Description
Key facts
Cell type:HeLa,
Species or organism:Human,
Tissue:Cervix,
Form:LiquidSee storage information,
Knockout validation:Sanger Sequencing,
Mutation description:Knockout achieved by using CRISPR/Cas9, Homozygous: Insertion of the selection cassette in exon 4,
Disease:Adenocarcinoma
Product details:
We will provide viable cells that proliferate on revival.
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-GTPBP2, Gene editing type-Knockout, Gene editing method-CRISPR technology, Knockout validation-Sanger Sequencing, Zygosity-Homozygous, Shipped at conditions-Dry Ice, Appropriate short-term storage conditions--196°C, Appropriate long-term storage conditions--196°C
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
GTPBP2 also known as GTP-binding protein 2 is a protein that functions as a GTPase. It hydrolyzes GTP to GDP which is important for signaling and cellular processes. GTPBP2 has a molecular mass of approximately 75 kDa. It is widely expressed in various tissues including the brain thyroid and lung. Its expression suggests a significant role in cellular regulation across diverse cell types.
Biological function summary
This GTPase is involved in ribosome function and plays a role in translation regulation. Though not part of a large protein complex GTPBP2 interacts with certain ribosomal components which indicates its involvement in protein synthesis. It can influence mRNA translation efficiency through these interactions impacting cellular growth and function.
Pathways
GTPBP2 participates in the mRNA surveillance pathway and the regulation of translation. It ensures the fidelity of mRNA translation and prevents errors during protein synthesis. In these pathways GTPBP2 works in conjunction with other proteins like eEF2 and eRF1 which are essential for elongation and termination phases of protein translation respectively.
GTPBP2 is linked to neurodegenerative diseases and certain types of cancer. Mutations or dysregulation in GTPBP2 can contribute to neurodegenerative conditions possibly due to impaired translation regulation in neurons. Additionally abnormalities in its function have been associated with increased cancer risk. GTPBP2 connections with proteins such as p53 and Rb highlight its influence on cell cycle regulation and apoptosis further affecting disease progression.
