Recombinant Rat Sodium/potassium-transporting ATPase subunit alpha-2 (Atp1a2), partial

Code CSB-YP002323RA
MSDS
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Source Yeast
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Code CSB-EP002323RA
MSDS
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Source E.coli
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Code CSB-EP002323RA-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP002323RA
MSDS
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Source Baculovirus
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Code CSB-MP002323RA
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Atp1a2
Uniprot No.
Alternative Names
Atp1a2Sodium/potassium-transporting ATPase subunit alpha-2; Na(+)/K(+) ATPase alpha-2 subunit; EC 7.2.2.13; Na(+)/K(+) ATPase alpha(+) subunit; Sodium pump subunit alpha-2
Species
Rattus norvegicus (Rat)
Protein Length
Partial
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

Function
This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients.
Gene References into Functions
  1. cardiomyocyte ATP1A2 is a target of A/R injury PMID: 29394489
  2. Hypoxia reduces smooth muscle cell expression of Atp1a2 which may contribute to basilar artery vasoconstriction. PMID: 26924456
  3. Data suggest that, in polycystic ovary syndrome, heart exhibits alteration in processing of Atp1a2 (Na+/K+ transporting ATPase alpha 2) with decreases in plasma membrane content of this enzyme subunit. PMID: 25988879
  4. Na-K-ATPase alpha2 does not regulate Src. PMID: 26108663
  5. Na,K-ATPase alterations precede hindlimb suspension-induced muscle atrophy. PMID: 25654120
  6. Relationship between intracellular Na+ concentration and reduced Na+ affinity in Na+,K+-ATPase mutants causing neurological disease PMID: 24356962
  7. Results suggest that the increase in the Na(+)/water ratio and a reduction in ATP1alpha2 may be associated with cerebral aneurysm formation. PMID: 23045463
  8. The nicotinic acetylcholine receptor and the Na,K-ATPase alpha2 isoform interact to regulate membrane electrogenesis in skeletal muscle. PMID: 20595385
  9. The Na+K+ ATPase alpha 2 subunit is localized in astrocytic processes around axonal or dendritic elements of glutamatergic axo-dendritic synaptic junctions in the frontoparietal somatosensory cortex. PMID: 11950769
  10. Structural basis for alpha1 versus alpha2 isoform-distinct behavior of the Na,K-ATPase PMID: 12529322
  11. beta(1)-Na(+),K(+)-ATPase is likely to represent the most physiologic and efficient subunit for HKalpha(2) assembly in distal colon. PMID: 15327400
  12. missense mutants R689Q and M731T have reduced catalytic turnover and increased apparent affinity for extracellular K(+) PMID: 16037212
  13. cyclic stretch mainly stimulated translocation of alpha2-subunit of Na+-K+-ATPase from endosomes to the plasma membrane via a PI 3-kinase-dependent mechanism in cultured skeletal muscle cells in vitro, which in turn increased the activity of the Na pump. PMID: 16893515
  14. The functional density of NKA-alpha2 is approximately 4.5 times higher in the T-tubules vs. external sarcolemma in ventricular cardiomyocytes. PMID: 17392375
  15. Downregulation of Atp1a2 attenuated control of Na/Ca exchanger activity in heart failure, reducing its capability to extrude Ca2+ from cardiomyocytes. PMID: 18203708
  16. Protein and mRNA levels for Na(+)-K(+)-ATPase alpha2 isoform were decreased in failing hearts. This was prevented by analapril or losartan. PMID: 18418421
  17. Analysis of exercise-induced Na+-K+ exchange in rat skeletal muscle in vivo. PMID: 18586859
  18. Disturbances in skeletal muscle Na(+)-K(+)-ATPase regulation, particularly the alpha(2)-subunit, may contribute to impaired ion homeostasis in insulin-resistant states such as obesity and type 2 diabetes. PMID: 19366873

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Subcellular Location
Membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
Protein Families
Cation transport ATPase (P-type) (TC 3.A.3) family, Type IIC subfamily
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