L-Asparagine (hydrate)
(Synonyms: L-天冬酰胺一水合物) 目录号 : GC49295
A non-essential amino acid
Cas No.:5794-13-8
Sample solution is provided at 25 µL, 10mM.
;)
,-1-7$$$37316672.jpg');)
;)
;)
$$$36806353.jpg');)
;33(7)%EF%BC%9A546-561$$$37156877.jpg');)
;)
;)
;)
%201124-1138.$$$35908550.jpg');)
%20766-780.$$$37100057.jpg');)
%20418-432.$$$36893736.jpg');)
%EF%BC%9A-240-255.$$$35108512.jpg');)
533-545$$$36543525.jpg');)
%201-13.$$$36600053.jpg');)
;)
Quality Control & SDS
- View current batch:
- Purity: >99.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
L-Asparagine is a non-essential amino acid.1 It is formed from L-aspartic acid and L-glutamine by asparagine synthetase (ASNS), and it is deamidated by L-asparaginase to produce L-aspartic acid and ammonia.2,3 L-Asparagine (0.3 mM) reverses ASNS siRNA knockdown-induced decreases in proliferation in a panel of six human cancer cell lines, indicating that both exogenous and endogenous L-asparagine promote proliferation of these cells.4 Formulations containing L-asparagine have been used as dietary supplements.
1.Chiu, M.I., Taurino, G., Bianchi, M.G., et al.Asparagine synthetase in cancer: Beyond acute lymphoblastic leukemiaFront. Oncol.91480(2020) 2.Zhu, W., Radadiya, A., Bisson, C., et al.High-resolution crystal structure of human asparagine synthetase enables analysis of inhibitor binding and selectivityCommun. Biol.2345(2019) 3.Covini, D., Tardito, S., Bussolati, O., et al.Expanding targets for a metabolic therapy of cancer: L-AsparaginaseRecent Pat. Anticancer Drug Discov.7(1)4-13(2012) 4.Pathria, G., Lee, J.S., Hasnis, E., et al.Translational reprogramming marks adaptation to asparagine restriction in cancerNat. Cell Biol.21(12)1590-1603(2019)
| Cas No. | 5794-13-8 | SDF | |
| 别名 | L-天冬酰胺一水合物 | ||
| Canonical SMILES | NC(C[C@H](N)C(O)=O)=O.O | ||
| 分子式 | C4H8N2O3·H2O | 分子量 | 150.1 |
| 溶解度 | Methanol: slightly soluble,PBS (pH 7.2): slightly soluble | 储存条件 | -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。 |
||
| 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 | |||
 |
1 mg | 5 mg | 10 mg |
| 1 mM | 6.6622 mL | 33.3111 mL | 66.6223 mL |
| 5 mM | 1.3324 mL | 6.6622 mL | 13.3245 mL |
| 10 mM | 0.6662 mL | 3.3311 mL | 6.6622 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。
Large-scale recovery and purification of L-asparaginase from Erwinia carotovora
Appl Biochem Biotechnol 1986 Jun;12(3):229-47.PMID:3752984DOI:10.1007/BF02798424.
A large-scale process was developed to purify gram quantities of a therapeutic enzyme, L-asparaginase, from submerged cultures of Erwinia carotovora. Cells were harvested from 150 L of fermentation broth and washed. A cellular acetone powder was prepared and extracted with pH 9.5 borate buffer. After continuous centrifugation and filtration to remove cell debris, the acetone powder extract was adjusted to pH 7.7 and adsorbed onto a 16-L CM-Sepharose Fast Flow column, with a precolumn packed with Cell Debris Remover. The enzyme was desorbed from the catin-exchange column at pH 9.0 and further purified with an affinity column of L-Asparagine Sepharose CL-4B. After dialysis-concentration to remove buffer salt, the enzyme was depyrogenated, formulated, sterile filled, and lyophilized as a single-dose final product. The final-product evaluation included analysis of the content of protein, sodium chloride, glycine, sodium, glucose hydrate, phosphate, and endotoxin, as well as reconstitution, potency, pH, specific activity, uniformity of fill, and sterility. The product was further subjected to visual examination, sodium dodecyl sulfate polyacrylamide gel electrophoresis, native gel electrophoresis, isoelectric focusing, amino acid analysis, N-terminal sequencing, peptide mapping, and immunological comparison.
Study of the behaviour of amino acids in aqueous solution by time-domain NMR and high-resolution NMR
Magn Reson Chem 2005 Apr;43(4):309-15.PMID:15674820DOI:10.1002/mrc.1538.
The study of protein hydration by time-domain NMR is complicated by the great number of interactions involved, resulting from the presence of several amino acids and the possible modifications produced by the various structures. Moreover, a good comprehension of the molecular interactions of the simple amino acids in solution is essential to elucidate the mechanism of the biological functions of proteins. Measurements of transverse relaxation rates of the protons of water (R(2) = 1/T(2)) in aqueous solutions of amino acids such as L-glycine, L-Asparagine, L-arginine and L-tryptophan were carried out in order to study the effects of chemical exchange and molecular diffusion on the amplitude of R(2). The values of R(2) measured by the Carr-Purcell-Meiboom-Gill (CPMG) sequence were studied while varying the solution pH and the parameters of the CPMG sequence. The dependence of R(2) on pH and tau (inter-pulse delay between the first and the second pulses of the CPMG sequence) is interpreted in terms of chemical exchange between the protons of water and those of the labile amino acid groups. This interpretation was confirmed by the analysis of the proton spectra acquired using a 300 MHz NMR spectrometer.
Racemization of the Succinimide Intermediate Formed in Proteins and Peptides: A Computational Study of the Mechanism Catalyzed by Dihydrogen Phosphate Ion
Int J Mol Sci 2016 Oct 10;17(10):1698.PMID:27735868DOI:10.3390/ijms17101698.
In proteins and peptides, d-aspartic acid (d-Asp) and d-β-Asp residues can be spontaneously formed via racemization of the succinimide intermediate formed from l-Asp and L-Asparagine (l-Asn) residues. These biologically uncommon amino acid residues are known to have relevance to aging and pathologies. Although nonenzymatic, the succinimide racemization will not occur without a catalyst at room or biological temperature. In the present study, we computationally investigated the mechanism of succinimide racemization catalyzed by dihydrogen phosphate ion, H₂PO₄-, by B3LYP/6-31+G(d,p) density functional theory calculations, using a model compound in which an aminosuccinyl (Asu) residue is capped with acetyl (Ace) and NCH₃ (Nme) groups on the N- and C-termini, respectively (Ace-Asu-Nme). It was shown that an H₂PO₄- ion can catalyze the enolization of the Hα-Cα-C=O portion of the Asu residue by acting as a proton-transfer mediator. The resulting complex between the enol form and H₂PO₄- corresponds to a very flat intermediate region on the potential energy surface lying between the initial reactant complex and its mirror-image geometry. The calculated activation barrier (18.8 kcal·mol-1 after corrections for the zero-point energy and the Gibbs energy of hydration) for the enolization was consistent with the experimental activation energies of Asp racemization.