Technical Data
032271
ATP1B2, ID (ATP1B2, Sodium/potassium-transporting ATPase subunit beta-2, Sodium/potassium-dependent ATPase subunit beta-2)
Description:
The protein belongs to the family of Na+/K+ and H+/K+ ATPases beta chain proteins, and to the subfamily of Na+/K+ -ATPases. Na+/K+ -ATPase is an integral membrane protein responsible for establishing and maintaining the electrochemical gradients of Na and K ions across the plasma membrane. These gradients are essential for osmoregulation, for sodium-coupled transport of a variety of organic and inorganic molecules, and for electrical excitability of nerve and muscle. This enzyme is composed of two subunits, a large catalytic subunit (alpha) and a smaller glycoprotein subunit (beta). The beta subunit regulates, through assembly of alpha/beta heterodimers, the number of sodium pumps transported to the plasma membrane.

Applications:
Suitable for use in Western Blot, Immunohistochemistry, Flow Cytometry, ELISA

Recommended Dilution:
ELISA: 1:1,000
Western Blot: 1:100-500
Immunohistochemistry: 1:50-100
Flow Cytometry: 1:10-50

Storage and Stability:
May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20C. Aliquots are stable for 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
TypeIsotypeCloneGrade
PabIgGAffinity Purified
SizeStorageShippingSourceHost
200ul-20CBlue IceHumanRabbit
Concentration:
As reported
Immunogen:
ATP1B2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 121~150 amino acids from the Center region of human ATP1B2.
Purity:
Purified by Protein A affinity chromatography.
Form
Supplied as a liquid in PBS, pH 7.2, 0.09% sodium azide.
Specificity:
Human
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
Guey,L.T., et.al., Eur. Urol. 57 (2), 283-292 (2010)
Tokhtaeva,E., et.al., Biochemistry 48 (48), 11421-11431 (2009)
Hosgood,H.D. et.al., Respir Med 103 (12), 1866-1870 (2009)