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H(+) /K(+) ATPase beta subunit knockout mice had decreased bone mineral content and bone mineral density, reduced cortical thickness and inferior mechanical bone strength.
The endogenous H+/K+ ATPase beta autoantigen in normal mice plays a critical role in the the tolerance of pathogenic H/Kbeta-specific T cells.
These results may imply that the H(+),K(+)-ATPase (show ATP1A1 Proteins) in the cochlear lateral wall is crucial for K(+) circulation and thus plays a critical role in generation of endocochlear potential.
Prevention of autoimmune gastritis requires the extra-thymic purging of highly autoaggressive H(+)/K(+) ATPase-specific T cells to produce a T-cell repertoire that is more susceptible to the suppressive activity of regulatory T cells.
these findings demonstrated that a decrease in pHi, caused by H+/K+-ATPase inhibition induced by BMT-1, triggered the dysfunction of the mitochondria resulting in the apoptosis of MM cells
Downregulation of ATP4B gene is associated with gastric cancer.
BCL-2 (show BCL2 Proteins) inhibits formation of reactive oxygen species.
Thus prolonged exhaustive exercise impaired each of the maximal in vitro Na+-K+-ATPase (show ATP1A1 Proteins) activity, Ca2 (show CA2 Proteins)+ release, and Ca2 (show CA2 Proteins)+ uptake rates.
Use of fold recognition methods enables the prediction that a C-terminal domain of the beta subunits of Na,K-ATPase (show ATP1A1 Proteins) and H,K-ATPase (show ATP1A1 Proteins) has an immunoglobulin-like fold, which resembles cell adhesion molecules.
New cryo-electron microscopic structures of H+,K+-ATPase (show ATP1A1 Proteins) using a phosphate analog and a specific antagonist, SCH28080.
for the Na(+)/K(+)-ATPase (show ATP1A1 Proteins), Mg(2 (show MCOLN1 Proteins)+)-vanadate is unable to recruit all the Rb(+)-bound to the Rb(+)-occluded form of the Rb(+)-vanadate-H(+)/K(+)-ATPase complex
Results provide strong evidence that the catalytic unit of octaethylene glycol dodecyl ether-solubilized gastric H/K-ATPase is (show ATP11A Proteins) a tetraprotomer.
Data describe the functional characteristics of the oligomeric form of the membrane-bound gastric H,K-ATPase (show ATP1A1 Proteins).
The number of parietal cells explained part of the differences in the expression of the H(+)/K(+)-ATPase gene.
structural rearrangements in the H+,K+-ATPase are much smaller than those observed in the related SERCA ATPase
The protein encoded by this gene belongs to a family of P-type cation-transporting ATPases. The gastric H+, K+-ATPase is a heterodimer consisting of a high molecular weight catalytic alpha subunit and a smaller but heavily glycosylated beta subunit. This enzyme is a proton pump that catalyzes the hydrolysis of ATP coupled with the exchange of H(+) and K(+) ions across the plasma membrane. It is also responsible for gastric acid secretion. This gene encodes the beta subunit of the gastric H+, K+-ATPase.
ATPase, H+/K+ transporting, beta polypeptide, gastric specific
, H+/K+-ATPase beta
, gastric H(+)/K(+) ATPase subunit beta
, potassium-transporting ATPase subunit beta
, proton pump beta chain
, ATPase H+K+-transporting beta / (gastric HK-ATPase beta subunit) defined by SSR
, ATPase, H+,K+-transporting, beta / (gastric H,K-ATPase beta subunit), defined by SSR
, ATPase, H+/K+ transporting, beta polypeptide
, H+ K+ ATPase beta subunit
, gastric H+/K+ ATPase beta subunit
, gastric hydrogen-potassium ATPase, beta
, potassium-transporting ATPase beta chain
, H.K-ATPase, beta subunit
, gastric H+/K+-ATPase beta subunit