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L-赖氨酸

L-赖氨酸(56-87-1,L-Lysine)是人体生长和组织修复所必需的9种必需氨基酸之一,赖氨酸由许多食物提供,尤其是红肉,鱼和乳制品。 赖氨酸似乎对单纯疱疹病毒有活性,并以多种形式的饮食补充剂存在。 产生这种作用的机制是基于病毒对氨基酸精氨酸的需求。 赖氨酸与精氨酸竞争吸收和进入细胞。 赖氨酸通过敲除精氨酸来抑制HSV的生长。
货品编码 规格 纯度 价格 (¥) 现价(¥) 特价(¥) 库存描述 数量 总计 (¥)
SS3405-500g 500g 98% ¥ 256.00 ¥ 256.00 Instock
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¥ 0.00
SS3405-100g 100g 98% ¥ 86.00 ¥ 86.00 Instock
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¥ 0.00
SS3405-25g 25g 98% ¥ 38.00 ¥ 38.00 Instock
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中文别名 L-赖氨酸(56-87-1,L-Lysine);L-已氨酸;(S)-2,6-二氨基己酸;2,6二氨基己酸;L-(+)-赖氨酸;L-2,6-二氨基已酸,L-已氨酸,L-松氨酸;L-2,6-二氨基己酸
英文别名 L-Lysine(CAS:56-87-1);L-(+)-Lysine;h-Lys-oh;lysine acid;(S)-Lysine;Aminutrin
CAS号 56-87-1
Inchi InChI=1S/C6H14N2O2/c7-4-2-1-3-5(8)6(9)10/h5H,1-4,7-8H2,(H,9,10)/t5-/m0/s1
InchiKey KDXKERNSBIXSRK-YFKPBYRVSA-N
分子式 Molecular Weight C6H14N2O2
分子量 Formula 146.19
溶解度Solubility Soluble in water (300 g/l), and methanol (partly). Insoluble in diethyl ether, acetone, and ethanol.
性状 白色结晶粉末
储藏条件 Storage conditions 常温储存

L-赖氨酸(56-87-1,L-Lysine) 实验注意事项:
1.使用56-87-1实验前需戴好防护眼镜,穿戴防护服和口罩,佩戴手套,避免与皮肤接触。
2.使用56-87-1实验过程中如遇到有毒或者刺激性物质及有害物质产生,必要时实验操作需要手套箱内完成以免对实验人员造成伤害。
3.取样品56-87-1的移液枪头需及时更换,必要时为避免交叉污染尽可能选择滤芯吸头。
4.称量药品时选用称量纸,并无风处取药和称量以免扬撒,试剂的容器使用前务必确保干净,并消毒。
5.取药品56-87-1时尽量采用多个药勺分别使用,使用后清洗干净。
6.实验后产生的废弃物需分类存储,并交于专业生物废气物处理公司处理,以免造成环境污染。
大规格定制:定制产品请将信息发送至sales@bio-fount.com。

L-Lysine(CAS:56-87-1) Experimental considerations:
1. Wear protective glasses, protective clothing and masks, gloves, and avoid contact with the skin during the experiment.
2. The waste generated after the experiment needs to be stored separately, and handed over to a professional biological waste gas treatment company to avoid environmental pollution.

Tag:L-赖氨酸(56-87-1,L-Lysine),L-赖氨酸试剂,L-赖氨酸的作用,L-赖氨酸的纯度,L-赖氨酸的价格,L-赖氨酸的厂家,L-赖氨酸的厂家,L-赖氨酸的外观,L-赖氨酸的溶解度,L-赖氨酸的注意事项,L-赖氨酸的成分,L-赖氨酸的合成,L-赖氨酸的MSDS
产品说明 L-赖氨酸(56-87-1)是一种营养补品,包含必需氨基酸赖氨酸的生物活性L-异构体,L-赖氨酸具有潜在的抗粘膜炎活性.L-赖氨酸溶解度,L-赖氨酸MSDS详见主页.
IntroductionL-Lysine (56-87-1,L-赖氨酸) is a nutritional supplement that contains the biologically active L-isomer of the essential amino acid lysine with potential anti-mucositis activity.
Application1L-赖氨酸可促进健康的组织功能,生长和愈合,并改善免疫系统。
Application2L-赖氨酸可促进钙的吸收,这对肉碱生产和胶原蛋白形成至关重要。
Application3L-Lysine promotes calcium uptake, is essential for carnitine production and collagen formation. As collagen is essential for connective tissue maintenance, this agent may also help heal mucosal wounds
L-Lysine(CAS:56-87-1), also known as (S)-lysine or L-lysin, belongs to the class of organic compounds known as l-alpha-amino acids. These are alpha amino acids which have the L-configuration of the alpha-carbon atom. L-Lysine exists as a solid, soluble (in water), and a moderately acidic compound (based on its pKa). L-Lysine has been found throughout all human tissues, and has also been detected in most biofluids, including feces, blood, sweat, and cerebrospinal fluid. Within the cell, L-lysine is primarily located in the cytoplasm, mitochondria, nucleus and peroxisome. L-Lysine exists in all eukaryotes, ranging from yeast to humans. L-Lysine participates in a number of enzymatic reactions. In particular, L-Lysine and oxoglutaric acid can be converted into saccharopine; which is mediated by the enzyme Alpha-aminoadipic semialdehyde synthase, mitochondrial. Furthermore, L-Lysine can be converted into L-lysine through its interaction with the enzyme low affinity cationic amino acid transporter 2. Finally, L-Lysine and S-adenosylmethionine can be converted into N6, N6, N6-trimethyl-L-lysine and S-adenosylhomocysteine; which is mediated by the enzyme histone-lysine N-methyltransferase SETD7. In humans, L-lysine is involved in the biotin metabolism pathway, the lysine degradation pathway, carnitine synthesis pathway, and the pyridoxine dependency with seizures pathway. L-Lysine is also involved in several metabolic disorders, some of which include the hyperlysinemia II or saccharopinuria pathway, the saccharopinuria/hyperlysinemia II pathway, the glutaric aciduria type I pathway, and the hyperlysinemia I, familial pathway. L-Lysine has been found to be associated with several diseases known as pyruvate carboxylase deficiency, leukemia, schizophrenia, and lipoyltransferase 1 deficiency; l-lysine has also been linked to the inborn metabolic disorders including tyrosinemia I.
Dietary supplementation with l-lysine affects body weight and blood hematological and biochemical parameters in rats(Molecular Biology Reports,2018)
Green Emission of Tb-doped Mg-Al Layered Double Hydroxide Response to L-lysine(Journal of Fluorescence,2016)
Use of the guanidination reaction for determining reactive lysine, bioavailable lysine and gut endogenous lysine(Amino Acids,2015)
Dietary l-lysine supplementation altered the content of pancreatic polypeptide, enzymes involved in glutamine metabolism, and β-actin in rats(Amino Acids,2018)
Enhancement of ε-poly-l-lysine production coupled with precursor l-lysine feeding in glucose–glycerol co-fermentation by Streptomyces sp. M-Z18

