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, 20 bp deletion in exon 2 and 7 bp deletion in exon 2,
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 and ERS Genomics Limited, and is developed with patented technology. For full details of the limited use licenses and relevant patents please refer to our
limited use license
patent pages
Properties and Storage Information:
Gene name-DPH2, Gene editing type-Knockout, Gene editing method-CRISPR technology, Knockout validation-Sanger Sequencing, 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.
DPH2 also known as diphthamide biosynthesis protein 2 functions mechanically in catalyzing the first step of diphthamide biosynthesis. The protein incorporates a unique post-translational modification into histidine residues on elongation factor 2 (EEF2). DPH2 weighs approximately 53 kDa and is expressed in various tissues with high levels seen in the liver and testis. Its structural genes reside on human chromosome 17.
Biological function summary
Diphthamide biosynthesis is important to protein synthesis and cellular resilience against bacterial toxins like diphtheria toxin. DPH2 operates within a multiprotein complex including DPH1 and DPH3 necessary for EEF2 modification. Proper function of DPH2 ensures that EEF2 maintains its role in translational fidelity which is indispensable for normal cellular processes.
Pathways
Diphthamide biosynthesis connects to the protein synthesis and modification pathway. DPH2's activities integrate seamlessly with the translational machinery specifically influencing EEF2's function in the ribosome. In addition DPH2 works with DPH1 DPH3 and other proteins in the biosynthesis pathway to fulfill its role efficiently supporting cellular defense mechanisms against translational errors induced by toxins.
Defects in DPH2 relate to cancer and neurological conditions. Loss of function mutations in DPH2 can affect cellular processes potentially contributing to tumorigenesis where DPH1 is another connected protein of interest. Genetic alterations in DPH2 can also interfere with neural cell proliferation and survival linking to certain neurodegenerative disorders and emphasizing its role in maintaining cell health.
