L-Lysine
(Synonyms: L-赖氨酸) 目录号 : GC36470
Lysine is an α-amino acid that is used in the biosynthesis of proteins and is required for growth and tissue repair.
Cas No.:56-87-1
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
Lysine is an α-amino acid that is used in the biosynthesis of proteins and is required for growth and tissue repair.
| Cas No. | 56-87-1 | SDF | |
| 别名 | L-赖氨酸 | ||
| Canonical SMILES | N[C@@H](CCCCN)C(O)=O | ||
| 分子式 | C6H14N2O2 | 分子量 | 146.19 |
| 溶解度 | Water: 100 mg/mL (684.04 mM); DMSO: < 1 mg/mL (insoluble or slightly soluble) | 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 | 6.8404 mL | 34.2021 mL | 68.4041 mL |
| 5 mM | 1.3681 mL | 6.8404 mL | 13.6808 mL |
| 10 mM | 0.684 mL | 3.4202 mL | 6.8404 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。
Comprehensive Safety Assessment of L-Lysine Supplementation from Clinical Studies: A Systematic Review
J Nutr 2020 Oct 1;150(Suppl 1):2561S-2569S.PMID:33000161DOI:10.1093/jn/nxaa218.
Background: Despite the widespread use of L-Lysine in dietary supplements, the safety information pertinent to excessive L-Lysine ingestion is limited and, to the best of our knowledge, there is no published systematic review of safety. Objective: The objective of this study was to assess the clinical safety of L-Lysine supplementation of a regular diet. Methods: We searched PubMed, Cochrane Library, Ichushi Web, and EBSCOhost using the relevant keywords, "L-Lysine" and "clinical trial." To investigate all adverse events observed during intervention trials, we included all intervention studies with orally ingested L-Lysine without restricting background factors, environment, study designs, and sample sizes. Results: We identified 71 articles, which included 3357 study subjects. The L-Lysine doses ranged from 16.8 to 17.5 g/d, and the dosing period ranged from 1 to 1095 d. The observed adverse events were mainly subjective gastrointestinal tract symptoms; however, the risk analysis for incidence of gastrointestinal symptoms was not statistically significant (risk ratio of 1.02). Conclusion: The provisional no-observed-adverse-effect level in healthy human subjects was based on gastrointestinal symptoms and identified at 6.0 g/d. The review protocol was registered at umin.ac.jp as UMIN000028914 before the beginning of the study.
L-Lysine: Its antagonism with L-arginine in controlling viral infection. Narrative literature review
Br J Clin Pharmacol 2022 Nov;88(11):4708-4723.PMID:35723628DOI:10.1111/bcp.15444.
Knowledge about viral characteristics, mechanisms of entry into the host cell and multiplication/dissemination can help in the control and treatment of viral pathologies. Several nutritional factors linked to the host may favour viral multiplication and their control, may lead to new prophylactic alternatives and/or antiviral therapies. The objective of this review is to discuss the relationship between the amino acid L-Lysine and the control of viral infections, aiming at a possible therapeutic property. This research used databases such as PubMed, Web of Science, Scielo, Medline and Google Scholar, as well as searching for references cited by journals. The time frame covered the period between 1964 and January 2022. The observed studies have shown that the usual antiviral therapies are not able to interfere with the viruses in their latent state; however, they can interfere with the adhesion and fusion of viral particles or the production of proteins, which play an important role in viral epidemiology and control, particularly in the initial moment and in reactivation. Lysine is an amino acid that can interfere mainly in the formation of capsid proteins and DNA by a competitive antagonism with amino acid arginine, which is an essential amino acid for some viruses, and also by promoting the increase of arginase, increasing the catabolism of arginine. Although there is evidence of the importance of L-Lysine in viral control, more studies are needed, with a view to new antiviral therapies.
A comprehensive review of methods for determination of L-Lysine with detailed description of biosensors
Int J Biol Macromol 2021 Sep 1;186:445-461.PMID:34229019DOI:10.1016/j.ijbiomac.2021.07.010.
