Abcam, ab164258, Recombinant Human PUS1 protein

Size: 10µg
Recombinant Human PUS1 protein is a Human Full Length protein, in the 1 to 399 aa range, expressed in Wheat germ, suitable for ELISA, WB.
Key facts
Expression system:Wheat germ,
Tags:GST tag N-Terminus,
Applications:WB, ELISASee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:No,
Accession:Q9Y606,
Animal free:No,
Carrier free:No,
Species:Human,
Storage buffer:pH: 8Constituents: 0.79% Tris HCl, 0.31% Glutathione

Properties and Storage Information:
Shipped at conditions-Dry Ice, Appropriate short-term storage conditions--80°C, Appropriate long-term storage conditions--80°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

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.