Description
Key facts
Detection method:Colorimetric/Fluorometric,
Sample types:Tissue Extracts, Tissue Lysate,
Assay type:Enzyme activity,
Sensitivity:>= 30 µU,
Assay Platform:Microplate reader
Product details:
This product is manufactured by BioVision, an Abcam company and was previously sold under product code K2104.
Glycogen phosphorylase (EC 2.4.1.1) catalyzes the rate-limiting step in the glycogenolysis pathway, cleaving the α1-4 glycoside bonds on linear glycogen chains to release glucose and utilizing inorganic phosphate to produce glucose-1-phosphate (G1P). In mammals, glycogen phosphorylase is abundant in muscle, liver and brain tissues. There are two forms of glycogen phosphorylase, namely glycogen phosphorylase a and b isoforms. Glycogen phosphorylase a is the highly active form found in muscle tissue, whereas glycogen phosphorylase b isoform has only limited activity. Glycogen phosphorylase is a clinically significant enzyme, as various mutations are associated with different congenital glycogen storage diseases affecting both muscle and liver. In addition, this enzyme has been suggested as a biomarker for gastric cancer and has been investigated as a drug target for treatment of type 2 diabetes. The Glycogen Phosphorylase Activity Assay Kit is based on the detection of glucose-1-phosphate by a set of enzymatic reactions, ultimately reducing a fluorogenic probe to form a stable fluorophore measured at Ex/Em = 538/587 nm. The intensity of the fluorescence is directly proportional to the glycogen phosphorylase activity in samples. This kit is a rapid, sensitive and a convenient tool for detecting glycogen phosphorylase activity in samples. The kit can detect as low as 30 μU of enzyme activity in a variety of sample types.
Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage duration-Up to 12 months, Appropriate short-term storage conditions--20°C, Appropriate long-term storage conditions--20°C, Storage information-Please refer to protocols
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Glycogen Phosphorylase also known as 'Phosphorylase' is an enzyme that catalyzes the breakdown of glycogen into glucose-1-phosphate. This enzyme exists in different isoforms including muscle liver and brain glycogen phosphorylases. The molecular mass of glycogen phosphorylase is approximately 97 kDa. It typically expresses in tissues that store glycogen such as liver and muscle enabling these tissues to convert stored glycogen into glucose during times of energy demand.
Biological function summary
This protein plays a role in glycogen metabolism by releasing glucose units through the glycogen phosphorylase reaction. It is not part of a complex but functions independently. Glycogen phosphorylase activity increases during fasting or physical exertion providing an accessible source of glucose. This regulation is important for maintaining blood glucose levels especially in liver tissue where glycogen phosphorylase function is essential for homeostasis.
Pathways
Glycogen phosphorylase is integral to glycogenolysis a part of carbohydrate metabolism. It works alongside other enzymes such as glycogen synthase in balancing the breakdown and synthesis of glycogen. In hormonal control pathways glycogen phosphorylase activity is modulated by epinephrine and glucagon which promote its conversion to the active form. Through these pathways phosphorylases exhibit dynamic responses to varying energy needs.
Glycogen phosphorylase is linked to McArdle's disease a glycogen storage disorder resulting from muscle phosphorylase deficiency. This condition causes muscle pain and weakness upon exertion. Another related disorder is Hers disease caused by liver glycogen phosphorylase deficiency resulting in hypoglycemia and hepatomegaly. Both conditions highlight the importance of the glycogen phosphorylase function for normal muscle and liver physiology.
