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L-半胱氨酸
NMR and HPLC COA下载 MSDS下载 - Names：
L-Cysteine
- CAS号：
52-90-4
MDL Number： MFCD00064306 - MF(分子式)： HSCH2CH(NH2)CO2H MW(分子量)： 121.16
- EINECS:200-158-2 Reaxys Number:
- Pubchem ID: Brand:BIOFOUNT
L-半胱氨酸(L-Cysteine,52-90-4)也称为C或E920，属于称为半胱氨酸及其衍生物的有机化合物。半胱氨酸和衍生物是含有半胱氨酸或其衍生物的化合物，该化合物是由氨基或羧基上的半胱氨酸反应或由杂原子取代甘氨酸的任何氢而得到的。 L-半胱氨酸是用于预防与对乙酰氨基酚过量有关的肝损害和肾损害的药物。 L-半胱氨酸以固体，可溶（在水中）和中等酸性化合物（基于其pKa）存在。半胱氨酸在整个人体大多数组织中均已发现，并且在包括粪便，唾液，尿液和血液在内的大多数生物流体中也已发现。在细胞内，L-半胱氨酸主要位于细胞质，线粒体和髓鞘中。半胱氨酸存在于从酵母到人类的所有真核生物中。
| 货品编码 | 规格 | 纯度 | 价格 (¥) | 现价(¥) | 特价(¥) | 库存描述 | 数量 | 总计 (¥) |
|---|---|---|---|---|---|---|---|---|
| SS3295-500g | 500g | 99% | ¥ 290.00 | ¥ 290.00 | 3-5days | ¥ 0.00 | ||
| SS3295-100g | 100g | 99% | ¥ 102.00 | ¥ 102.00 | Instock | ¥ 0.00 | ||
| SS3295-25g | 25g | 99% | ¥ 58.00 | ¥ 58.00 | Instock | ¥ 0.00 |
| 中文别名 | L-半胱氨酸(CAS:52-90-4); L-beta-巯基丙氨酸; L-2-氨基-3-巯基丙酸; L-半膀胱氨基酸; L-半胱氨酸碱; L-丰胱胺酸; L-硫氢化氨基丙酸; 半胱氨酸; 一巯基氨基丙盐酸盐; L-β-硫氢代丙氨酸; (+)-2-氨基-3-巯基丙酸; L-Β-巯基丙氨酸; Α-氨基-Β-巯基丙酸; 巯基丙氨酸; L-低铁-半胱氨酸盐酸盐—水物; L-半光氨酸 L-CYSTEINE; Β-巯基-Α-氨基丙酸; L(+)-半胱氨酸/L(+)-巯基氨基丙酸 |
| 英文别名 | L-Cysteine(CAS:52-90-4);L-cysteine; cysteine; Cystein; Half-cystine;; (R)-Cysteine Thioserine; (R)-2-Amino-3-mercaptopropanoic acid; L-(+)-Cysteine; L-Cystein |
| CAS号 | 52-90-4 |
| Inchi | InChI=1S/C3H7NO2S/c4-2(1-7)3(5)6/h2,7H,1,4H2,(H,5,6)/t2-/m0/s1 |
| InchiKey | XUJNEKJLAYXESH-REOHCLBHSA-N |
| 分子式 Molecular Weight | HSCH2CH(NH2)CO2H |
| 分子量 Formula | 121.16 |
| 溶解度Solubility | Soluble in water (10 mg/ml), 1N HCl (50 mg/ml), and ethanol. |
| 性状 | 8.75 o (C=12, 2N HCL) |
| 储藏条件 Storage conditions | 充氩储存;储存温度2-8℃ |
L-半胱氨酸(L-Cysteine,52-90-4)毒理性质：
L-半胱氨酸(CAS:52-90-4;英文名:L-Cysteine;)实验注意事项：
1.使用52-90-4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52-90-4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52-90-4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52-90-4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。
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-半胱氨酸蒸汽压,L-半胱氨酸合成,L-半胱氨酸标准,L-半胱氨酸应用,L-半胱氨酸合成,L-半胱氨酸沸点,L-半胱氨酸闪点,L-半胱氨酸用途,L-半胱氨酸溶解度,L-半胱氨酸价格,L-半胱氨酸作用,L-半胱氨酸结构式,L-半胱氨酸用处
| 动物 | 测试类型 | 途径 | 实验摄入量 (标准摄入量) | 影响 | 文献来源 |
| rat | LD50 | oral | 1890 mg/kg (1890 mg/kg) | BEHAVIORAL: SOMNOLENCE (GENERAL DEPRESSED ACTIVITY); LUNGS, THORAX, OR RESPIRATION: DYSPNEA; KIDNEY, URETER, AND BLADDER: OTHER CHANGES IN URINE COMPOSITION | Agents and Actions, A Swiss Journal of Pharmacology., 4(125), 1974 [PMID:4842541] |
| rat | LD50 | intraperitoneal | 1620 mg/kg (1620 mg/kg) | BEHAVIORAL: SOMNOLENCE (GENERAL DEPRESSED ACTIVITY); BEHAVIORAL: ATAXIA; LUNGS, THORAX, OR RESPIRATION: RESPIRATORY DEPRESSION | Oyo Yakuri. Pharmacometrics., 7(1251), 1973 |
| rat | LD50 | subcutaneous | 1550 mg/kg (1550 mg/kg) | BEHAVIORAL: SOMNOLENCE (GENERAL DEPRESSED ACTIVITY); BEHAVIORAL: ATAXIA; LUNGS, THORAX, OR RESPIRATION: RESPIRATORY DEPRESSION | Oyo Yakuri. Pharmacometrics., 7(1251), 1973 |
