Product Pathways - Cytoskeletal Signaling
Phospho-Na,K-ATPase α1 (Ser23) Antibody #4006
|4006S||100 µl (10 western blots)||---||In Stock||---|
|4006||carrier free and custom formulation / quantity||email request|
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Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting
Specificity / Sensitivity
Phospho-Na,K-ATPase α1 (Ser23) Antibody recognizes endogenous levels of Na,K-ATPase α1 only when phosphorylated at Ser23. The residue number, Ser23, is based on the sequence of the immature form of the protein, corresponding to Ser18 of the mature cleaved form.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser23 of rat Na,K-ATPase α1. Antibodies are purified using protein A and peptide affinity chromatography.
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, C541-566.
- Féraille, E. et al. (1999) Mol. Biol. Cell 10, 2847-2859.
- Fisone, G. et al. (1994) J. Biol. Chem. 269, 9368-9373.
- Feschenko, M.S. and Sweadner, K.J. (1995) J. Biol. Chem. 270, 14072-14077.
- Beguin, P. et al. (1994) J. Biol. Chem. 269, 24437-24445.
- Yingst, D.R. et al. (2004) Am. J. Physiol. Renal Physiol. 287, F713-F721.
- Al-Khalili, L. et al. (2004) J. Biol. Chem. 279, 25211-25218.
- Tian, J. et al. (2006) Mol. Biol. Cell 17, 317-326.
- Liang, M. et al. (2006) J. Biol. Chem. 281, 19709-19719.
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For Research Use Only. Not For Use In Diagnostic Procedures.
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