A277
Monoclonal Anti-Na+/K+ ATPase (α1 Subunit) antibody produced in mouse
clone M8-P1-A3, ascites fluid
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About This Item
Numéro MDL:
Code UNSPSC :
12352203
Produits recommandés
Source biologique
mouse
Conjugué
unconjugated
Forme d'anticorps
ascites fluid
Type de produit anticorps
primary antibodies
Clone
M8-P1-A3, monoclonal
Poids mol.
antigen ~110 kDa
Espèces réactives
sheep, canine, rat, pig
Ne doit pas réagir avec
chicken, Xenopus
Technique(s)
immunohistochemistry (frozen sections): 1:100
western blot: 1:250
Isotype
IgG1
Numéro d'accès UniProt
Conditions d'expédition
dry ice
Température de stockage
−20°C
Informations sur le gène
rat ... Atp1a1(24211)
Description générale
Epitope mapping studies indicates the epitope is between amino acids 496 and 506 of lamb kidney Na+/K+ ATPase. No reactivity is observed in chicken or Xenopus. Staining is consistent with the plasma membrane localization of Na+/K+ ATPase.
Mouse monoclonal anti-Na+/K+ ATPase (α1 subunit) reacts with the α1 subunit of Na+/K+-ATPase in sheep, canine, rat and pig. In rat, the antibody shows no reactivity with the α2 or α3 subunits.
Na+/K+ transporting ATPase subunit α 1 is an ion transport pump critical for maintaining the gradient of Na and K ions across the plasma membrane.
Immunogène
lamb kidney α1 subunit of Na+/K+ ATPase.
Application
Mouse monoclonal anti-Na+/K+ ATPase (α1 subunit) has been used for western blot and co-immunoprecipitation assays. The product can also be used for immunohistochemistry applications using frozen sections at a dilution of 1:100.
Forme physique
Solution in phosphate buffered saline containing 0.05% sodium azide.
Clause de non-responsabilité
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Code de la classe de stockage
10 - Combustible liquids
Classe de danger pour l'eau (WGK)
WGK 1
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
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Valdilene S Ribeiro et al.
Biochimica et biophysica acta, 1864(7), 2458-2471 (2018-04-15)
α-Tocopherol (α-Toc) overload increases the risk of dying in humans (E.R. Miller III et al. Meta-analysis: high-dosage vitamin E supplementation may increase all-cause mortality Ann Int Med. 142 (2005) 37-46), and overload during early development leads to elevation of blood
Mun Aw et al.
American journal of physiology. Regulatory, integrative and comparative physiology, 314(4), R563-R573 (2018-01-20)
In general, the mammalian whole body mass-specific metabolic rate correlates positively with maximal urine concentration (Umax) irrespective of whether or not the species have adapted to arid or mesic habitat. Accordingly, we hypothesized that the thick ascending limb (TAL) of
W J Ball et al.
Biochimica et biophysica acta, 719(3), 413-423 (1982-12-17)
Four stable hybridoma cell lines secreting antibodies specific to the membrane (Na+ + K+)-dependent ATPase isolated from lamb kidney medulla have been produced by fusing mouse myeloma cells with spleen cells from immunized mice. These cell lines produce IgG gamma
Zinaeli López-González et al.
Journal of molecular histology, 51(6), 701-716 (2020-10-19)
The kidney controls body fluids, electrolyte and acid-base balance. Previously, we demonstrated that hyperpolarization-activated and cyclic nucleotide-gated (HCN) cation channels participate in ammonium excretion in the rat kidney. Since acid-base balance is closely linked to potassium metabolism, in the present
Helen X Pu et al.
The Journal of biological chemistry, 277(23), 20270-20276 (2002-04-04)
The two variants of the gamma subunit of the rat renal sodium pump, gamma(a) and gamma(b), have similar effects on the Na,K-ATPase. Both increase the affinity for ATP due to a shift in the enzyme's E(1) <--> E(2) conformational equilibrium
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