G7163
α-Galactosidase, positionally specific from Escherichia coli
recombinant, expressed in E. coli, buffered aqueous solution
Synonym(s):
1,6-alpha-D-galactoside galactohydrolase, alpha-Galactosidase, melibiase
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About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.32
Recommended Products
recombinant
expressed in E. coli
Quality Level
form
buffered aqueous solution
specific activity
≥20 units/mg protein
mol wt
80 kDa
shipped in
wet ice
storage temp.
2-8°C
Gene Information
Escherichia coli CFT073 ... melA(1037886)
Related Categories
Biochem/physiol Actions
Cleaves α(1→3)- and α(1→6)-linked, non-reducing terminal galactose from complex carbohydrates and glycoproteins. It is particularly efficient for removing α-linked galactose under conditions where the pH must be neutral or above, for example, with live cells.
Unit Definition
One unit will hydrolyze 1 μmole of p-nitrophenyl α-D-galactopyranoside per min at pH 6.5 at 25 °C.
Physical form
This product is a sterile-filtered aqueous buffered solution.
inhibitor
Product No.
Description
Pricing
substrate
Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 2
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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K Schmid et al.
European journal of biochemistry, 67(1), 95-104 (1976-08-01)
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Journal of microbiology and biotechnology, 22(11), 1532-1539 (2012-11-06)
The α-galactosidase-coding gene agaAJB13 was cloned from Sphingomonas sp. JB13 showing 16S rDNA (1,343 bp) identities of < or =97.2% with other identified Sphingomonas strains. agaAJB13 (2,217 bp; 64.9% GC content) encodes a 738-residue polypeptide (AgaAJB13) with a calculated mass
Xiao-Liang Pan et al.
The journal of physical chemistry. B, 117(2), 484-489 (2012-12-20)
The enzyme α-galactosidase (α-GAL), a member of glycoside hydrolase family 27, catalyzes the removal of a nonreducing terminal α-galactose residue from polysaccharides, glycolipids, and glycopeptides. α-GAL is believed to have the double displacement retaining reaction mechanism. In this work, the
M Benelmekki et al.
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Biomagnetic immobilization of histidine-rich proteins based on the single-step affinity adsorption of transition metal ions continues to be a suitable practice as a cost effective and a up scaled alternative to the to multiple-step chromatographic separations. In our previous work
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