Phosphoglycerate Dehydrogenase (PHGDH) Activity Assay Kit (Colorimetric) (ab273328) provides a quick and easy method for monitoring PHGDH activity in a variety of samples.
Individual kit components also available for purchase with a minimum order of 20 units. Contact us to discuss your needs.
Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate and the reversible oxidation of (S)-malate to oxaloacetate.
PGDH3, PHGDH, D-3-phosphoglycerate dehydrogenase, 3-PGDH, 2-oxoglutarate reductase, Malate dehydrogenase
Phosphoglycerate Dehydrogenase (PHGDH) Activity Assay Kit (Colorimetric) (ab273328) provides a quick and easy method for monitoring PHGDH activity in a variety of samples.
Individual kit components also available for purchase with a minimum order of 20 units. Contact us to discuss your needs.
Phosphoglycerate Dehydrogenase (PHGDH) Activity Assay Kit (Colorimetric) (ab273328) provides a quick and easy method for monitoring PHGDH activity in a variety of samples. In this kit, Phosphoglycerate Dehydrogenase converts 3-phosphoglycerate and NAD into 3-phosphohydroxyglerate and NADH respectively. The oxidation of NADH reduces a probe generating a strong, stable absorbance signal (OD: 450 nm).
The assay is simple, sensitive, high-throughput adaptable and can detect Phosphoglycerate Dehydrogenase activity less than 0.1 mU per sample.
Other Notes
This product was previously called K569 Biovision Phosphoglycerate Dehydrogenase (PHGDH) Activity Assay Kit (Colorimetric). Biovision was acquired by Abcam in 2021.
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Phosphoglycerate dehydrogenase also known as PHGDH is an enzyme that catalyzes the conversion of 3-phosphoglycerate to 3-phosphohydroxypyruvate. It has an approximate mass of 57 kDa. The PHGDH is located in the cytoplasm and mitochondria where it plays a role in serine biosynthesis. Malate dehydrogenase might also get mentioned together with PHGDH because both enzymes link to metabolic processes. The expression of PHGDH is noted in various tissues with higher levels observed in some cancer cells.
PHGDH is essential for the serine synthesis pathway and cellular metabolism regulation. It does not form part of large complexes but operates independently to convert substrates necessary for cell growth and proliferation. The enzyme supports the synthesis of nucleotides and proteins impacting cell cycle and survival. Researchers investigate PHGDH to understand its role in metabolic reprogramming especially in cancer cells.
PHGDH is important in the serine biosynthesis pathway which is part of the larger glycolytic process. It connects to pathways that contribute to cellular carbon metabolism and energy production. PHGDH interacts with glutamate dehydrogenase protein (GDH) and also influences one-carbon metabolism and redox balance within the cell. These pathways play important roles in providing building blocks for nucleotide and lipid biosynthesis.
PHGDH has relevance in cancer and neurological disorders. Alterations and overexpression of PHGDH have been linked to oncogenesis and tumor growth particularly in breast cancer. The enzyme also associates with neurodegenerative diseases as proper serine levels are important for neuron function. In both conditions PHGDH becomes connected with glutamate dehydrogenase as alterations can impact amino acid metabolism and neurotransmitter balance. The study of PHGDH inhibitors is gaining attention for therapeutic potentials in these diseases.
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NADH Standard Curve.
Kinetic measurement of Phosphoglycerate Dehydrogenase activity from various samples.
Relative PHGDH Activity was calculated in lysates prepared from HEK cells (4.5μg) and HeLa cells (7.8μg).
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