Description
Key facts
Cell type:A549,
Species or organism:Human,
Tissue:Lung,
Form:LiquidSee storage information,
Knockout validation:Next Generation Sequencing,Western blot,
Disease:Carcinoma
Product details:
Although we aim to provide customers with a homozygous clone, feasibility will be dependent on the biology of the protein. Should only heterozygous edits be achieved, you will be notified of the outcome and be asked to confirm whether the cell line is acceptable. All clones will be accompanied with DNA sequencing data, and the mutation description.
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-EIF2AK3, Gene editing type-Knockout, Gene editing method-CRISPR technology, Knockout validation-Next Generation Sequencing, Western blot, 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.
PERK also known as EIF2AK3 is a protein kinase involved in the unfolded protein response (UPR). Researchers commonly identify it by its phosphorylation state in western blots recognizable as phospho-PERK or p-PERK. The molecular weight of PERK is approximately 125 kDa. It is predominantly expressed in the endoplasmic reticulum (ER) of cells acting as a sensor for misfolded proteins. PERK acts mechanistically by phosphorylating the translation initiation factor eIF2α reducing overall protein synthesis and alleviating ER stress.
Biological function summary
PERK plays an important role in maintaining cellular homeostasis during stress conditions. It forms part of a larger complex that regulates the adaptive response to ER stress. Upon activation PERK arrests general protein translation while allowing for selective translation of stress response proteins. This mechanism prevents the accumulation of unfolded proteins and assists in the survival of cells under adverse conditions. PERK also contributes to the regulation of oxidative stress and cell apoptosis adding further layers to its biological significance.
Pathways
PERK's activity intersects with the integrated stress response and UPR pathways. It shares a close functional relationship with proteins like ATF4 which is synthesized upon PERK activation and is important for the transcription of genes related to stress adaptation. The UPR pathway coordinates with the IRE1 and ATF6 pathways forming an important network for managing ER stress. These pathways collectively ensure cellular resilience adjusting metabolic demands and promoting cellular recovery.
PERK's malfunction can contribute to conditions such as diabetes and neurodegenerative diseases like Alzheimer's. In diabetes improper regulation of PERK affects insulin synthesis and secretion leading to pancreatic β-cell dysfunction. Alzheimer’s disease shows links with heightened ER stress and dysregulation of the PERK-eIF2α signaling pathway potentially contributing to neuronal death. PERK dysfunction can also associate with other proteins such as CHOP which mediates apoptosis during prolonged ER stress exacerbating these conditions.