| rat | LD50 | intravenous | 1140 mg/kg (1140 mg/kg) | Journal of the American College of Toxicology., 12(113), 1993 | |
| mouse | LD50 | oral | 660 mg/kg (660 mg/kg) | Archives of Toxicology., 41(79), 1978 [PMID:214056] | |
| mouse | LD50 | intraperitoneal | 1400 mg/kg (1400 mg/kg) | BEHAVIORAL: SOMNOLENCE (GENERAL DEPRESSED ACTIVITY); BEHAVIORAL: ATAXIA; LUNGS, THORAX, OR RESPIRATION: RESPIRATORY DEPRESSION | Oyo Yakuri. Pharmacometrics., 7(1251), 1973 |
| mouse | LD50 | subcutaneous | 1360 mg/kg (1360 mg/kg) | BEHAVIORAL: SOMNOLENCE (GENERAL DEPRESSED ACTIVITY); BEHAVIORAL: ATAXIA; LUNGS, THORAX, OR RESPIRATION: RESPIRATORY DEPRESSION | Oyo Yakuri. Pharmacometrics., 7(1251), 1973 |
| mouse | LD50 | intravenous | 1250 mg/kg (1250 mg/kg) | Yakugaku Zasshi. Journal of Pharmacy., 89(1138), 1969 [PMID:5388616] |
L-半胱氨酸(CAS:52-90-4;英文名:L-Cysteine;)实验注意事项：
1.使用52-90-4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52-90-4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52-90-4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52-90-4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。
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-半胱氨酸蒸汽压,L-半胱氨酸合成,L-半胱氨酸标准,L-半胱氨酸应用,L-半胱氨酸合成,L-半胱氨酸沸点,L-半胱氨酸闪点,L-半胱氨酸用途,L-半胱氨酸溶解度,L-半胱氨酸价格,L-半胱氨酸作用,L-半胱氨酸结构式,L-半胱氨酸用处
| 产品说明 | L-半胱氨酸(52-90-4)也称为C或E920,L-半胱氨酸属于称为半胱氨酸及其衍生物的有机化合物,L-半胱氨酸溶解度,L-半胱氨酸MSDS,L-半胱氨酸结构式详见主页. |
| Introduction | L-Cysteine(L-半胱氨酸,52-90-4), also known as C or E920, belongs to the class of organic compounds known as cysteine and derivatives. |
| Application1 | Cysteine and derivatives are compounds containing cysteine or a derivative thereof resulting from reaction of cysteine at the amino group or the carboxy group, or from the replacement of any hydrogen |
| Application2 | A non-essential amino acid. |
| Application3 | L-半胱氨酸以固体，可溶（在水中）和中等酸性化合物（基于其pKa）存在。 |
1.L-Cysteine, also known as C or E920, belongs to the class of organic compounds known as cysteine and derivatives. Cysteine and derivatives are compounds containing cysteine or a derivative thereof resulting from reaction of cysteine at the amino group or the carboxy group, or from the replacement of any hydrogen of glycine by a heteroatom. L-Cysteine is a drug which is used for the prevention of liver damage and kidney damage associated with overdoses of acetaminophen. L-Cysteine exists as a solid, soluble (in water), and a moderately acidic compound (based on its pKa). L-Cysteine has been found throughout most human tissues, and has also been detected in most biofluids, including feces, saliva, urine, and blood. Within the cell, L-cysteine is primarily located in the cytoplasm, mitochondria and myelin sheath. L-Cysteine exists in all eukaryotes, ranging from yeast to humans. L-Cysteine participates in a number of enzymatic reactions. In particular, L-Glutamic acid and L-cysteine can be converted into Gamma-glutamylcysteine; which is catalyzed by the enzyme glutamate--cysteine