Description
Key facts
Cell type:HEK-293T,
Species or organism:Human,
Tissue:Kidney,
Form:LiquidSee storage information,
Knockout validation:Sanger Sequencing,
Mutation description:Knockout achieved by using CRISPR/Cas9, Homozygous: 1 bp insertion in exon 4
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-APEH, Gene editing type-Knockout, Gene editing method-CRISPR technology, Knockout validation-Sanger Sequencing, 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 target protein APH also known as Aminoglycoside Phosphotransferase or APH(2") serves a critical role in antibiotic resistance mechanisms by phosphorylating aminoglycoside antibiotics leading to inactivation. APH with a mass of approximately 31 kDa can be found in bacteria that are often resistant to several antibiotics. Although mainly located in prokaryotes certain modified forms also show expression in eukaryotic systems for research purposes.
Biological function summary
APH plays a significant role in cell survival by protecting bacteria from antibiotic stress a process necessary for maintaining membrane integrity under antibiotic pressure. This enzyme is not a part of a larger protein complex but exhibits highly specific interactions with aminoglycosides. It commonly associates with resistance mechanisms allowing bacteria to survive in otherwise lethal environments.
Pathways
APH significantly impacts aminoglycoside metabolic pathways and contributes to the overarching antibiotic resistance pathway. This phosphotransferase action is often coordinated alongside AAC (Aminoglycoside N-acetyltransferase) and ANT (Aminoglycoside O-nucleotidyltransferase) proteins. They collectively enable bacteria survival by modifying antibiotics preventing their effective binding to bacterial ribosomal targets.
APH presents a considerable threat due to its association with multidrug-resistant bacterial infections and urinary tract infections. The protein's role in resistance complicates treatment protocols and is integrated into bacterial adaptation strategies. Alongside proteins like AAC and ANT APH contributes to bacterial resilience making it a target of interest in studies focused on developing novel antibacterial treatments.
