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傘菌素I

NMR下載 COA and HPLC MSDS下載
names：
Parasin I
CAS號：
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

傘菌素I(Parasin I,219552-69-9)是一種由19個氨基酸殘基組成的摻雜物，Parasin I源于從鯰魚皮膚分離到的組蛋白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定位在細(xì)胞膜上，隨后滲透到外部和細(xì)胞質(zhì)膜上。Parasin I及其活性類似物顯示出強大的細(xì)胞質(zhì)膜通透活性。與人溶菌酶融合的密碼子優(yōu)化的parasin I在巴斯德畢赤酵母中表達，并具有有效的抗生素活性。

貨品編碼	規(guī)格	純度	價格 (￥)	現(xiàn)價(￥)	特價(￥)	庫存描述	數(shù)量	總計 (￥)
YZM000200-500μg	500μg	>97%	￥ 682.50	￥ 682.50		1-3天	- +	￥ 0.00

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中文別名	傘菌素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-賴氨酰-甘氨酰-L-精氨酰-甘氨酰-L-賴氨酰-L-谷氨酰胺基-甘氨酰-L-丙氨酰-L-賴氨酰-L-丙氨酰-L-賴氨酰-L-蘇氨酰-L-精氨酸-L-絲氨酸-L-絲氨酸;
英文別名	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號	219552-69-9
Inchi
InchiKey	NFEQUGKCQWAGLY-UAAVROCESA-N
分子式 Formula	C82H154N34O24
分子量 Molecular Weight	2000.31
溶解度Solubility
性狀	Solid
儲藏條件 Storage conditions	存放在陰涼干燥處

傘菌素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

傘菌素I(Parasin I,219552-69-9)實驗注意事項：
1.實驗前需戴好防護眼鏡，穿戴防護服和口罩，佩戴手套，避免與皮膚接觸。
2.實驗過程中如遇到有毒或者刺激性物質(zhì)及有害物質(zhì)產(chǎn)生，必要時實驗操作需要手套箱內(nèi)完成以免對實驗人員造成傷害
3.實驗后產(chǎn)生的廢棄物需分類存儲，并交于專業(yè)生物廢氣物處理公司處理，以免造成環(huán)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試劑,Parasin I雜質(zhì),Parasin I中間體,Parasin I密度,Parasin I溶解度,Parasin I旋光度,Parasin I閃點,Parasin I熔點,Parasin I購買,Parasin I結(jié)構(gòu)式,

產(chǎn)品說明	傘菌素I(Parasin I,219552-69-9) 是從鯰魚皮膚中分離的19個氨基酸的組蛋白H2A衍生肽，具有抗菌活性。
Introduction	傘菌素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

傘菌素I(Parasin I,219552-69-9)藥理學(xué)：

1、傘菌素I(Parasin I,219552-69-9)是一種由19個氨基酸殘基組成的摻雜物，Parasin I源于從鯰魚皮膚分離到的組蛋白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定位在細(xì)胞膜上，隨后滲透到外部和細(xì)胞質(zhì)膜上。Parasin I及其活性類似物顯示出強大的細(xì)胞質(zhì)膜通透活性。與人溶菌酶融合的密碼子優(yōu)化的parasin I在巴斯德畢赤酵母中表達，并具有有效的抗生素活性。

2、傘菌素I從鯰魚的皮膚中分離出的19氨基酸組蛋白H2A衍生的肽Parasin I是一種可透過細(xì)胞的陽離子抗菌劑。

3、傘菌素I具有可比的抗微生物活性的Parasin I定位在細(xì)胞膜上，隨后滲透到外部和細(xì)胞質(zhì)膜上。Parasin I及其活性類似物顯示出強大的細(xì)胞質(zhì)膜通透活性。傘菌素I與人溶菌酶融合的密碼子優(yōu)化的parasin I在巴斯德畢赤酵母中表達，并具有有效的抗生素活性。

警示圖
危險性	warning
危險性警示	Not available
安全聲明	H303吞入可能有害+H313皮膚接觸可能有害+H2413吸入可能對身體有害
安全防護	P264處理后徹底清洗+P280戴防護手套/穿防護服/戴防護眼罩/戴防護面具+P305如果進入眼睛+P351用水小心沖洗幾分鐘+P338取出隱形眼鏡（如果有）并且易于操作,繼續(xù)沖洗+P337如果眼睛刺激持續(xù)+P2393獲得醫(yī)療建議/護理
備注	實驗過程中防止吸入、食入，做好安全防護

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

傘菌素I(Parasin I,219552-69-9)參考文獻：

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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