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-3 subunit has been found in neuronal and to skeletal and cardiac muscle, lung and stomach tissues.
Applications:
Suitable for use in Immunocytochemistry/Immunofluorescence, Western Blot, Immunohistochemistry and Blocking/Neutralization. Other applications not tested.
Recommended Dilutions:
Immunofluorescence/ Immunocytochemistry: 5ug/ml
Western Blot: 1ug/ml detects a band at~110kD from canine skeletal muscle extract.
Immunohistochemistry (Frozen): 3ug/ml, Staining of rat retina yeilds a pattern consistant with plasma membrane localization.
Immunohistochemistry (Paraffin): 1:10-1:2000
Blocking/Neutralization: 1:10
Optimal dilutions to be determined by the researcher.
Positive Control: Human tonsil and prostate, rat retina
Storage and Stability:
May be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Aliquots are stable for 12 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.