Cat. No.: 512 015
Amount: 50 µg
Price:
$460.00
|
|
|
| Cat. No. 512 015 |
50 µg specific antibody, lyophilized. Affinity purified with the immunogen. Albumin and azide were added for stabilization. For reconstitution add 50 µl H2O to get a 1mg/ml solution in PBS. Then aliquot and store at -20°C to -80°C until use. Antibodies should be stored at +4°C when still lyophilized. Do not freeze! |
| Applications | |
| Immunogen | Synthetic peptide corresponding to residues surrounding AA 550 from human ATP1A2 (UniProt Id: P50993) |
| Reactivity |
Reacts with: rat (P06686), mouse (Q6PIE5). Other species not tested yet. |
| Specificity | The peptide sequence used for immunization is specific for subunit alpha-2 and should not recognize the other subunits alpha 1, 3 or 4. |
| Data sheet | 512_015.pdf |
|
|
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).