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Merck
CN

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:
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产品名称

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

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。

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。

Physical form

该产品是无菌过滤的水性缓冲溶液。

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

历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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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
Costanza Simoncini et al.
The neurologist, 18(6), 413-414 (2012-11-02)
Fabry disease (FD) is a rare, X-linked lysosomal storage disorder with multiorgan involvement. FD is caused by a partial or total deficit of α-galactosidase A enzyme, which is responsible for the accumulation of glycosphingolipids in a variety of cell types.
Masahisa Kobayashi et al.
Molecular genetics and metabolism, 107(4), 711-715 (2012-11-14)
Fabry disease is an X-linked lysosomal disorder resulting from mutations in the α-galactosidase A (GLA) gene. Recent reports described that the E66Q mutation of GLA is not a disease-causing mutation. However, no pathological study was reported. We carried out pathological

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