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
Número MDL:
Código UNSPSC:
12352203
Productos recomendados
origen biológico
mouse
conjugado
unconjugated
forma del anticuerpo
ascites fluid
tipo de anticuerpo
primary antibodies
clon
M8-P1-A3, monoclonal
mol peso
antigen ~110 kDa
reactividad de especies
sheep, canine, rat, pig
no debe reaccionar con
chicken, Xenopus
técnicas
immunohistochemistry (frozen sections): 1:100
western blot: 1:250
isotipo
IgG1
Nº de acceso UniProt
Condiciones de envío
dry ice
temp. de almacenamiento
−20°C
Información sobre el gen
rat ... Atp1a1(24211)
Descripción general
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.
Inmunógeno
lamb kidney α1 subunit of Na+/K+ ATPase.
Aplicación
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.
Forma física
Solution in phosphate buffered saline containing 0.05% sodium azide.
Cláusula de descargo de responsabilidad
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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Código de clase de almacenamiento
10 - Combustible liquids
Clase de riesgo para el agua (WGK)
WGK 1
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
Equipo de protección personal
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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