219552-69-9|伞菌素I|Parasin I|MFCD02261960-范德生物科技公司

伞菌素I

NMR下载 COA and HPLC MSDS下载
names：
Parasin I
CAS号：
219552-69-9
MDL Number： MFCD02261960
MF(分子式)： C82H154N34O24 MW(分子量)： 2000.31
EINECS: Reaxys Number:
Pubchem ID:16198073 Brand:BIOFOUNT

伞菌素I(Parasin I,219552-69-9)是一种由19个氨基酸残基组成的掺杂物，Parasin I源于从鲶鱼皮肤分离到的组蛋白H2A，Parasin I具有抗菌的作用。Parasin I具有可比的抗微生物活性的Parasin I定位在细胞膜上，随后渗透到外部和细胞质膜上。Parasin I及其活性类似物显示出强大的细胞质膜通透活性。与人溶菌酶融合的密码子优化的parasin I在巴斯德毕赤酵母中表达，并具有有效的抗生素活性。

货品编码	规格	纯度	价格 (¥)	现价(¥)	特价(¥)	库存描述	数量	总计 (¥)
YZM000200-500μg	500μg	>97%	¥ 682.50	¥ 682.50		1-3天	- +	¥ 0.00

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中文别名	伞菌素I(219552-69-9);H-Lys-Gly-Arg-Gly-Lys-Gln-Gly-Gly-Lys-Val-Arg-Ala-Lys-Ala-Lys-Thr-Arg-Ser-Ser-OH; L-赖氨酰-甘氨酰-L-精氨酰-甘氨酰-L-赖氨酰-L-谷氨酰胺基-甘氨酰-L-丙氨酰-L-赖氨酰-L-丙氨酰-L-赖氨酰-L-苏氨酰-L-精氨酸-L-丝氨酸-L-丝氨酸;
英文别名	Parasin I(219552-69-9); H-Lys-Gly-Arg-Gly-Lys-Gln-Gly-Gly-Lys-Val-Arg-Ala-Lys-Ala-Lys-Thr-Arg-Ser-Ser-OH; L-lysyl-glycyl-L-arginyl-glycyl-L-lysyl-L-glutaminyl-glycyl-glycyl-L-lysyl-L-valyl-L-arginyl-L-alanyl-L-lysyl-L-alanyl-L-lysyl-L-threonyl-L-arginyl-L-seryl-L-serine;
CAS号	219552-69-9
SMILES	[H]/N=C(\N)/NCCC[C@@H](C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(=O)N)C(=O)NCC(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCCN/C(=N/[H])/N)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCCN/C(=N/[H])/N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)O)NC(=O)CNC(=O)[C@H](CCCCN)N
Inchi
InchiKey	NFEQUGKCQWAGLY-UAAVROCESA-N
分子式 Formula	C82H154N34O24
分子量 Molecular Weight	2000.31
闪点 FP
熔点 Melting point	No data available
沸点 Boiling point
Polarizability极化度
密度 Density	1.5±0.1克/厘米3
蒸汽压 Vapor Pressure
溶解度Solubility
性状	Solid
储藏条件 Storage conditions	存放在阴凉干燥处

伞菌素I(Parasin I,219552-69-9)InChI:
InChI:1S/C82H154N34O24/c1-43(2)63(115-74(134)50(21-8-13-31-85)107-60(122)38-99-59(121)37-101-69(129)55(27-28-58(89)120)110-72(132)49(20-7-12-30-84)106-62(124)40-102-68(128)48(24-16-34-96-80(90)91)105-61(123)39-100-67(127)47(88)19-6-11-29-83)77(137)111-53(25-17-35-97-81(92)93)71(131)104-44(3)65(125)108-51(22-9-14-32-86)70(130)103-45(4)66(126)109-52(23-10-15-33-87)75(135)116-64(46(5)119)78(138)112-54(26-18-36-98-82(94)95)73(133)113-56(41-117)76(136)114-57(42-118)79(139)140/h43-57,63-64,117-119H,6-42,83-88H2,1-5H3,(H2,89,120)(H,99,121)(H,100,127)(H,101,129)(H,102,128)(H,103,130)(H,104,131)(H,105,123)(H,106,124)(H,107,122)(H,108,125)(H,109,126)(H,110,132)(H,111,137)(H,112,138)(H,113,133)(H,114,136)(H,115,134)(H,116,135)(H,139,140)(H4,90,91,96)(H4,92,93,97)(H4,94,95,98)/t44-,45-,46+,47-,48-,49-,50-,51-,52-,53-,54-,55-,56-,57-,63-,64-/m0/s1

伞菌素I(Parasin I,219552-69-9)实验注意事项：
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.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.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.

