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Cutinase belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is cutin hydrolase. Cutinase is a serine esterase containing the classical Ser, His, Asp triad of serine hydrolases. The protein belongs to the alpha-beta class, with a central beta-sheet of 5 parallel strands covered by 5 helices on either side of the sheet. Cutin monomers released from the cuticle by small amounts of cutinase on fungal spore surfaces can greatly increase the amount of cutinase secreted by the spore. The active site cleft is partly covered by 2 thin bridges formed by amino acid side chains, by contrast with the hydrophobic lid possessed by other lipases. The protein also contains 2 disulfide bridges, which are essential for activity, their cleavage resulting in complete loss of enzymatic activity.
规格 | 价格 | 库存 | 数量 |
---|---|---|---|
10 μg | ¥ 1,170 | 5日内发货 | |
50 μg | ¥ 3,470 | 5日内发货 | |
500 μg | ¥ 13,200 | 5日内发货 | |
1 mg | ¥ 18,900 | 5日内发货 |
生物活性 | Activity has not been tested. It is theoretically active, but we cannot guarantee it. If you require protein activity, we recommend choosing the eukaryotic expression version first. |
产品描述 | Cutinase belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is cutin hydrolase. Cutinase is a serine esterase containing the classical Ser, His, Asp triad of serine hydrolases. The protein belongs to the alpha-beta class, with a central beta-sheet of 5 parallel strands covered by 5 helices on either side of the sheet. Cutin monomers released from the cuticle by small amounts of cutinase on fungal spore surfaces can greatly increase the amount of cutinase secreted by the spore. The active site cleft is partly covered by 2 thin bridges formed by amino acid side chains, by contrast with the hydrophobic lid possessed by other lipases. The protein also contains 2 disulfide bridges, which are essential for activity, their cleavage resulting in complete loss of enzymatic activity. |
种属 | Thermobifida fusca |
表达系统 | E. coli |
标签 | C-6xHis |
蛋白编号 | E5BBQ3 |
别名 | Cutinase |
氨基酸序列 | Ala1-Phe261 |
蛋白构建 | Ala1-Phe261 |
蛋白纯度 | Greater than 95% as determined by reducing SDS-PAGE. (QC verified) |
分子量 | 28-30 KDa (reducing condition) |
内毒素 | < 0.1 ng/µg (1 EU/µg) as determined by LAL test. |
缓冲液 | Supplied as a 0.2 μm filtered solution of PBS, 50% Glycerol, pH 7.4. |
存储 | Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots. |
运输方式 | In general, Lyophilized powders are shipping with blue ice. Solutions are shipping with dry ice. |
研究背景 | Cutinase belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is cutin hydrolase. Cutinase is a serine esterase containing the classical Ser, His, Asp triad of serine hydrolases. The protein belongs to the alpha-beta class, with a central beta-sheet of 5 parallel strands covered by 5 helices on either side of the sheet. Cutin monomers released from the cuticle by small amounts of cutinase on fungal spore surfaces can greatly increase the amount of cutinase secreted by the spore. The active site cleft is partly covered by 2 thin bridges formed by amino acid side chains, by contrast with the hydrophobic lid possessed by other lipases. The protein also contains 2 disulfide bridges, which are essential for activity, their cleavage resulting in complete loss of enzymatic activity. |
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