Description
Key facts
Cell type:HEK-293T,
Species or organism:Human,
Tissue:Kidney,
Form:LiquidSee storage information,
Knockout validation:Immunocytochemistry,Sanger Sequencing,Western blot,
Mutation description:Knockout achieved by using CRISPR/Cas9, Homozygous: 1 bp insertion in exon 5
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-APP, Gene editing type-Knockout, Gene editing method-CRISPR technology, Knockout validation-Immunocytochemistry, Sanger Sequencing, Western blot, 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.
The Amyloid Precursor Protein (APP) also known as amyloid protein is a transmembrane protein that is approximately 695 to 770 amino acids in length depending on the isoform. The molecular mass of APP can vary but typically falls around 100 to 140 kDa. It is heavily expressed in the central nervous system particularly in neurons but also in other tissues like muscle and kidney. The APP undergoes proteolytic processing which leads to the generation of various fragments including beta-amyloid peptides.
Biological function summary
The processing of APP plays a fundamental role in neuronal growth survival and repair. APP is cleaved into fragments that can regulate synaptic function and plasticity. It does not operate as a part of a complex but interacts with various cellular components. The protein participates in signaling pathways influencing cellular adhesion motility and neurite outgrowth. APP's numerous interaction partners facilitate its involvement in different cellular processes highlighting its critical role in normal cell function.
Pathways
The APP is a central component in the amyloidogenic pathway where its cleavage by beta-secretase and gamma-secretase yields beta-amyloid. This pathway is one of two primary metabolic routes for APP—alternative enzymatic processing through the non-amyloidogenic pathway precludes beta-amyloid formation releasing peptides that do not aggregate. Enzymes like BACE1 (beta-secretase 1) and presenilin are important in the amyloidogenic pathway directly resulting in the production of the neurotoxic amyloid beta-peptide.
APP is intensely linked to Alzheimer's disease and cerebral amyloid angiopathy. Accumulation of beta-amyloid peptides formed from APP cleavage is a hallmark of Alzheimer's disease leading to plaque formation in the brain. This aggregation impacts neuronal function and is associated with neurodegenerative processes. Interactions with proteins like tau are significant as tau also plays an essential role in Alzheimer's disease pathology. Misprocessing of APP and the resulting beta-amyloid aggregates are also contributors to cerebral amyloid angiopathy where deposits within cerebrovascular walls compromise vascular integrity.
