Phenylalanine Ammonia-Lyase Activity Assay Kit (Fluorometric) (ab284571) (K2055) measures the activity of PAL via a two-step plate-based assay.
Purified protein, Serum
Mammals
>= 3 µU
Phenylalanine Ammonia-Lyase Activity Assay Kit (Fluorometric) (ab284571) (K2055) measures the activity of PAL via a two-step plate-based assay.
Purified protein, Serum
Mammals
>= 3 µU
Blue Ice
-20°C
-20°C
-20°C
Phenylalanine Ammonia-Lyase Activity Assay Kit (Fluorometric) (ab284571) (K2055) measures the activity of PAL via a two-step plate-based assay. The products of the PAL enzymatic reaction, generated in the first step, react with the developers resulting in the formation of a fluorescent compound, which is detected at Ex/Em = 410/470 nm. The kit can detect as low as 3 μU (3 pmol substrate catalysis/minute) of PAL under assay conditions.
This product is manufactured by BioVision, an Abcam company and was previously called K2055 Phenylalanine Ammonia-Lyase Activity Assay Kit (Fluorometric). K2055-100 is the same size as the 100 test size of ab284571.
This supplementary information is collated from multiple sources and compiled automatically.
Phenylalanine ammonia-lyase also known as PAL or phenylalanine lyase is an enzyme involved in catalyzing the non-oxidative deamination of L-phenylalanine to trans-cinnamic acid and ammonia. It has a molecular mass of approximately 76 kDa. This enzyme is primarily expressed in plants certain fungi and some bacteria. In plants it plays a significant role in the phenylpropanoid pathway influencing various aspects of growth and defense mechanisms.
Phenylalanine ammonia-lyase takes part in the synthesis of compounds that provide plants structural and defensive functions. These include lignin flavonoids and other phenolic derivatives that contribute to plant rigidity and protection against pathogens. PAL is often involved as a standalone enzyme but its activity influences the operation of a complex web of metabolic processes involved in plant defense and adaptation.
Phenylalanine ammonia-lyase acts within the phenylpropanoid pathway. This pathway converts phenylalanine into numerous secondary metabolites important for the plant's development and stress response. PAL works alongside other enzymes like cinnamate 4-hydroxylase to convert products into lignin a critical component of the plant cell wall. These interactions underline an important role for PAL in facilitating complex plant pathways that maintain structural integrity and stress management.
Phenylalanine ammonia-lyase relates to phenylketonuria (PKU) an inherited metabolic disorder although its role in this disorder is largely indirect. In individuals with PKU phenylalanine accumulates due to defective phenylalanine hydroxylase leading to potential neurological damage. While not the primary protein involved in PKU the understanding of PAL's pathway highlights how alternative pathways for phenylalanine breakdown may be exploited or considered in treatment strategies. Additionally the study of PAL in certain plant diseases may contribute insights into how modifying its activity can increase plant resistance against pathogens.
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Ammonium Chloride Standard Curve
Human Male Serum spiked with PAL.
Pooled normal human male AB serum was spiked with 5.5, 9.3, 12.7 and 20.6 μU of PAL respectively. The corresponding units of PAL recovered were 4.3, 8.8, 13.2 and 19.7 μU (recovery rates ranging from 78.4- 103.7%). The data shown is the average of three replicates where experiments were performed according to the kit protocol.
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