BioReagent 级 ，适用于对基线干扰要求严格的色谱和分析工作流程。
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在色谱分析、有机合成和交叉偶联反应领域已被 0 篇同行评审文献引用。
苯丙氨酸解氨酶（PAL）是催化L-苯丙氨酸脱氨生成反式肉桂酸的关键酶，广泛存在于高等植物、酵母及真菌中。该酶于1961年由J. Koukol在大麦中发现，分子量约为300 kDa，是苯丙烷代谢途径的入口酶，负责将苯丙氨酸导向酚类化合物及木质素的合成。其活性对外界刺激（如光照、损伤、激素）响应迅速，但常在诱导升高后伴随快速失活，该特性使其成为研究植物抗逆反应与木质素沉积代谢机制的核心指标，对改良水果品质（如减少石细胞）具有重要意义。 本试剂盒原理是：在最适反应条件下，酶催化产物反式肉桂酸在290 nm处具有特征吸收，通过酶标仪动态测定该波长下吸光度随时间的变化速率，即可精准计算出酶活性。本品适用于植物组织裂解液、匀浆液或血清等样品的内源性PAL活性检测，尤其针对水果材料优化，仅限科研使用。
Phenylalanine ammonia-lyase (PAL) is a key enzyme that catalyzes the deamination of L-phenylalanine to produce trans-cinnamic acid. It is widely present in higher plants, yeast, and fungi. Discovered in barley by J. Koukol in 1961 with a molecular weight of approximately 300 kDa, PAL serves as the gateway enzyme of the phenylpropanoid metabolic pathway, directing phenylalanine toward the synthesis of phenolic compounds and lignin. Its activity responds rapidly to external stimuli such as light, injury, and hormones, but this induced increase is often followed by rapid inactivation. This characteristic makes PAL a central indicator for studying plant stress responses and the metabolic mechanisms of lignin deposition, holding significant importance for improving fruit quality, such as by reducing stone cell content. The principle of this kit is based on the characteristic absorption of the enzymatic product, trans-cinnamic acid, at 290 nm under optimal reaction conditions. By dynamically measuring the rate of absorbance change over time at this wavelength using a microplate reader, the PAL activity can be accurately calculated. This product is suitable for the detection of endogenous PAL activity in samples such as plant tissue lysates, homogenates, or serum, with particular optimization for fruit materials. It is intended for research use only.
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