Phospho-Na,K-ATPase α1 (Ser16) Antibody #4020
- WB
Supporting Data
| REACTIVITY | R |
| SENSITIVITY | Endogenous |
| MW (kDa) | 100 |
| SOURCE | Rabbit |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- R-Rat
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
Storage
Protocol
Specificity / Sensitivity
Phospho-Na,K-ATPase α1 (Ser16) Antibody recognizes endogenous levels of Na,K-ATPase α1 only when phosphorylated at Ser16. The residue number, Ser16, is based on the sequence of the immature form of the protein, corresponding to Ser11 of the mature cleaved form.
Species Reactivity:
Rat
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:
Mouse, Bovine, Pig
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser16 of rat Na,K-ATPase α1. Antibodies are purified using protein A and peptide affinity chromatography.
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).
Limited Uses
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