1.Origin of pK
Wu X;Lee J;Brooks BR J Phys Chem B. 2017 Apr 20;121(15):3318-3330. doi: 10.1021/acs.jpcb.6b08249. Epub 2016 Oct 18.

Protein internal ionizable groups can exhibit large shifts in pK;a; values. Although the environment and interaction changes have been extensively studied both experimentally and computationally, direct calculation of pK;a; values of these internal ionizable groups in explicit water is challenging due to energy barriers in solvent interaction and in conformational transition. The virtual mixture of multiple states (VMMS) method is a new approach designed to study chemical state equilibrium. This method constructs a virtual mixture of multiple chemical states in order to sample the conformational space of all states simultaneously and to avoid crossing energy barriers related to state transition. By applying VMMS to 25 variants of staphylococcal nuclease with lysine residues at internal positions, we obtained the pK;a; values of these lysine residues and investigated the physics underlining the pK;a; shifts. Our calculation results agree reasonably well with experimental measurements, validating the VMMS method for pK;a; calculation and providing molecular details of the protonation equilibrium for protein internal ionizable groups. Based on our analyses of protein conformation relaxation, lysine side chain flexibility, water penetration, and the microenvironment, we conclude that the hydrophobicity of the microenvironment around the lysine side chain (which affects water penetration differently for different protonation states) plays an important role in the pK;a; shifts.

2.Nitrogen regulator GlnR directly controls transcription of genes encoding lysine deacetylases in Actinobacteria.
Xu Y;You D;Ye BC Microbiology. 2017 Nov;163(11):1702-1710. doi: 10.1099/mic.0.000553. Epub 2017 Oct 23.

N-Lysine acetylation is a dynamic, reversible and regulatory post-translational modification (PTM) in prokaryotes, which integrates and coordinates metabolisms responding to environmental clues. However, the molecular mechanism underlying the signalling pathway from nutrient sensing to protein acetylation remains incompletely understood in micro-organisms. Here we found that global nitrogen regulator GlnR directly controls transcription of genes encoding lysine deacetylases in Actinobacteria. Electrophoretic mobility shift assays and real-time PCR (RT-PCR) in three Actinobacteria species (Saccharopolyspora erythraea, Streptomyces coelicolor and Mycobacterium smegmatis) revealed that GlnR regulator protein is able to interact with the promoter regions of these genes and activate their transcription. Furthermore, it was demonstrated that cellular acetylation status (acetylome) is modulated by extracellular nitrogen availability. Our results present an example of the novel complete signal transduction mechanism of regulating protein deacetylation through a nutrient-sensing pleiotropic regulator in response to nutrient availability.

3.Maleimide-functionalized closo-dodecaborate albumin conjugates (MID-AC): Unique ligation at cysteine and lysine residues enables efficient boron delivery to tumor for neutron capture therapy.
Kikuchi S;Kanoh D;Sato S;Sakurai Y;Suzuki M;Nakamura H J Control Release. 2016 Sep 10;237:160-7. doi: 10.1016/j.jconrel.2016.07.017. Epub 2016 Jul 12.

Maleimide-conjugating closo-dodecaborate sodium form 5c (MID) synthesized by the nucleophilic ring-opening reaction of closo-dodecaborate-1,4-dioxane complex 2 with tetrabutylammonium (TBA) azide was found to conjugate to free SH of cysteine and lysine residues in BSA under physiological conditions, forming highly boronated BSA that showed high and selective accumulation in tumor and significant tumor growth inhibition in colon 26 tumor-bearing mice subjected to thermal neutron irradiation.

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