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Galactose 1-phosphate Potassium salt Sale

(Synonyms: 阿尔法-D-半乳糖1-磷酸二钾盐五水合物) 目录号 : GC31493

An intermediate in the interconversion of glucose and galactose

Galactose 1-phosphate Potassium salt Chemical Structure

Cas No.:19046-60-7

规格 价格 库存 购买数量
10mM (in 1mL Water)
¥491.00
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50mg
¥1,071.00
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Sample solution is provided at 25 µL, 10mM.

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产品描述

α-D-Galactose-1-phosphate is an intermediate in the interconversion of glucose and galactose. It is produced from galactose by galactokinase. Galactose-1-phosphate uridyl transferase reversibly catalyzes the conversion of UDP-glucose (Item No. 15602 and galactose-1-phosphate to glucose-1-phosphate and UDP-galactose.

Chemical Properties

Cas No. 19046-60-7 SDF
别名 阿尔法-D-半乳糖1-磷酸二钾盐五水合物
Canonical SMILES O=P(O[K])(O[K])O[C@H]1O[C@@H]([C@H](O)[C@H](O)[C@H]1O)CO
分子式 C6H15K2O11P 分子量 372.35
溶解度 Water : 125 mg/mL (371.67 mM) 储存条件 Store at -20°C
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溶解性数据

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1 mg 5 mg 10 mg
1 mM 2.6856 mL 13.4282 mL 26.8565 mL
5 mM 0.5371 mL 2.6856 mL 5.3713 mL
10 mM 0.2686 mL 1.3428 mL 2.6856 mL
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Research Update

Hereditary Dystonia Overview

The purpose of this overview on hereditary dystonia is to help clinicians determine if an individual has a hereditary dystonia in order to provide information regarding recurrence risk and evaluation of relatives at risk. Goal 1: Describe the clinical characteristics of dystonia. Goal 2: Review the causes of hereditary dystonia. Goal 3: Provide an evaluation strategy to determine the etiology of hereditary dystonia in a proband. Goal 4: Review the differential diagnosis of hereditary dystonia (i.e., non-genetic causes of dystonia). Goal 5: Provide information regarding recurrence risk and evaluation of relatives of a proband with hereditary dystonia who are at risk.

The C-terminal domain of the Salmonella enterica WbaP (UDP-galactose:Und-P galactose-1-phosphate transferase) is sufficient for catalytic activity and specificity for undecaprenyl monophosphate

Two families of membrane enzymes catalyze the initiation of the synthesis of O-antigen lipopolysaccharide. The Salmonella enterica Typhimurium WbaP is a prototypic member of one of these families. We report here the purification and biochemical characterization of the WbaP C-terminal (WbaP(CT)) domain harboring one putative transmembrane helix and a large cytoplasmic tail. An N-terminal thioredoxin fusion greatly improved solubility and stability of WbaP(CT) allowing us to obtain highly purified protein. We demonstrate that WbaP(CT) is sufficient to catalyze the in vitro transfer of galactose (Gal)-1-phosphate from uridine monophosphate (UDP)-Gal to the lipid carrier undecaprenyl monophosphate (Und-P). We optimized the in vitro assay to determine steady-state kinetic parameters with the substrates UDP-Gal and Und-P. Using various purified polyisoprenyl phosphates of increasing length and variable saturation of the isoprene units, we also demonstrate that the purified enzyme functions highly efficiently with Und-P, suggesting that the WbaP(CT) domain contains all the essential motifs to catalyze the synthesis of the Und-P-P-Gal molecule that primes the biosynthesis of bacterial surface glycans.

Purification, properties, and isozyme pattern of galactose-1-phosphate uridyl transferase from calf liver