Abcam, ab138878, Aspartate Aminotransferase Activity Assay Kit (Fluorometric)

Size: 1Kit
Aspartate Aminotransferase Activity Assay Kit / AST Assay Kit (Fluorometric) ab138878 provides a quick and sensitive assay for AST activity in biological samples.
Key facts
Detection method:Fluorescent,
Sample types:Serum, Other biological fluids,
Assay type:Enzyme activity,
Sensitivity:= 2 mU/mL,
Assay Platform:Microplate reader

Product details:
Aspartate Aminotransferase Activity Assay Kit / AST Assay Kit (Fluorometric) ab138878 provides a quick and sensitive assay for AST activity in biological samples.
In the AST assay protocol, AST catalyzes the reaction of aspartate and α-ketoglutarate to oxaloacetate and glutamate:
Aspartate (Asp) + α-ketoglutarate ⇌ oxaloacetate + glutamate (Glu)
The product L-glutamate is measured by the generation of a red fluorescent product through an enzyme coupled reaction cycle.
The assay signal can be read by a fluorescence microplate reader at Ex/Em = 530-570 nm/590-600 nm (optimal Ex/Em = 540 nm/590 nm). The AST activity assay can detect as little as 2 mU/mL AST in a 100 μL reaction volume. The assay is robust, and can be readily adapted for a wide variety of applications.
Aspartate aminotransferase (AST), also called Glutamic Oxaloacetic transaminase (GOT), is a member of transferase family. It catalyzes the reversible transfer of an α-amino group between aspartate and glutamate, and is an important enzyme in amino acid metabolism.

Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage conditions--20°C, Appropriate long-term storage conditions--20°C, Storage information--20°C

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Aspartate Aminotransferase (AST) also known as aspartate transaminase or aspartate transferase is an enzyme important for amino acid metabolism. Mechanically it catalyzes the reversible transfer of an amino group from aspartate to α-ketoglutarate forming oxaloacetate and glutamate. AST has a molecular mass of approximately 92 kDa and is expressed in various tissues with high levels found in liver heart muscle and kidneys. Its presence in these tissues highlights its importance in cellular metabolic processes.
Biological function summary
AST facilitates the interconversion between aspartate and oxaloacetate playing a role in the amino acid and urea cycles. Though not part of a large complex AST works closely with similar enzymes such as alanine aminotransferase (ALT) to maintain amino acid balance and support energy production. This enzymatic activity is important in nitrogen metabolism and glutamate use which are necessary for synthesizing other essential molecules within the cell.
Pathways
AST participates in the citric acid cycle and malate-aspartate shuttle enabling efficient energy production and NADH transport. The enzyme assists in converting oxaloacetate a pivotal intermediate in the citric acid cycle to keep the cycle active ensuring efficient cellular respiration. Additionally in the malate-aspartate shuttle AST works alongside malate dehydrogenase to facilitate the transfer of reducing equivalents across the mitochondrial membrane which is essential for ATP generation.
Elevated AST levels often indicate liver damage such as in hepatitis or cirrhosis reflecting its significant tissue expression. The enzyme is also linked to myocardial infarction as damaged heart muscle releases AST into the bloodstream. In these conditions AST serves as a biomarker for tissue damage often in conjunction with ALT levels allowing clinicians to assess the extent of liver or cardiac injury.