Technical Data
A4000-52A
ATPase alpha 1, Na, K
Description:
Na,K-ATPase is an integral membrane protein complex that hydrolyzes ATP to maintain the transmembrane gradients of Na+ and K+ found in most mammalian cells. The enzyme is comprised of an alpha and beta subunit. The alpha-polypeptide has been shown to be the catalytically active subunit, whereas the Beta-polypeptide appears to be necessary for the assembly and transport of the sodium pump to the plasma membrane. Na,K-ATPase alpha-1 subunit, in brain, is expressed in both neuronal and non-neuronal cells.

Applications:
Suitable for use in Western Blot, Immunohistochemistry and Immunofluorescence. Other applications have not been tested.

Recommended Dilution:
Western Blot: 1:1000-1:10,000 Detects a band at ~112kD. Do not boil the sample prior to loading on the gel (60C is sufficient).
Immunohistochemistry (Paraffin): 1:200
Immunofluorescence: 1:100-1:1000
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20C. 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.
TypeIsotypeCloneGrade
MabIgG1,k3C114Ascites
SizeStorageShippingSourceHost
50ul-20CBlue IceRabbitMouse
Concentration:
Not Determined
Immunogen:
Purified Na,K-ATPase from rabbit renal outer medulla
Purity:
Ascities
Form
Supplied as a liquid, 0.1% sodium azide.
Specificity:
Recognizes rabbit Na,K-ATPase alpha 1 subunit. Species Crossreactivity: Human, porcine, monkey, mouse, canine, sheep, rat and Xenopus. Note: This antibody has been used as a plasma membrane marker.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Pietrini, et al., Proc. Natl. Acad. Sci. USA 89: 8414 (1992). 2. Gottardi & Caplan, Science 260: 552 (1993). 3. Gottardi & Caplan, J. Biol. Chem. 268: 14,342 (1993). 4. Pietrini, et al., J. Biol. Chem. 269: 4668 (1994). 5. Van Why et al., Am. J. Physiol. 267: F75 (1994).