Anti-Beta 1 Na+/K+ ATPase (extracellular) Antibody

Antibodies

Sodium-Potassium ATPase Subunit Beta 1, ATP1B, ATP1B1

Shipped at room temperature. Product as supplied can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C

Lyophilized powder. Reconstituted antibody contains phosphate buffered saline (PBS), pH 7.4

Sodium-Potassium ATPase Subunit Beta 1, ATP1B, ATP1B1 - A Rabbit Polyclonal antibody to Beta 1 Na+/K+ ATPase (extracellular)

Rat, human - identical

Confirmed by amino acid analysis and mass spectrometry

0.8 mg/ml

Extracellular, C-terminus.

Mouse

41116161

Ion channels are multimeric proteins located in the plasma membrane that play a critical role in the regulation of cellular processes1. The gradient of sodium (Na+) and potassium (K+) across the plasma membrane is regulated by the Na+/K+-ATPase enzyme complex. Na/K-ATPase hydrolyzes one ATP molecule in order to pump three Na+ ions out of the cell and two K+ ions into the cell during every pumping cycle. Na+/K+-ATPase activity is vital for sodium and potassium homeostasis in cells, which are important for numerous enzymatic functions and secondary transport of different molecules2. Na+/K+-ATPase is a heteromeric transmembrane protein complex consisting of α- and β-subunits and a regulatory subunit belonging to the FXYD proteins. The catalytic α-subunit is responsible for transport activities and contain 10 transmembrane domains (TMDs). The β-subunit is heavily glycosylated and function as a molecular chaperone. The association of the β-subunit increases the stability of the catalytic α-subunit and dictates the affinity toward sodium and potassium. In addition, the β-subunit is necessary for the complex migration into the plasma membrane3.β-subunits has three different isoforms β-1, β-2 and β-3 that consist of small N-terminal (30-AA), a TM helix and large C-terminal (240-AA) with different tissue specificities. β-1 found to have additional role in the response of cells to oxidative stress via glutathionylation of a cysteine residue located at the center of the TMD, the same cysteine is absent in the other beta subunits4.