Abcam, ab256932, Human GPX1 (Glutathione Peroxidase 1) knockout HEK-293T cell lysate

Size: 1Kit
GPX1 KO cell lysate available now. KO validated by. Free of charge wild type control included. Knockout achieved by using CRISPR/Cas9, Homozygous: 1 bp insertion in exon 1.
Key facts
Cell type:HEK-293T,
Species or organism:Human,
Tissue:Kidney,
Knockout validation:Sanger Sequencing,
Mutation description:Knockout achieved by using CRISPR/Cas9, Homozygous: 1 bp insertion in exon 1.

Product details:
Knockout cell lysate achieved by CRISPR/Cas9.
REACH authorisation
Abcam has not and does not intend to apply for the REACH Authorisation of customers' uses of products that contain European Authorisation list (Annex XIV) substances.
It is the responsibility of our customers to check the necessity of application of REACH Authorisation, and any other relevant authorisations, for their intended uses.
Lysate preparation:
Our lysates are made using RIPA buffer to which we add a protease inhibitor cocktail and phosphatase inhibitor cocktail (ratio: 300:100:10).
This means that the protein of interest is denatured.
If you require a native form of the protein please use the live cell version. Please refer to our lysis protocol for further details on how our lysates are prepared.
User storage instructions:
Lyophilizate may be stored at 4°C. After reconstitution, store at -20°C for short-term storage or -80°C for long-term storage.
This product is subject to limited use licenses from The Broad Institute, ERS Genomics Limited and Sigma-Aldrich Co. LLC, and is developed with patented technology. For full details of the licenses and patents please refer to our
limited use license
patent pages

Properties and Storage Information:
Gene name-GPX1, Gene editing type-Knockout, Gene editing method-CRISPR technology, Knockout validation-Sanger Sequencing, Zygosity-Homozygous, Shipped at conditions-Ambient - Can Ship with Ice, Appropriate short-term storage conditions--20°C, Appropriate long-term storage conditions--20°C

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Glutathione Peroxidase 1 (GPx1) also known as GSH peroxidase is a selenium-containing enzyme with a mass of approximately 22 kDa. It plays an important role in reducing hydrogen peroxide to water using glutathione as a substrate therefore protecting cells from oxidative damage. GPx1 is widely expressed in many tissues but is found in high concentrations in the liver and erythrocytes. Researchers use antibodies specific to GPx1 often obtained from specialized suppliers to study and quantify this enzyme in various biological samples.
Biological function summary
The enzyme guards cellular components by neutralizing free radicals. GPx1 is not part of a large complex but functions as a homotetramer. Its activity is essential for preserving the redox balance within the cell preventing cellular damage from reactive oxygen species (ROS). Enzyme-linked immunosorbent assays (ELISA) often measure GPx1 activity to assess oxidative stress levels in research and clinical settings.
Pathways
GPx1 is important in the glutathione metabolism and cellular antioxidant defense pathways. Within these pathways GPx1 works closely with proteins like glutathione reductase to maintain reduced glutathione levels. This interplay with other antioxidant proteins ensures cellular protection against oxidative damage. Studies focus on GPx1's role in these pathways as it underpins many critical cellular processes maintaining cell health.
Decreased GPx1 activity links to neurodegenerative diseases and cardiovascular disorders. In neurodegenerative diseases such as Alzheimer's the oxidative stress overwhelms the antioxidant defenses including GPx1. Similarly in cardiovascular disorders a diminished GPx1 activity correlates with increased oxidative stress contributing to disease progression. Researchers also investigate connections between GPx1 and other oxidative stress-related proteins like superoxide dismutase to fully understand GPx1's role in disease mechanisms.