ligase. Furthermore, L-Cysteine and 2-ketobutyric acid can be biosynthesized from L-cystathionine; which is mediated by the enzyme cystathionine gamma-lyase. Furthermore, L-Cysteine and glycine can be biosynthesized from cysteinylglycine; which is catalyzed by the enzymes aminopeptidase N and caspase-7. Finally, L-Glutamic acid and L-cysteine can be converted into Gamma-glutamylcysteine through the action of the enzyme glutamate--cysteine ligase. In humans, L-cysteine is involved in the homocysteine degradation pathway, the glucose transporter defect (SGLT2) pathway, the cysteine metabolism pathway, and the metolazone action pathway. L-Cysteine is also involved in several metabolic disorders, some of which include the chlorothiazide action pathway, the triamterene action pathway, cystathionine Beta-synthase deficiency, and homocystinuria, cystathionine beta-synthase deficiency. L-Cysteine is a potentially toxic compound.
2.L-cysteine is an optically active form of cysteine having L-configuration. It has a role as a flour treatment agent, a human metabolite and an EC 4.3.1.3 (histidine ammonia-lyase) inhibitor. It is a serine family amino acid, a proteinogenic amino acid, a cysteine and a L-alpha-amino acid. It is a conjugate base of a L-cysteinium. It is a conjugate acid of a L-cysteinate(1-). It is an enantiomer of a D-cysteine. It is a tautomer of a L-cysteine zwitterion.
3.Cysteine is a non-essential sulfur-containing amino acid in humans, related to cystine, Cysteine is important for protein synthesis, detoxification, and diverse metabolic functions. Found in beta-keratin, the main protein in nails, skin, and hair, Cysteine is important in collagen production, as well as skin elasticity and texture. Also required in the manufacture of amino acid taurine, Cysteine is a component of the antioxidant glutathione, and plays a role in the metabolism of essential biochemicals such as coenzyme A, heparin, and biotin.
2.L-cysteine is an optically active form of cysteine having L-configuration. It has a role as a flour treatment agent, a human metabolite and an EC 4.3.1.3 (histidine ammonia-lyase) inhibitor. It is a serine family amino acid, a proteinogenic amino acid, a cysteine and a L-alpha-amino acid. It is a conjugate base of a L-cysteinium. It is a conjugate acid of a L-cysteinate(1-). It is an enantiomer of a D-cysteine. It is a tautomer of a L-cysteine zwitterion.
3.Cysteine is a non-essential sulfur-containing amino acid in humans, related to cystine, Cysteine is important for protein synthesis, detoxification, and diverse metabolic functions. Found in beta-keratin, the main protein in nails, skin, and hair, Cysteine is important in collagen production, as well as skin elasticity and texture. Also required in the manufacture of amino acid taurine, Cysteine is a component of the antioxidant glutathione, and plays a role in the metabolism of essential biochemicals such as coenzyme A, heparin, and biotin.
