melA E. coli

Alpha-Galactosidase E.coli Recombinant
Cat. No.
BT21411
Source
E.coli.
Synonyms
Mel-7, Alpha-galactosidase, b4119, JW4080.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90% 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

melA E. coli Recombinant produced in E. coli is a single polypeptide chain containing 474 amino acids (1-451) and having a molecular mass of 53.0kDa.
melA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
melA, a member of the glycosyl hydrolase 4 family, catalyzes the hydrolysis of saccharides containing o-1,6,-galactoside bonds. This enzymatic activity is conserved across E. coli, human, and yeast, although the enzyme's cellular localization differs between these species. In E. coli, melA is cytoplasmic, while in humans and yeast, it is secreted. Despite these localization differences, the active melA enzyme from all three species exhibits nearly identical molecular weight and likely shares structural similarities.
Description
Recombinant melA from E. coli, produced in E. coli, is a single polypeptide chain comprising 474 amino acids (residues 1-451) with a molecular mass of 53.0 kDa. The protein consists of the melA sequence fused to a 23 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Physical Appearance
A sterile, colorless solution.
Formulation
The melA solution is provided at a concentration of 1 mg/ml in a buffer containing 20 mM Tris-HCl (pH 8.0), 1 mM DTT, 0.1 M NaCl, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), store at 4°C. For long-term storage, freeze at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
Purity is determined to be greater than 90% by SDS-PAGE analysis.
Synonyms
Mel-7, Alpha-galactosidase, b4119, JW4080.
Source
E.coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMMSAPKI TFIGAGSTIF VKNILGDVFH REALKTAHIA LMDIDPTRLE ESHIVVRKLM DSAGASGKIT CHTQQKEALE DADFVVVAFQ IGGYEPCTVT DFEVCKRHGL EQTIADTLGP GGIMRALRTI PHLWQICEDM TEVCPDATML NYVNPMAMNT WAMYARYPHI KQVGLCHSVQ GTAEELARDL NIDPATLRYR CAGINHMAFY LELERKTADG SYVNLYPELL AAYEAGQAPK PNIHGNTRCQ NIVRYEMFKK LGYFVTESSE HFAEYTPWFI KPGREDLIER YKVPLDEYPK RCVEQLANWH KELEEYKKAS RIDIKPSREY ASTIMNAIWT GEPSVIYGNV RNDGLIDNLP QGCCVEVACL VDANGIQPTK VGTLPSHLAA LMQTNINVQT LLTEAILTEN RDRVYHAAMM DPHTAAVLGI DEIYALVDDL IAAHGDWLPG WLHR.

Product Science Overview

Structure and Function

Alpha-Galactosidase from E. coli is a positionally specific enzyme that cleaves alpha (1→3)- and alpha (1→6)-linked, non-reducing terminal galactose residues from complex carbohydrates and glycoproteins . The enzyme is particularly efficient under neutral or slightly alkaline conditions, making it suitable for applications involving live cells .

The recombinant form of this enzyme is typically expressed in E. coli and purified to achieve high specific activity. For instance, one unit of alpha-galactosidase can hydrolyze 1 μmole of p-nitrophenyl alpha-D-galactopyranoside per minute at pH 6.5 and 25°C . The molecular weight of the enzyme is approximately 80 kDa .

Applications

  1. Food Industry: Alpha-galactosidase is used to reduce flatulence caused by the consumption of legumes and other plant-based foods that contain raffinose and stachyose. By breaking down these complex sugars, the enzyme helps in reducing gastrointestinal discomfort.

  2. Medical Applications: The enzyme is used in the treatment of Fabry disease, a genetic disorder caused by the deficiency of alpha-galactosidase A. Recombinant alpha-galactosidase can help in breaking down the accumulated glycolipids in the cells of affected individuals.

  3. Biotechnological Research: Alpha-galactosidase is used in various research applications, including the study of glycoprotein biosynthesis and the development of glycoengineering techniques. The enzyme’s ability to cleave specific galactosidic linkages makes it a valuable tool in the structural analysis of complex carbohydrates.

Production and Purification

The production of recombinant alpha-galactosidase involves cloning the gene encoding the enzyme into an E. coli expression system. The recombinant enzyme is then purified using chromatographic techniques to achieve high purity and specific activity . The enzyme is typically supplied as a sterile-filtered aqueous buffered solution and stored at 2-8°C to maintain its stability .

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