Phospho-Na,K-ATPase α1 (Tyr10) (E1Y9C) Rabbit mAb #13566
- WB
Supporting Data
| REACTIVITY | H M |
| SENSITIVITY | Endogenous |
| MW (kDa) | 100 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
Storage
Protocol
Specificity / Sensitivity
Phospho-Na,K-ATPase α1 (Tyr10) (E1Y9C) Rabbit mAb recognizes endogenous levels of Na,K-ATPase α1 protein only when phosphorylated at Tyr10. The antibody cross-reacts with an induced 75-80 kDa doublet of unknown origin.
Species Reactivity:
Human, Mouse
The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.
Species predicted to react based on 100% sequence homology:
Rat, Bovine, Dog, Pig
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr10 of human Na,K-ATPase α1 protein.
Background
The Na,K-ATPase is an integral membrane heterodimer belonging to the P-type ATPase family. This ion channel uses the energy derived from ATP hydrolysis to maintain membrane potential by driving sodium export and potassium import across the plasma membrane against their electrochemical gradients. It is composed of a catalytic α subunit and a β subunit (reviewed in 1). Several phosphorylation sites have been identified for the α1 subunit. Tyr10 is phosphorylated by an as yet undetermined kinase (2), Ser16 and Ser23 are phosphorylated by PKC, and Ser943 is phosphorylated by PKA (3-5). All of these sites have been implicated in the regulation of enzyme activity in response to hormones and neurotransmitters, altering trafficking and kinetic properties of Na,K-ATPase. Altered phosphorylation in response to angiotensin II stimulates activity in the rat proximal tubule (6). Na,K-ATPase is also involved in other signal transduction pathways. Insulin regulates its localization in differentiated primary human skeletal muscle cells, and this regulation is dependent on ERK1/2 phosphorylation of the α subunit (7). Na,K-ATPase and Src form a signaling receptor complex that affects regulation of Src kinase activity and, subsequently, its downstream effectors (8,9).
- Therien, A.G. and Blostein, R. (2000) Am J Physiol Cell Physiol 279, C541-66.
- Féraille, E. et al. (1999) Mol Biol Cell 10, 2847-59.
- Fisone, G. et al. (1994) J Biol Chem 269, 9368-73.
- Feschenko, M.S. and Sweadner, K.J. (1995) J Biol Chem 270, 14072-7.
- Beguin, P. et al. (1994) J Biol Chem 269, 24437-45.
- Yingst, D.R. et al. (2004) Am J Physiol Renal Physiol 287, F713-21.
- Al-Khalili, L. et al. (2004) J Biol Chem 279, 25211-8.
- Tian, J. et al. (2006) Mol Biol Cell 17, 317-26.
- Liang, M. et al. (2006) J Biol Chem 281, 19709-19.
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