| 警示图 | |
| 危险性 | warning |
| 危险性警示 | Not Available |
| 安全声明 | H302 |
| 安全防护 | |
| 备注 | 避免吸入，误食以及与皮肤接触 |
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| 31400341 2019-09-25 Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids c |
| 31067004 2019-08-01 Association of p38MAPK-p53-Fas aggregation in S-allyl cysteine mediated regulation of hepatocarcinoma Environmental toxicology |
| 30242128 2018-11-16 Dynamic disulfide exchange in a crystallin protein in the human eye lens promotes cataract-associated aggregation The Journal of biological chemistry |
1.[Modification of cysteine residues for mass spectrometry-based proteomic analysis: facts and artifacts]/PMID 32116223; Biomeditsinskaia khimiia 2020 Jan; 66(1):18-29 (Review Article)/Name matches: disulfide cysteine
Abstract in English, Russian：Mass spectrometric proteomic analysis at the sample preparation stage involves the artificial reduction of disulfide bonds in proteins formed between cysteine residues. Such bonds, when preserved in their native state, complicate subsequent enzymatic hydrolysis and interpretation of the research results. To prevent the re-formation of the disulfide bonds, cysteine residues are protected by special groups, most often by alkylation. In this review, we consider the methods used to modify cysteine residues during sample preparation, as well as possible artifacts of this stage. Particularly, adverse reactions of the alkylating agents with other amino acid residues are described. The most common alkylating compound used to protect cysteine residues in mass spectrometric proteomic analysis is iodoacetamide. However, an analysis of the literature in this area indicates that this reagent causes more adverse reactions than other agents used, such as chloroacetamide and acrylamide. The latter can be recommended for wider use. In the review we also discuss the features of the cysteine residue modifications and their influence on the efficiency of the search for post-translational modifications and protein products of single nucleotide substitutions.
2.Cysteine Oxidations in Mitochondrial Membrane Proteins: The Case of VDAC Isoforms in Mammals/PMID 32582695; Frontiers in cell and developmental biology 2020; 8(?):397 (Review Article)/Name matches: disulfide cysteine
Abstract：Cysteine residues are reactive amino acids that can undergo several modifications driven by redox reagents. Mitochondria are the source of an abundant production of radical species, and it is surprising that such a large availability of highly reactive chemicals is compatible with viable and active organelles, needed for the cell functions. In this work, we review the results highlighting the modifications of cysteines in the most abundant proteins of the outer mitochondrial membrane (OMM), that is, the voltage-dependent anion selective channel (VDAC) isoforms. This interesting protein family carries several cysteines exposed to the oxidative intermembrane space (IMS). Through mass spectrometry (MS) analysis, cysteine posttranslational modifications (PTMs) were precisely determined, and it was discovered that such cysteines can be subject to several oxidization degrees, ranging from the disulfide bridge to the most oxidized, the sulfonic acid, one. The large spectra of VDAC cysteine oxidations, which is unique for OMM proteins, indicate that they have both a regulative function and a buffering capacity able to counteract excess of mitochondrial reactive oxygen species (ROS) load. The consequence of these peculiar cysteine PTMs is discussed.
3.Cysteine, glutathione and a new genetic code: biochemical adaptations of the primordial cells that spread into open water and survived biospheric oxygenation/PMID 31318686; Biological chemistry 2020 02; 401(2):213-231 (Review Article)/Name matches: glutathione cysteine
Abstract：Life most likely developed under hyperthermic and anaerobic conditions in close vicinity to a stable geochemical source of energy. Epitomizing this conception, the first cells may have arisen in submarine hydrothermal vents in the middle of a gradient established by the hot and alkaline hydrothermal fluid and the cooler and more acidic water of the ocean. To enable their escape from this energy-providing gradient layer, the early cells must have overcome a whole series of obstacles. Beyond the loss of their energy source, the early cells had to adapt to a loss of external iron-sulfur catalysis as well as to a formidable temperature drop. The developed solutions to these two problems seem to have followed the principle of maximum parsimony: Cysteine was introduced into the genetic code to anchor iron-sulfur clusters, and fatty acid unsaturation was installed to maintain lipid bilayer viscosity. Unfortunately, both solutions turned out to be detrimental when the biosphere became more oxidizing after the evolution of oxygenic photosynthesis. To render cysteine thiol groups and fatty acid unsaturation compatible with life under oxygen, numerous counter-adaptations were required including the advent of glutathione and the addition of the four latest amino acids (methionine, tyrosine, tryptophan, selenocysteine) to the genetic code. In view of the continued diversification of derived antioxidant mechanisms, it appears that modern life still struggles with the initially developed strategies to escape from its hydrothermal birthplace. Only archaea may have found a more durable solution by entirely exchanging their lipid bilayer components and rigorously restricting cysteine usage.
