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Study provides evidence that the conserved N-terminal transmembrane domain of GPX8, in addition to its enzymatic activity, is essential for regulating Ca(2+) dynamics revealing a novel level of integration between redox-related proteins and Ca(2+) signaling/homeostasis.
GPX8 is transcriptionally regulated by HIFalpha and modulates growth factor signaling in HeLa cells.
Along with the induction of GPX8 in ER-stressed cells, these findings question a ubiquitous role of Ero1alpha as a producer of cytoplasmic ROS under ER stress
Quantitative proteomics identifies the membrane-associated peroxidase GPx8 as a cellular substrate of the hepatitis C virus NS3-4A protease.
GPx8 labeled as secreted glutathione peroxidase, is actually endoplasmic reticulum-resident protein disulfide isomerase peroxidase
the deficiency of AtGPX8 accelerates the progression of oxidative stress in knockout out plants.
These results suggest that AtGPX8 plays an important role in the protection of cellular components including nuclear DNA against oxidative stress.
May constitute a glutathione peroxidase-like protective system against oxidative stresses (By similarity).
probable glutathione peroxidase 8