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
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.
Physical form
This product is a sterile-filtered aqueous buffered solution.
Other Notes
One unit will hydrolyze 1 μmole of p-nitrophenyl α-D-galactopyranoside per min at pH 6.5 at 25 °C.
Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 2
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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K Schmid et al.
European journal of biochemistry, 67(1), 95-104 (1976-08-01)
The utilization by Escherichia coli K12 of raffinose as sole carbon source depends on a new raffinose transport system, an invertase and an alpha-galactosidase specified by the Raf-plasmid D1021. The alpha-galactosidase was purified to homogeneity from a mutant strain with
Shuo Gao et al.
Frontiers in chemistry, 9, 709581-709581 (2021-08-03)
For wide applications of the lacZ gene in cellular/molecular biology, small animal investigations, and clinical assessments, the improvement of noninvasive imaging approaches to precisely assay gene expression has garnered much attention. In this study, we investigate a novel molecular platform
Romain Merceron et al.
The Journal of biological chemistry, 287(47), 39642-39652 (2012-09-27)
The α-galactosidase AgaA from the thermophilic microorganism Geobacillus stearothermophilus has great industrial potential because it is fully active at 338 K against raffinose and can increase the yield of manufactured sucrose. AgaB has lower affinity for its natural substrates but
Hongwei Gao et al.
Artificial cells, nanomedicine, and biotechnology, 41(1), 32-36 (2012-10-04)
Enzymatical conversion of A or B RBCs into group O RBCs (ECORBCs) was achieved by using α-N-acetylgalactosaminidase and α-galactosidase, respectively. Now, we initiated AB to O-RBC conversion by using these two enzymes together. But α-N-acetylgalactosaminidase and α-galactosidase's preserving and their
Camilla Tøndel et al.
Journal of the American Society of Nephrology : JASN, 24(1), 137-148 (2013-01-01)
The effect of early-onset enzyme replacement therapy on renal morphologic features in Fabry disease is largely unknown. Here, we evaluated the effect of 5 years of treatment with agalsidase alfa or agalsidase beta in 12 consecutive patients age 7-33 years
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