L-Lysine being one of the essential amino acids is not produced by the body, but is obtained through diet. L-Lysine determination is important in the food and pharmaceutical industries as well as have medical and diagnostic applications. The normal L-Lysine levels in a healthy human serum sample is 150 to 250 μmol/l. There is imbalance in L-Lysine levels in certain diseased conditions. So, it could be a biomarker for diagnosis. Various basic methods are available for the determination of L-Lysine such as colorimetric, radioisotope dilution, chromatographic, fluorometric and voltammetric methods. These methods have certain disadvantages like sample pretreatment, costly, time consuming and requirement of skilled personnel. These drawbacks are overcome by the use of biosensors due to their high sensitivity, stability and specificity. The present review article discusses about the principles, merits and demerits of the various analytic methods for determination of L-Lysine with special emphasis on biosensors. L-Lysine biosensors work ideally under the optimum pH 5 to 10, potential range -0.05 to 1.5 V, temperature 25 to 40 °C, with linear range 0.01 to 5500 μM, detection limit 0.000004 to 650 μM and response time 2 to 300 s. The sensor had storage stability between 14 and 200 days.
Comparative review of the recent enzymatic methods used for selective assay of L-Lysine
Anal Biochem 2019 Nov 1;584:113335.PMID:31176610DOI:10.1016/j.ab.2019.06.006.
L-Lysine is an essential amino acid important for maintaining human health. To date, many enzymatic methods for assay of L-Lysine have been developed. The first method has been developed using L-Lysine α-oxidase (l-LysOα). However, low specificity towards L-Lysine of l-LysOα is a disadvantage inherent in this method. Recently, methods more specific to L-Lysine were developed using newly discovered enzymes such as L-Lysine ε-oxidase (l-LysOε), l-amino acid oxidase/monooxygenase (l-AAO/MOG) and L-Lysine decarboxylase/oxidase (l-Lys-DC/OD). The present paper reviews recent enzymatic methods used for assay of L-Lysine. These L-Lysine selective assays rely on detecting and quantifying hydrogen peroxide, a product generated by the oxidase reaction of these enzymes. l-LysOε catalyzes the oxidative deamination of the ε-amino group of L-Lysine, thus assays using this enzyme are more specific towards L-Lysine than the ones using l-LysOα. The l-AAO/MOG has high substrate specificity towards L-Lysine; however it exhibits L-Lysine oxidase and monooxygenase activities. The sensitivity of l-AAO/MOG method was improved either by using its mutant, which has reduced monooxygenase activity, or by coupling with an aminoamide-oxidizing enzyme. The l-Lys-DC/OD exhibits both L-Lysine decarboxylase and oxidase activities. The sensitivity of the l-Lys-DC/OD method was improved by using putrescine oxidase to oxidize the decarboxylation product of L-Lysine.
l-Arginine and L-Lysine retard aggregation and polar residue modifications of myofibrillar proteins: Their roles in solubility of myofibrillar proteins in frozen porcine Longissimus lumborum
Food Chem 2022 Nov 1;393:133347.PMID:35661602DOI:10.1016/j.foodchem.2022.133347.
This study investigated the ability of l-arginine and L-Lysine to inhibit the adverse effects of freezing on the structure and solubility of myofibrillar proteins extract (MPE) in porcine Longissimus lumborum. The results showed that freezing decreased solubility of MPE, band densities of actin and myosin heavy and light chains, fluorescence intensity, and contents of free amino group and total sulfhydryls, but increased content of carbonyl groups and absolute zeta-potential of MPE. l-Arginine and L-Lysine effectively alleviated the adverse effects of freezing. l-Arginine and L-Lysine significantly increased β-sheet content, Tmax1 and ΔH1, but decreased α-helix content and disulfide bond content in MPE. Additionally, the SDS-PAGE analysis showed that l-arginine and L-Lysine could prevent appearance of bands at about 150 kDa. Overall, this study shows that both l-arginine and L-Lysine could not only abate the aggregation and disruption of MPs, but also reduce the oxidation of their polar amino groups, which ultimately contribute to their superior solubility. The results may be interesting in meat industry.