G7163
α-半乳糖苷酶，位置特异性 来源于大肠杆菌
recombinant, expressed in E. coli, buffered aqueous solution
别名:
1,6-alpha-D-galactoside galactohydrolase, alpha-Galactosidase, melibiase
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关于此项目
化学文摘社编号:
UNSPSC Code:
12352204
NACRES:
NA.32
MDL number:
Specific activity:
≥20 units/mg protein
Recombinant:
expressed in E. coli
recombinant
expressed in E. coli
form
buffered aqueous solution
specific activity
≥20 units/mg protein
mol wt
80 kDa
shipped in
wet ice
storage temp.
2-8°C
Quality Level
Gene Information
Escherichia coli CFT073 ... melA(1037886)
Biochem/physiol Actions
从复杂的碳水化合物和糖蛋白中裂解 α（1→3）-和 α（1→6）-连接的非还原性末端半乳糖。在 pH 必须为中性或更高的条件下（例如，活细胞），这种方法对于去除 α-连接的半乳糖特别有效。
Physical form
该产品是无菌过滤的水性缓冲溶液。
Other Notes
在 pH 6.5，25°C 下，一个单位每分钟将水解 1 μ 摩尔对硝基苯基 α-D-吡喃半乳糖苷。
存储类别
12 - Non Combustible Liquids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
常规特殊物品
此项目有
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
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
Junpei Zhou et al.
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
M Benelmekki et al.
Colloids and surfaces. B, Biointerfaces, 101, 370-375 (2012-09-27)
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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