GLDA E.coli, Active
Glycerol dehydrogenase E.coli Recombinant, Active
Cat. No.
BT8916
Source
Escherichia Coli.
Synonyms
ECK3937,
JW5556, Glycerol dehydrogenase, GDH, GLDH, b3945.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description
GLDA E.coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 390 amino acids (1-367 a.a) and having a molecular mass of 41.1kDa.
GLDA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
GLDA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Introduction
Glycerol dehydrogenase (GldA) is an enzyme that facilitates the NAD-dependent oxidation of glycerol to dihydroxyacetone (glycerone). This process is crucial for microorganisms as it enables them to utilize glycerol as a carbon source in anaerobic environments. In E. coli, GldA plays a vital role in regulating the intracellular levels of dihydroxyacetone by catalyzing the reverse reaction, converting dihydroxyacetone back into glycerol. GldA exhibits broad substrate specificity, demonstrating its ability to oxidize 1,2-propanediol and reduce glycolaldehyde, methylglyoxal, and hydroxyacetone into ethylene glycol, lactaldehyde, and 1,2-propanediol, respectively.
Description
Recombinant GLDA from E. coli, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 390 amino acids (amino acids 1-367) and possessing a molecular weight of 41.1 kDa. For purification purposes, a 23 amino acid His-tag is fused to the N-terminus of GLDA, and proprietary chromatographic techniques are employed.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The GLDA protein solution has a concentration of 1 mg/ml and is prepared in a solution of phosphate-buffered saline (pH 7.4) containing 10% glycerol.
Stability
For short-term storage (up to 2-4 weeks), the product can be stored at 4°C. For longer storage, it is recommended to freeze the product at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Repeated freezing and thawing should be avoided.
Purity
The purity is determined to be greater than 95.0% based on SDS-PAGE analysis.
Biological Activity
The specific activity is measured to be greater than 14 units per milliliter. One unit is defined as the amount of enzyme required to oxidize 1.0 micromole of glycerol to dihydroxyacetone per minute at a pH of 8.0 and a temperature of 25°C.
Synonyms
ECK3937,
JW5556, Glycerol dehydrogenase, GDH, GLDH, b3945.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMDRIIQS PGKYIQGADV INRLGEYLKP LAERWLVVGD KFVLGFAQST
VEKSFKDAGL VVEIAPFGGE CSQNEIDRLR GIAETAQCGA ILGIGGGKTL DTAKALAHFM GVPVAIAPTI
ASTDAPCSAL SVIYTDEGEF DRYLLLPNNP NMVIVDTKIV AGAPARLLAA GIGDALATWF EARACSRSGA
TTMAGGKCTQ AALALAELCY NTLLEEGEKA MLAAEQHVVT PALERVIEAN TYLSGVGFES GGLAAAHAVH
NGLTAIPDAH HYYHGEKVAF GTLTQLVLEN APVEEIETVA ALSHAVGLPI TLAQLDIKED VPAKMRIVAE
AACAEGETIH NMPGGATPDQ VYAALLVADQ YGQRFLQEWE.
Product Science Overview
Source and Expression
The recombinant glycerol dehydrogenase from Escherichia coli (E. coli) is a full-length protein expressed in E. coli cells. This recombinant form is often tagged with a His-tag at the N-terminus to facilitate purification through chromatographic techniques . The enzyme typically consists of 367 amino acids and has a molecular mass of approximately 41.1 kDa .
Purity and Activity
The recombinant glycerol dehydrogenase from E. coli is known for its high purity, often exceeding 95%, making it suitable for various analytical techniques such as SDS-PAGE, functional assays, and mass spectrometry . The enzyme exhibits specific activity greater than 14 units per milligram of protein, indicating its high catalytic efficiency .
Applications
This enzyme is utilized in several applications, including:
- Biotransformation: It is used in the aerobic biotransformation of glycerol to produce value-added metabolic products .
- Research: Due to its high purity and activity, it is widely used in research to study glycerol metabolism and related pathways.
- Industrial Processes: The enzyme’s ability to convert glycerol into dihydroxyacetone makes it valuable in industrial processes that require this conversion.
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