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ATP1A2 antibody - 512 004

ATP1A2 is the catalytic subunit of the Na+/K+ transporting ATPase expressed in glia cells in the brain
Guinea pig polyclonal antiserum
Cat. No.: 512 004
Amount: 100 µl
Price: $365.00
Cat. No. 512 004 100 µl antiserum, lyophilized. For reconstitution add 100 µl H2O, then aliquot and store at -20°C until use.
Antibodies should be stored at +4°C when still lyophilized. Do not freeze!
Applications
 
WB: 1 : 1000 up to 1 : 2000 (AP-staining) gallery  
ICC: 1 : 500 up to 1 : 1000 gallery  
Immunogen Two synthetic peptides corresponding to residues near the carboxy terminus and surrounding AA 550, respectively from human ATP1A2 (UniProt Id: P50993)
Reactivity Reacts with: mouse (P06686), rat (Q6PIE5).
Other species not tested yet.
Specificity The peptide sequences used for immunization are specific for subunit alpha-2 and should not recognize the other subunits alpha 1, 3 or 4.
Data sheet 512_004.pdf
Cat. No.: 512 004
Amount: 100 µl
Price: $365.00
Background

ATP1A2, also referred to as Sodium/potassium-transporting ATPase subunit alpha-2, is the catalytic subunit of the enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This process is essential for maintaining the asymmetrical distribution of Na+ and K+ ions and the resting membrane potential, thereby providing the energy needed for active nutrient transport.
A functional Na+/K+ ATPase consists of a catalytic α-subunit, which contains the ATP-binding sites, and a smaller β-subunit, necessary for full enzymatic activity and serving as an anchoring protein. Auxiliary proteins, such as γ subunits (FXYD polypeptides), further modify the enzyme's transport properties.
Currently, four catalytic (α) and two glycoprotein (β) subunits have been identified, each distributed in a highly tissue- and cell-specific manner. In the brain, three α subunit isoforms (α1, α2, and α3) are expressed: ATP1A1 is present in all cell types, ATP1A3 is primarily found in neurons, and ATP1A2 is almost exclusively expressed in glial cells (1).
Specific roles for glial Na+/K+-ATPases, and specifically the α2-subunit containing enzyme include a contribution to K+ homeostasis and to neurotransmitter (notably glutamate) clearing from the synaptic cleft. Interestingly, it has been shown that a glial Sodium/potassium-transporting ATPase containing the α2 subunit is recruited in response to glutamate uptake and is necessary to couple neuronal activity to glucose utilization (2).