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: 29 bp deletion in exon 1
Product details:
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-GRHPR, 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.
GRHPR also called glyoxylate reductase/hydroxypyruvate reductase is an enzyme with mass about 35 kDa. It catalyzes the conversion of glyoxylate to glycolate and hydroxypyruvate to D-glycerate. This protein exists in the cytoplasm and is found in tissues like liver kidney and pancreas. Its enzymatic activity plays a role in regulating the balance between glyoxylate and glycolate within cells.
Biological function summary
GRHPR acts as a detoxifying agent by reducing glyoxylate levels protecting cells from glyoxylate-mediated toxicity. This enzyme is not part of a larger complex and functions independently. Well-balanced glyoxylate and glycolate levels are critical for cellular homeostasis and GRHPR ensures proper maintenance and regulation within metabolic pathways.
Pathways
GRHPR participates in glyoxylate and dicarboxylate metabolism helping control the flow of metabolites. This involvement is significant in the context of the glyoxylate cycle and serine metabolism. Additionally it interacts with proteins such as lactate dehydrogenase during its activity within these metabolic pathways demonstrating its interconnectedness within cellular processes.
GRHPR mutations are associated with primary hyperoxaluria type 2 a disorder characterized by excessive oxalate production leading to kidney stones. In this context GRHPR dysfunction can lead to increased glyoxylate levels causing elevated oxalate synthesis. The enzyme's connection to this disease is critical as it is one of the few proteins whose dysfunction directly results in the metabolic imbalance observed in primary hyperoxaluria type 2.
