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Cutinase Protein, Thermobifida fusca, Recombinant (His)

(Synonyms: Cutinase) Copy Product Info

Synonyms: Cutinase

Catalog No. TMPJ-01440 Copy Product Info
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.
Pack SizePriceUSA StockGlobal StockQuantity
5 μg$1127-10 days7-10 days
10 μg$1837-10 days7-10 days
20 μg$2927-10 days7-10 days
50 μg$5457-10 days7-10 days
100 μg$8137-10 days7-10 days
200 μg$1,1907-10 days7-10 days
500 μg$2,0707-10 days7-10 days
1 mg$2,9707-10 days7-10 days
For In stock only · Estimated delivery: USA Stock (1-2 days) Global Stock (5-7 days)
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For research use only—not for human use. No sales to individuals. Use as intended only.
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Purity:Greater than 95% as determined by reducing SDS-PAGE.
Appearance:Liquid
Color:Transparent
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Product Introduction

Bioactivity
Bioactivity
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.
Description
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.
Species
Thermobifida fusca
Expression System
E. coli
TagC-6xHis
Accession NumberE5BBQ3
Amino AcidAla1-Phe261
ConstructionAla1-Phe261
Protein Purity
Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Endotoxin< 0.1 ng/µg (1 EU/µg) as determined by LAL test.
FormulationSupplied as a 0.2 μm filtered solution of PBS, 50% Glycerol, pH 7.4.
Stability & StorageLyophilized 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.
ShippingProteins are shipped with blue ice.
SynonymsCutinase
Research Background
Chemical Properties
Molecular Weight28-30 KDa (reducing condition)
Storage & Solubility Information
StorageStore at low temperature Lyophilized powder: -20~-80°C for 1 year | Solution: -80°C for 6 months

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Please see Inhibitor Handling Instructions for more frequently ask questions. Topics include: how to prepare stock solutions, how to store products, and cautions on cell-based assays & animal experiments, etc
Related Tags: Cutinase Protein, Thermobifida fusca, Recombinant (His) chemical structure | Cutinase Protein, Thermobifida fusca, Recombinant (His) molecular weight