Abstract in English, Russian：Mass spectrometric proteomic analysis at the sample preparation stage involves the artificial reduction of disulfide bonds in proteins formed between cysteine residues. Such bonds, when preserved in their native state, complicate subsequent enzymatic hydrolysis and interpretation of the research results. To prevent the re-formation of the disulfide bonds, cysteine residues are protected by special groups, most often by alkylation. In this review, we consider the methods used to modify cysteine residues during sample preparation, as well as possible artifacts of this stage. Particularly, adverse reactions of the alkylating agents with other amino acid residues are described. The most common alkylating compound used to protect cysteine residues in mass spectrometric proteomic analysis is iodoacetamide. However, an analysis of the literature in this area indicates that this reagent causes more adverse reactions than other agents used, such as chloroacetamide and acrylamide. The latter can be recommended for wider use. In the review we also discuss the features of the cysteine residue modifications and their influence on the efficiency of the search for post-translational modifications and protein products of single nucleotide substitutions.
2.Cysteine Oxidations in Mitochondrial Membrane Proteins: The Case of VDAC Isoforms in Mammals/PMID 32582695; Frontiers in cell and developmental biology 2020; 8(?):397 (Review Article)/Name matches: disulfide cysteine
Abstract：Cysteine residues are reactive amino acids that can undergo several modifications driven by redox reagents. Mitochondria are the source of an abundant production of radical species, and it is surprising that such a large availability of highly reactive chemicals is compatible with viable and active organelles, needed for the cell functions. In this work, we review the results highlighting the modifications of cysteines in the most abundant proteins of the outer mitochondrial membrane (OMM), that is, the voltage-dependent anion selective channel (VDAC) isoforms. This interesting protein family carries several cysteines exposed to the oxidative intermembrane space (IMS). Through mass spectrometry (MS) analysis, cysteine posttranslational modifications (PTMs) were precisely determined, and it was discovered that such cysteines can be subject to several oxidization degrees, ranging from the disulfide bridge to the most oxidized, the sulfonic acid, one. The large spectra of VDAC cysteine oxidations, which is unique for OMM proteins, indicate that they have both a regulative function and a buffering capacity able to counteract excess of mitochondrial reactive oxygen species (ROS) load. The consequence of these peculiar cysteine PTMs is discussed.
3.Cysteine, glutathione and a new genetic code: biochemical adaptations of the primordial cells that spread into open water and survived biospheric oxygenation/PMID 31318686; Biological chemistry 2020 02; 401(2):213-231 (Review Article)/Name matches: glutathione cysteine
Abstract：Life most likely developed under hyperthermic and anaerobic conditions in close vicinity to a stable geochemical source of energy. Epitomizing this conception, the first cells may have arisen in submarine hydrothermal vents in the middle of a gradient established by the hot and alkaline hydrothermal fluid and the cooler and more acidic water of the ocean. To enable their escape from this energy-providing gradient layer, the early cells must have overcome a whole series of obstacles. Beyond the loss of their energy source, the early cells had to adapt to a loss of external iron-sulfur catalysis as well as to a formidable temperature drop. The developed solutions to these two problems seem to have followed the principle of maximum parsimony: Cysteine was introduced into the genetic code to anchor iron-sulfur clusters, and fatty acid unsaturation was installed to maintain lipid bilayer viscosity. Unfortunately, both solutions turned out to be detrimental when the biosphere became more oxidizing after the evolution of oxygenic photosynthesis. To render cysteine thiol groups and fatty acid unsaturation compatible with life under oxygen, numerous counter-adaptations were required including the advent of glutathione and the addition of the four latest amino acids (methionine, tyrosine, tryptophan, selenocysteine) to the genetic code. In view of the continued diversification of derived antioxidant mechanisms, it appears that modern life still struggles with the initially developed strategies to escape from its hydrothermal birthplace. Only archaea may have found a more durable solution by entirely exchanging their lipid bilayer components and rigorously restricting cysteine usage.
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