The sodium/potassium ATPase is an integral membrane enzyme found in all cells of higher organisms and is responsible for the ATP-dependent transport of sodium and potassium across the cell membrane. This membrane-bound enzyme is related to a number of other ATPases including sarcoplasmic and endoplasmic reticulum calcium ATPase (SERCA) and plasma membrane calcium ATPase (PMCA). The sodium/potassium ATPase consists of a large, multipass, transmembrane catalytic subunit, termed the alpha subunit, and an associated smaller glycoprotein, termed the beta subunit. Studies indicate that there are three isoforms of the alpha subunit (alpha 1, alpha 2, alpha 3) and two isoforms of the beta subunit (beta 1 and beta 2) encoded by two multigene families. The different isoforms of the sodium/potassium ATPase exhibit tissue-specific and developmental patterns of expression. The alpha 1 and beta mRNAs are present in all cell types examined, whereas the alpha 2 and alpha 3 mRNAs exhibit a more restricted pattern of cell-specific expression. The alpha subunit has been found in kidney, brain, heart, and to a lesser extent liver, skeletal and smooth muscle.
Suitable for use in ELISA, Immunoprecipitation and Immunohistochemistry. Other applications not tested.
Immunohistochemistry: 1:1000. Staining in rat liver yeilds a pattern consistent with plasma membrane localization.
Optimal dilutions to be determined by the researcher.
Storage and Stability:
May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
| Not Determined |
|Purified rat kidney sodium/potassium ATPase. Epitope: Within an intracellular region at or near Asp-369 of the sodium/potassium ATPase alpha 1 subunit.|
|Supplied as a liquid in PBS, pH 7.2, 0.05% sodium azide.|
|Recognizes rat ATPase alpha 1, Na, K. Species Crossreactivity: human, canine and chicken.|
|Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.|
1. Schenk DB & Leffert HL Monoclonal antibodies to rat Na+,K+-ATPase block enzymatic activity. Proc Natl Acad Sci U S A 80:5281-5 (1983). 2. Simon FR et al. Hepatic Na(+)-K(+)-ATPase enzyme activity correlates with polarized beta-subunit expression. Am J Physiol 269:C69-84 (1995). 3. Ting-Beall HP et al. Identification of monoclonal antibody binding domains of Na+,K(+)-ATPase by immunoelectron microscopy. FEBS Lett 265:121-5 (1990). 4. Sweadner KJ Isozymes of the Na+/K+-ATPase. Biochim Biophys Acta 988:185-220 (1989). 5. Ariyasu RG et al. Distribution of (Na+ + K+)ATPase and sodium channels in skeletal muscle and electroplax. J Neurocytol 16:511-22 (1987). 6. Hubert J et al. Rat hepatic (Na+, K+)-ATPase: alpha-subunit isolation by immunoaffinity chromatography and structural analysis by peptide mapping. Biochemistry 25:4156-63 (1986). 7. Ariyasu RG et al. Localization of sodium/potassium adenosine triphosphatase in multiple cell types of the murine nervous system with antibodies raised against the enzyme from kidney. J Neurosci 5:2581-96 (1985). 8. Leffert HL et al. Hepatic (Na+,K+)-ATPase: a current view of its structure, function and localization in rat liver as revealed by studies with monoclonal antibodies. Hepatology 5:501-7 (1985). 9. Schenk DB et al. Use of a monoclonal antibody to quantify (Na+,K+)-ATPase activity and sites in normal and regenerating rat liver. J Biol Chem 259:14941-51 (1984). |