Description

Hydroxymandelonitrile Lyase, Arabidopsis Thaliana, Recombinant From E. Coli is a highly specific, recombinant enzyme derived from the model plant Arabidopsis thaliana and expressed in E. coli. This enzyme is critical for catalyzing the reversible cleavage of hydroxymandelonitrile to benzaldehyde and hydrogen cyanide, a key reaction in cyanogenic glycoside metabolism. It is an essential research tool for biochemists and molecular biologists studying plant defense mechanisms, cyanogenesis, and specialized metabolic pathways. The recombinant nature ensures high purity, batch-to-batch consistency, and reliable performance for demanding experimental applications.

Application

• Biochemical Research: Fundamental studies on the mechanism and kinetics of hydroxymandelonitrile lyase (HNL) activity.
• Plant Metabolism Studies: Investigating cyanogenic glycoside biosynthesis and degradation pathways in plants.
• Enzyme Engineering: Serving as a model protein for structure-function studies and protein engineering to alter substrate specificity or stability.
• Biosynthesis of Chiral Intermediates: Potential use in the stereoselective synthesis of cyanohydrins, which are valuable chiral building blocks for pharmaceuticals and agrochemicals.
• Educational Purposes: Used in advanced university laboratories for teaching enzymology and plant biochemistry principles.
• Comparative Genomics: Functional analysis of HNL gene homologs across different plant species.

Basic Information

Product Name	Hydroxymandelonitrile Lyase, Arabidopsis Thaliana, Recombinant From E. Coli
CAS No.	9075-38-1
Molecular Formula	Contact for details
Molecular Weight	Contact for details
Synonyms	Hydroxymandelonitrile lyase (HNL); (S)-Hydroxymandelonitrile lyase; AtHNL; Arabidopsis thaliana hydroxynitrile lyase; Oxynitrilase; Mandelonitrile lyase; Recombinant plant hydroxynitrile lyase; EC 4.1.2.11; Benzaldehyde lyase (in context); Cyanohydrin lyase
EINECS	Contact for details

Quality Control

Our recombinant enzyme is produced under stringent conditions to ensure high purity and specific activity. Each batch is subjected to rigorous quality testing, including SDS-PAGE for purity assessment and activity assays to confirm functional performance. Certificates of Analysis (COA) detailing protein concentration, specific activity, purity level, and buffer composition are provided with every shipment to guarantee compliance with research-grade standards.

Storage

Preserve in a tightly closed container, protected from light. For long-term stability, store the lyophilized powder at -20°C. Reconstituted enzyme solutions should be aliquoted and stored at -80°C to avoid repeated freeze-thaw cycles. The product is hygroscopic (moisture-sensitive).

Specification

Item	Specification
Appearance	Lyophilized powder
Purity (SDS-PAGE)	> 90%
Specific Activity	> 10 U/mg protein
Protein Content (Bradford)	> 80%
Identification (Activity)	Conforms
Endotoxin Level	< 1.0 EU/µg
Buffer	Tris-HCl, pH 8.0

Note: Specifications can be tailored. Please contact us for the detailed technical data sheet of a specific grade.