biological source
mouse
conjugate
unconjugated
antibody form
ascites fluid
antibody product type
primary antibodies
clone
9A-5, monoclonal
mol wt
antigen ~110 kDa
species reactivity
rat, human, canine, avian
technique(s)
immunohistochemistry (frozen sections): 1:1,000, indirect ELISA: suitable
isotype
IgG1
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Quality Level
Gene Information
human ... ATP1A1(476)
rat ... Atp1a1(24211)
General description
Epitope mapping studies indicate the antibody binds within the intracellular region at or near Asp-369 of the α subunit. Staining is consistent with the plasma membrane localization of Na+/K+ ATPase.
Mouse Monoclonal Anti-Na+/K+ ATPase (α1 Subunit) antibody localizes the Na+/ K+ ATPase α1 subunit in human, canine, rat and avian tissues.
Na+/K+ transporting ATPase subunit α1 is an ion transport pump critical for maintaining the gradient of Na and K ions across the plasma membrane.
The gene coding Na+,K+-ATPase is mapped to human chromosome 1p13.1, which is a plasma membrane ion transporter. It is ubiquitously expressed in all animals. The α subunit of the protein consists of 10 transmembrane helices, and three cytoplasmic domains A, N and P that serve as actuator, in nucleotide-binding and for phosphorylation, respectively.
Immunogen
rat kidney Na+/K+ ATPase.
Application
Monoclonal Anti-Na+/K+ ATPase (α1 Subunit) antibody produced in mouse has been used in immunohistochemistry.
Mouse Monoclonal Anti-Na+/K+ ATPase (α1 Subunit) antibody has been used for immunohistochemical assays. It has also been used for immunolabeling assays to quantify the expression of proteins involved in cellular ion transport. Furthermore, the product is suitable for use in indirect ELISA.
Biochem/physiol Actions
Na+,K+-ATPase facilitates the transport of Na+ and K+ ions across plasma membrane in an ATP-dependent manner. Therefore, it is responsible for maintaining ion homeostasis across the cell and controls cellular excitability in electrically active tissues. The Na+ potential established by Na+,K+-ATPase is required for the function of secondary active transporters. Variation in the gene mostly results in protein function alteration, otherwise in some cases its stability, expression or plasma membrane targeting property is affected. Mutation in the gene is known to cause a number of disease conditions including Familial Hemiplegic Migraine type 2, Rapid-onset Dystonia Parkinsonism and Alternating Hemiplegia of Childhood. Na+,K+-ATPase serves as a receptor for cardiotonic steroids, that play a vital role in triggering proinflammatory cytokine production, in chronic inflammatory diseases, such as atherosclerosis.
Physical form
Solution in phosphate buffered saline containing 0.05% sodium azide.
Disclaimer
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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存储类别
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
法规信息
低风险生物材料
常规特殊物品
此项目有
Cardiotonic Steroids Stimulate Macrophage Inflammatory Responses Through a Pathway Involving CD36, TLR4, and Na/K-ATPase
Chen Y, et al.
Arteriosclerosis, Thrombosis, and Vascular Biology (2017)
Ion Pathways in the Na+/K+-ATPase
C?echova? P, et al.
Journal of Chemical Information and Modeling, 56(12), 2434-2444 (2016)
Genome-Wide Linkage Analysis of Systolic and Diastolic Blood Pressure
Rice T, et al.
Circulation, 102(16), 1956-1963 (2000)
Agrin Regulation of α3 Sodium-Potassium ATPase Activity Modulates Cardiac Myocyte Contraction.
Hilgenberg LG, et al.
The Journal of Biological Chemistry, 284(25), 16956-16965 (2009)
Disruption of Ankyrin B and Caveolin-1 Interaction Sites Alters Na+,K+-ATPase Membrane Diffusion.
Junghans C, et al.
Biophysical Journal, 113(10), 2249-2260 (2017)
相关内容
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