Tags:Parasin I试剂,Parasin I杂质,Parasin I中间体,Parasin I密度,Parasin I溶解度,Parasin I旋光度,Parasin I闪点,Parasin I熔点,Parasin I购买,Parasin I结构式,

产品说明	伞菌素I(Parasin I,219552-69-9) 是从鲶鱼皮肤中分离的19个氨基酸的组蛋白H2A衍生肽，具有抗菌活性。
Introduction	伞菌素I(Parasin I,219552-69-9)is a 19mino acid histone H2Aerived peptide isolated from the skin of the catfish, and shows antimicrobial activity.
Application1
Application2
Application3

伞菌素I(Parasin I,219552-69-9)药理学：

1、伞菌素I(Parasin I,219552-69-9)是一种由19个氨基酸残基组成的掺杂物，Parasin I源于从鲶鱼皮肤分离到的组蛋白H2A，Parasin I具有抗菌的作用。Parasin I具有可比的抗微生物活性的Parasin I定位在细胞膜上，随后渗透到外部和细胞质膜上。Parasin I及其活性类似物显示出强大的细胞质膜通透活性。与人溶菌酶融合的密码子优化的parasin I在巴斯德毕赤酵母中表达，并具有有效的抗生素活性。

2、伞菌素I从鲶鱼的皮肤中分离出的19氨基酸组蛋白H2A衍生的肽Parasin I是一种可透过细胞的阳离子抗菌剂。

3、伞菌素I具有可比的抗微生物活性的Parasin I定位在细胞膜上，随后渗透到外部和细胞质膜上。Parasin I及其活性类似物显示出强大的细胞质膜通透活性。伞菌素I与人溶菌酶融合的密码子优化的parasin I在巴斯德毕赤酵母中表达，并具有有效的抗生素活性。

警示图
危险性	warning
危险性警示	Not available
安全声明	H303吞入可能有害+H313皮肤接触可能有害+H2413吸入可能对身体有害
安全防护	P264处理后彻底清洗+P280戴防护手套/穿防护服/戴防护眼罩/戴防护面具+P305如果进入眼睛+P351用水小心冲洗几分钟+P338取出隐形眼镜（如果有）并且易于操作,继续冲洗+P337如果眼睛刺激持续+P2393获得医疗建议/护理
备注	实验过程中防止吸入、食入，做好安全防护

Koo YS, et al. Structure-activity relations of parasin I, a histone H2A-derived antimicrobial peptide. Peptides. 2008 Jul;29(7):1102-8.

Zhao H, et al. Characterization of bioactive recombinant antimicrobial peptide parasin I fused with human lysozyme expressed in the yeast Pichia pastoris system. Enzyme Microb Technol. 2015 Sep;77:61-

Parasin I, an antimicrobial peptide derived from histone H2A in the catfish, Parasilurus asotus PMID 9824303; FEBS letters 1998 Oct; 437(3):258-62 Name matches: magainin 2 parasin i

Characterization of bioactive recombinant antimicrobial peptide parasin I fused with human lysozyme expressed in the yeast Pichia pastoris system PMID 26138401; Enzyme and microbial technology 2015 Se

Slow-Release and Nontoxic Pickering Emulsion Platform for Antimicrobial Peptide PMID 32559384; Journal of agricultural and food chemistry 2020 Jul; 68(28):7453-7466 Name matches: chitosan parasin i

伞菌素I(Parasin I,219552-69-9)参考文献：

1.Characterization of bioactive recombinant antimicrobial peptide parasin I fused with human lysozyme expressed in the yeast Pichia pastoris system.
Zhao H;Tang J;Cao L;Jia G;Long D;Liu G;Chen X;Cai J;Shang H Enzyme Microb Technol. 2015 Sep;77:61-7. doi: 10.1016/j.enzmictec.2015.06.001. Epub 2015 Jun 6.

