Abcam, ab258158, Human PUS1 knockout HEK-293T cell lysate

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PUS1 KO cell lysate available now. KO validated by Western blot. Free of charge wild type control included. Knockout achieved by using CRISPR/Cas9, 41 bp deletion in exon2 and 47 bp deletion in exon2.
Key facts
Cell type:HEK-293T,
Species or organism:Human,
Tissue:Kidney,
Knockout validation:Sanger Sequencing,Western blot,
Mutation description:Knockout achieved by using CRISPR/Cas9, 41 bp deletion in exon2 and 47 bp deletion in exon2.

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 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-PUS1, Gene editing type-Knockout, Gene editing method-CRISPR technology, Knockout validation-Sanger Sequencing, Western blot, 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.
PUS1 also known as pseudouridine synthase 1 is an enzyme responsible for catalyzing the isomerization of uridine to pseudouridine in RNA molecules. This protein has a mass of approximately 50 kDa and expresses widely in both the cytoplasm and mitochondria of human cells. Pseudouridine is the most abundant RNA modification and plays an important role in RNA stability and structure. The presence of PUS1 can vary among cell types supporting its necessity in diverse cellular contexts.
Biological function summary
The modification of RNA by PUS1 improves the stability and folding of the RNA structure aiding its functionality. The enzyme is not part of a larger complex but acts independently to achieve its role in RNA modification. Pseudouridine created by PUS1 permits enhanced base stacking and hydrogen bonding which influences the translation process and the overall efficiency of protein synthesis. This modification is important for the proper functioning of tRNA and rRNA ensuring fidelity during protein translation.
Pathways
PUS1 plays an essential role in the RNA processing and modification pathways. Its activity integrates into pathways such as ribosome biogenesis and RNA quality control. Particularly it interacts with other RNA-binding proteins and enzymes like TRUB1 another pseudouridine synthase which also contributes to the maturation of structured RNAs. These pathways are vital for maintaining cellular homeostasis and responding to various physiological demands.
Mutations in PUS1 are linked to mitochondrial myopathy and sideroblastic anemia a rare condition characterized by muscle weakness and anemia. These disorders illustrate the critical impact of RNA modification defects on cellular energy production and red blood cell formation. In these conditions PUS1 may interact with defective proteins leading to impaired pseudouridylation disrupting normal cellular functions and contributing to disease pathology. Understanding the role of PUS1 might provide insights into potential therapeutic strategies for such disorders.