Anti-Beta 2 Na+/K+ ATPase (extracellular)-FITC Antibody

FC, LCI

ATP1B2, Sodium/potassium-transporting ATPase subunit beta-2, Adhesion molecule on glia, AMOG

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

ATP1B2, Sodium/potassium-transporting ATPase subunit beta-2, Adhesion molecule on glia, AMOG - A Rabbit Polyclonal Antibody to ?-Opioid Receptor (extracellular) conjugated to the fluorescent dye FITC

Human - identical, mouse 13 out of 14 amino acid residues identical

Confirmed by amino acid analysis and mass spectrometry

1 mg/ml

Extracellular, C-terminus

Rat

41116161

P-type ATPases are a large family of molecular pumps that exploit a phosphorylated enzyme intermediate in a two-step mechanism of ATP hydrolysis, cycling through states which are associated with ion transport or ion counter-transport. The Na+/K+-ATPase, a member of this family, is almost exclusively found in animals, although close homologues have been reported in certain archaea, algae and oomycetes.The Na+/K+-ATPase is comprised of a nucleotide-binding (N) and phosphorylation (P) domain, a transmembrane core (M1-M6) and a large carboxy-terminal M7-M10 segment. Na+/K+-ATPase undergoes large conformational changes as part of its functional cycle giving rise to two distinct enzymatic states: E1, which is a high-affinity state for the primary transported ion- Na+ and E2, which is the low-affinity state for the Na+ ion. The two states arise from the autocatalysed formation and breakdown of a phosphoenzyme intermediate, coupled to the binding, occlusion, translocation and release of ions. The phosphorylation site is the Asp residue of a conserved DKTGT motif. The core of the membrane transport domain encompasses transmembrane helices M1-M6, which hold the main ion-binding sites and are necessary for cytoplasmic and extracellular ion transport. A terminal R domain extension, which serves as a regulatory unit, can be found in the C-terminal of the protein. This unit is auto-inhibitory and is predicted to restrict transmembrane helix movements and/or access of ions to the membrane transport core1. Na+/K+-ATPase has been implicated in the pathogenesis of Alzheimer's Disease. A deficiency in several Na+/K+-ATPase isoform genes induce learning and memory deficits, and the α isoform is altered in Alzheimer's Disease2.