Parasin I (PI) is a 19 amino acid peptide with potent antimicrobial activities against a broad spectrum of microorganisms and is a good candidate for development as a novel antimicrobial agent. The objective of this study was to express and characterize a codon optimized parasin I peptide fused with human lysozyme (hLY). A 513 bp cDNA fragment encoding the mature hLY protein and parasin I peptide was designed and synthesized according to the codon bias of Pichia pastoris. A 4×Gly flexible amino acid linker with an enterokinase cleavage (DDDDK) was designed to link the PI to the C-terminal of hLY. The codon optimized recombinant hLY-PI was cloned into the pPICZαA vector and expressed in P. pastoris. The over-expressed extracellular rehLY-PI was purified using Ni sepharose affinity column and exhibited a molecular mass of approximately 18 kDa. After digested with enterokinase the rehLY-PI protein release its corresponding rehLY and rePI, with molecular mass of 16 kDa and 2 kDa, respectively, on Tricine-SDS-PAGE. The released rehLY exhibited similar lytical activity against Micrococcus lysodeikticus to its commercial hLY. The digested rehLY-PI product exhibited antimicrobial activities against Bacillus subtilis, Staphylococcus aureus and Escherichia coli, and synergism has been found between the released rePI and rehLY.

2.Direct expression of antimicrobial peptides in an intact form by a translationally coupled two-cistron expression system.
Jang SA;Sung BH;Cho JH;Kim SC Appl Environ Microbiol. 2009 Jun;75(12):3980-6. doi: 10.1128/AEM.02753-08. Epub 2009 Apr 10.

We describe a novel prokaryotic expression system for the production of cationic antimicrobial peptides (AMPs). The method relies on a translationally coupled two-cistron system, in which the termination codon for the first cistron (which encodes the anionic polypeptide mIFc2, a derivative of human gamma interferon) overlaps with the initiation codon for the second cistron (which encodes a cationic AMP) in the sequence of 5'-TAATG-3'. By forming an insoluble complex with the AMP upon translation, the mIFc2 protein efficiently neutralized the toxicity of the coexpressed cationic AMP and minimized the sensitivity of AMP to proteolytic degradation in a host. The AMPs were retrieved from the insoluble inclusion bodies without any chemical or enzymatic cleavage step by simple cation-exchange chromatography. With our system, approximately 100 mg of various AMPs (buforin IIb, parasin I, and pexiganan) were obtained from 1 liter of Escherichia coli culture. Our expression system may represent a universal cost-effective solution for the mass production of intact AMPs in their natural forms.

3.Structure-activity relations of parasin I, a histone H2A-derived antimicrobial peptide.
Koo YS;Kim JM;Park IY;Yu BJ;Jang SA;Kim KS;Park CB;Cho JH;Kim SC Peptides. 2008 Jul;29(7):1102-8. doi: 10.1016/j.peptides.2008.02.019. Epub 2008 Mar 7.

The structure-activity relations and mechanism of action of parasin I, a 19-amino acid histone H2A-derived antimicrobial peptide, were investigated. Parasin I formed an amphipathic alpha-helical structure (residues 9-17) flanked by two random coil regions (residues 1-8 and 18-19) in helix-promoting environments. Deletion of the lysine residue at the N-terminal [Pa(2-19)] resulted in loss of antimicrobial activity, but did not affect the alpha-helical content of the peptide. The antimicrobial activity was recovered when the lysine residue was substituted with another basic residue, arginine ([R(1)]Pa), but not with polar, neutral, or acidic residues. Progressive deletions from the C-terminal [Pa(1-17), Pa(1-15)] slightly increased the antimicrobial activity (1-4 microg/ml) without affecting the alpha-helical content of the peptide. However, further deletion [Pa(1-14)] resulted in nearly complete loss of antimicrobial activity and alpha-helical structure. Confocal microscopic analysis and membrane permeabilization assays showed that parasin I and its analogs with comparable antimicrobial activities localized to the cell membrane and subsequently permeabilized the outer and cytoplasmic membranes.

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