DL-Asparagine
(Synonyms: DL-天冬酰胺) 目录号 : GC61431
DL-Asparagine是L-Aparagine和D-Aparagine对映异构体的外消旋混合物。DL-Asparagine可以用于细菌的生长培养基中。
Cas No.:3130-87-8
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >98.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
DL-Asparagine is a racemic melange of the Aparagine L and D-enantiomers. DL-Asparagine has been used in growth-media for bacteria-growth[1].
[1]. Nabila Moussa Slimane, et al. dl-Asparaginium nitrate. Acta Crystallogr Sect E Struct Rep Online. 2009 Aug 19;65(Pt 9):o2180-1.
| Cas No. | 3130-87-8 | SDF | |
| 别名 | DL-天冬酰胺 | ||
| Canonical SMILES | NC(C(O)=O)CC(N)=O | ||
| 分子式 | C4H8N2O3 | 分子量 | 132.12 |
| 溶解度 | 储存条件 | Store at -20°C | |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 制备储备液 | |||
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1 mg | 5 mg | 10 mg |
| 1 mM | 7.5689 mL | 37.8444 mL | 75.6888 mL |
| 5 mM | 1.5138 mL | 7.5689 mL | 15.1378 mL |
| 10 mM | 0.7569 mL | 3.7844 mL | 7.5689 mL |
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
Freezing effect on chirality amplification of L-asparagine by crystallization of the racemate in preferential condition
Cryo Letters 2011 Nov-Dec;32(6):447-50.PMID:22227704doi
The role of freezing in stereoselection by crystallization of a saturated DL-Asparagine solution in preferential condition of L-asparagine, has been investigated. To this end, the L-asparagine excess obtained by crystallization and then kept of different lengths of time at n20 degree C in frozen aqueous solution was analyzed. The samples of the yielded materials were derivatised according to Marfey's method. These derivatives were traced and evaluated by RP-HPLC analysis. The relatively best effects appeared after a one day treatment, where the freezing induced asymmetry amplifications and it increased the L-enantiomer excess from 10 mol percent to 34.9, 35.0 and 35.5 mol percent, respectively. Here we provide the first example of the influence of freezing on chirality amplification by preferential crystallization. Also some speculations are made about the implications of our findings in the prebiotic events of L-amino acids.
Degree of supersaturation-regulated chiral symmetry breaking in one crystal
J Phys Chem B 2007 Oct 4;111(39):11346-9.PMID:17824693DOI:10.1021/jp075238p.
This paper aimed at studying chiral symmetry-breaking phenomena in one crystal. Preferential crystallization of racemic asparagines was carried out in nonseeded stagnant solutions through slow cooling. By varying the supersaturation, only one transparent crystal could be obtained at enough low supersaturation of DL-Asparagine, and the crystal was not pure enantiomer with crystal enantiomeric excess increasing inversely with the degree of supersaturation. Crystal enantiomeric excess can amount up to 85% in one transparent crystal. Because no secondary nucleation occurred except for stochastic primary nucleation, we suggest that primary nucleation and competition between l- and d-nuclei were considered to be a mechanism for asymmetry amplification. High-performance capillary electrophoresis coupled with laser-induced fluorescence was used to separate and quantify l- and d-asparagine and the enantiomeric excess value can be calculated according to their concentration.
Simultaneous measurement of amino acid enantiomers in the serum of late-life depression patients using convenient LC-MS/MS method with Nα-(5-fluoro-2,4-dinitrophenyl)-l-leucinamide Derivatization
J Pharm Biomed Anal 2023 Apr 5;230:115387.PMID:37030045DOI:10.1016/j.jpba.2023.115387.
D-amino acids may be indicators of late-life depression but separation and quantification of enantiomers which differ only by optical rotation sign remain challenging due to their identical physical and chemical properties. A convenient LC-MS/MS method was developed for the simultaneous measurement of l- and d-amino acids based on the chiral derivatization reagent, Nα-(5-fluoro-2,4-dinitrophenyl)-L-leucinamide, and conventional octadecylsilane reversed-phase column. Methanol was used as the extraction solvent and a single-step derivatization reaction using volatile triethylamine eliminated the requirement for desalination prior to LC-MS/MS. Simultaneous separation and identification of 21 amino acids and the enantiomeric compositions of the 18 chiral proteogenic entities were achieved. Low limits of detection (0.03-4.0 nM), wide linear range (0.01-20 μM), good precision (RSDs < 10 %) and negligible matrix effects indicated the suitability of the method. Application of the method to the quantification of serum chiral amino acids in late-life depression patients (n = 40) and controls (n = 35) found a total of 17 L-amino acids, 14 D-amino acids, DL-Asparagine, glycine and γ-aminobutyric acid. The statistical evaluation showed significant differences of glycine, L-threonine and D-methionine between late-life depression patients and controls, indicating that these are potential biomarkers of late-life depression.
L-asparaginase activity in cell-free extracts of Thermoactinomyces vulgaris 13 M.E.S
Zentralbl Mikrobiol 1983;138(5):397-404.PMID:6649956doi
Crude extracts of Thermoactinomyces vulgaris 13 M.E.S. were prepared by different procedures and their L-asparaginase activity was compared. The optimum conditions for the enzyme activity in the crude extract was exerted at pH 8.8, using borate or tris-HCl buffer, or at pH 7.4, using phosphate buffer, after a reaction time of 30 minutes at 50-55 degrees C, using 1.35-5.4 mg protein of the crude extract. The enzyme showed an apparent km value of 4.5 x 10(-3), was more thermostable in crude extracts than in whole cells, and was inhibited by HgCl2, KCN, DL-Asparagine, L-aspartic acid, and ammonium hydroxide. Enzyme purification by alcohol precipitation and gel filtration was attempted.