ATP7A Antibody, Clone L60/4: FITC

ATP7A, also known as copper-transporting ATPase 1, is a transmembrane P-type ATPase that plays a critical role in cellular copper homeostasis. It facilitates the export of excess intracellular copper by trafficking it into the secretory pathway for vesicular exocytosis. This function is essential for systemic copper absorption in the intestine and reabsorption in the kidney, processes that are effectively modeled in polarized epithelial systems such as Madin-Darby canine kidney (MDCK) cells. In the nervous system, ATP7A is indispensable for delivering copper to cuproenzymes involved in neurotransmitter synthesis, antioxidant defense, and mitochondrial function. Disruption of ATP7A-mediated copper transport leads to severe neurodevelopmental consequences, as seen in Menkes disease, a fatal X-linked disorder characterized by copper deficiency, neurodegeneration, and connective tissue abnormalities. Emerging research links ATP7A dysfunction to broader neurodegenerative processes. Impaired copper regulation contributes to oxidative stress, protein misfolding, and mitochondrial dysfunction—hallmarks of diseases such as Alzheimer’s and Parkinson’s. Moreover, ATP7A expression is altered in various cancers and has been associated with resistance to platinum-based chemotherapies like cisplatin and carboplatin. Given its dual role in systemic copper regulation and neuronal health, ATP7A is a promising target for therapeutic strategies aimed at restoring metal homeostasis in neurodegenerative diseases. Understanding its regulation and trafficking dynamics may unlock new avenues for intervention in copper-related neuropathologies.

ATP7A, ATP 7A, ATP7A_HUMAN, ATPase Cu transporting, ATPase copper transporting alpha polypeptide, ATPase Cu++ transporting alpha polypeptide (Menkes syndrome), Copper transporting ATPase 1, Cu++ transporting P type ATPase, Menkes disease associated protein, Menkes syndrome, Menke, MC1, MC 1, MK, MNK, DSMAX, SMAX3, OHS, FLJ17790, OTTHUMP00000062077

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.

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].

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].