P type ATPase Antibody, Menkes disease associated protein Antibody, Menkes syndrome Antibody |
Clone Names | S60-4 |
Immunogen | Synthetic peptide amino acids 42-61 (cytoplasmic C-terminus) of human Copper- transporting ATPase1 |
Purification | Protein G Purified |
Storage | -20ºC |
Storage Buffer | PBS pH7.4, 50% glycerol, 0.09% sodium azide |
Shipping Temperature | Blue Ice or 4ºC |
Certificate of Analysis | 1 µg/ml of SMC-398 was sufficient for detection of Copper-transporting ATPase1 in 20 µg of rat brain lysate by colorimetric immunoblot analysis using Goat IgG:HRP as the secondary antibody. |
Cellular Localization | Endoplasmic Reticulum | Cytoplasm | Golgi Apparatus | Trans-Golgi Network Membrane | Cell Membrane |
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Provided below are standard protocols that you may find useful for product applications.
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.
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].
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