Na(+)/K(+)-transporting ATPase (pan α subunit) Antibody [G11K19]

Application: Reactivity: Human, Mouse, Rat

Lane 1: A-172, Lane 2: SH-SY5Y, Lane 3: Mouse brain, Lane 4: Rat brain

Usage Information

Dilution
WB1:1000 IHC1:5000 IF1:50 FCM1:500

Application
WB, IHC, IF, FCM

Reactivity
Human, Mouse, Rat

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Observed MW
110 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight.

Datasheet & SDS

Biological Description

Specificity
Na(+)/K(+)-transporting ATPase (pan α subunit) Antibody [G11K19] detects endogenous levels of total Na(+)/K(+)-transporting ATPase (pan α subunit) protein.

Clone
G11K19

Synonym(s)
Sodium/potassium-transporting ATPase subunit alpha-1; Na(+)/K(+) ATPase alpha-1 subunit; Sodium pump subunit alpha-1; ATP1A1

Background
Na(+)/K(+)-transporting ATPase, commonly known as the sodium-potassium pump, is a P-type ATPase heterotrimer consisting of pan α subunit isoforms (α1–α4, ~110 kDa each with 10 transmembrane helices forming ion occlusion sites), a β subunit (chaperone, single TM), and an FXYD regulatory subunit, and is essential for maintaining Na+ and K+ electrochemical gradients across plasma membranes via ATP hydrolysis. In its E1 (cytoplasm-open) state, the α subunit's N (nucleotide-binding), P (phosphorylation), and A (actuator) cytoplasmic domains position ATP at Asp369 for high-affinity 3 Na+ ion binding within TM1–6, triggering γ-phosphate transfer and formation of the occluded E1P·3Na state. Major A/P/N domain rotations then reorient TM helices to the E2P (extracellular-open) conformation, expelling Na+ and enabling 2 K+ binding at lower-affinity TM5/6 sites with water displacement. Hydrolysis-driven E2-to-E1 reset, accelerated by low-affinity ATP, enables 3Na+:2K+ counter-transport (~10^4 ions/sec), establishing the negative resting membrane potential (–70 mV), supporting secondary active transport (e.g., Na+/glucose symporters, Na+/Ca2+ exchangers), enabling action potentials, osmoregulation, and secondary messenger signaling such as ouabain-induced Src activation. Isoform-specific roles include α1 for general homeostasis, α2 in neurons/glia for excitability, α3 in fast-spiking neurons, and α4 in sperm motility. Mutations (e.g., α2 in familial hemiplegic migraine) or inhibition (by cardiac glycosides) can lead to arrhythmias, epilepsy, hypertension, and cancer due to disrupted ion balance and signaling.

Background

Na(+)/K(+)-transporting ATPase, commonly known as the sodium-potassium pump, is a P-type ATPase heterotrimer consisting of pan α subunit isoforms (α1–α4, ~110 kDa each with 10 transmembrane helices forming ion occlusion sites), a β subunit (chaperone, single TM), and an FXYD regulatory subunit, and is essential for maintaining Na+ and K+ electrochemical gradients across plasma membranes via ATP hydrolysis. In its E1 (cytoplasm-open) state, the α subunit's N (nucleotide-binding), P (phosphorylation), and A (actuator) cytoplasmic domains position ATP at Asp369 for high-affinity 3 Na+ ion binding within TM1–6, triggering γ-phosphate transfer and formation of the occluded E1P·3Na state. Major A/P/N domain rotations then reorient TM helices to the E2P (extracellular-open) conformation, expelling Na+ and enabling 2 K+ binding at lower-affinity TM5/6 sites with water displacement. Hydrolysis-driven E2-to-E1 reset, accelerated by low-affinity ATP, enables 3Na+:2K+ counter-transport (~10^4 ions/sec), establishing the negative resting membrane potential (–70 mV), supporting secondary active transport (e.g., Na+/glucose symporters, Na+/Ca2+ exchangers), enabling action potentials, osmoregulation, and secondary messenger signaling such as ouabain-induced Src activation. Isoform-specific roles include α1 for general homeostasis, α2 in neurons/glia for excitability, α3 in fast-spiking neurons, and α4 in sperm motility. Mutations (e.g., α2 in familial hemiplegic migraine) or inhibition (by cardiac glycosides) can lead to arrhythmias, epilepsy, hypertension, and cancer due to disrupted ion balance and signaling.

References
https://pubmed.ncbi.nlm.nih.gov/34964112/ https://pubmed.ncbi.nlm.nih.gov/28634454/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%