私たちは、シアノバクテリア菌株を提供するために大学自治・デ・マドリードから博士アントニオ・ケサダに感謝します。この作品は、スペイン語MINISTERIOデエコノミアのy Competitividad（MINECO）のSubdirección一般デProyectosデInvestigaciónによって資金を供給された、無許可します。 AYA2011-24803とESP2014-58494-R。

<ol>
	<li>Simis, S. G. H., Peters, S. W. M., Gons, H. J. <a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Search&doptcmdl=Citation&defaultField=Title+Word&term=Remote+sensing+of+the+cyanobacterial+pigment+phycocianin+in+turbid+inland+water.">Remote sensing of the cyanobacterial pigment phycocianin in turbid inland water.</a> Limnol. Oceanogr. 50 (1), 237-245 (2005).</li><li>Zamyadi, A., McQuaid, N., Prevost, M., Dorner, S. <a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Search&doptcmdl=Citation&defaultField=Title+Word&term=Monitoring+of+potentially+toxic+cyanobacteria+using+an+online+multi-probe+in+drinking+water+sources.">Monitoring of potentially toxic cyanobacteria using an online multi-probe in drinking water sources.</a> J. Environ. Monit. 14, 579-588 (2012).</li><li>Msagati, T. A. M., Siame, B. A., Shushu, D. D. <a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Search&doptcmdl=Citation&defaultField=Title+Word&term=Evaluation+of+methods+for+the+isolation,+detection+and+quantification+of+cyanobacterial+hepatotoxins.">Evaluation of methods for the isolation, detection and quantification of cyanobacterial hepatotoxins.</a> Aquat. Toxicol. 78 (4), 382-397 (2006).</li><li>Weller, M. G. <a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Search&doptcmdl=Citation&defaultField=Title+Word&term=Immunoassays+and+biosensors+for+the+detection+of+cyanobacterial+toxins+in+water.">Immunoassays and biosensors for the detection of cyanobacterial toxins in water.</a> Sensors. 13 (11), 15085-15112 (2013).</li><li>Baker, J. A., Neilan, B. A., Entsch, B., McKay, D. B. <a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Search&doptcmdl=Citation&defaultField=Title+Word&term=Identification+of+cyanobacteria+and+their+toxigenicity+in+environmental+samples+by+rapid+molecular+analysis.">Identification of cyanobacteria and their toxigenicity in environmental samples by rapid molecular analysis.</a> Environ. Toxicol. 16 (6), 472-482 (2001).</li><li>Li, H., Singh, A. K., McIntyre, L. M., Sherman, L. A. <a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Search&doptcmdl=Citation&defaultField=Title+Word&term=Differential+gene+expression+in+response+to+hydrogen+peroxide+and+the+putative+PerR+regulon+of+Synechocystis+sp.+Strain+PCC+6803.">Differential gene expression in response to hydrogen peroxide and the putative PerR regulon of Synechocystis sp. Strain PCC 6803.</a> J. Bacteriol. 186 (11), 3331-3345 (2004).</li><li>Anderson, D. M., Cembella, A. D., Hallegraeff, G. M. <a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Search&doptcmdl=Citation&defaultField=Title+Word&term=Progress+in+understanding+harmful+algal+blooms:+paradigm+shifts+and+new+technologies+for+research,+monitoring,+and+management.">Progress in understanding harmful algal blooms: paradigm shifts and new technologies for research, monitoring, and management.</a> Ann. Rev. Mar. Sci. 4, 143-176 (2012).</li><li>Dittami, S. M., Pazos, Y., Laspra, M., Medlin, L. K. <a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Search&doptcmdl=Citation&defaultField=Title+Word&term=Microarray+testing+for+the+presence+of+toxic+algae+monitoring+programme+in+Galicia+(NW+Spain).">Microarray testing for the presence of toxic algae monitoring programme in Galicia (NW Spain).</a> Environ. Sci. Pollut. Res. Int. 20, 6778-6793 (2013).</li><li>Kegel, J. U., Del Amo, ., Medlin, Y., K, L. <a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Search&doptcmdl=Citation&defaultField=Title+Word&term=Introduction+to+Project+MIDTAL:+its+methods+and+samples+from+Arcachon+Bay,+France.">Introduction to Project MIDTAL: its methods and samples from Arcachon Bay, France.</a> Environ. Sci. Pollut. Res. Int. 20 (10), 6690-6704 (2013).</li><li>Marcheggiani, S., et al. <a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Search&doptcmdl=Citation&defaultField=Title+Word&term=Detection+of+emerging+and+re-emerging+pathogens+in+surface+waters+close+to+an+urban+area.">Detection of emerging and re-emerging pathogens in surface waters close to an urban area.</a> Int. J. Environ. Res. Public Health. 12 (5), 5505-5527 (2015).</li><li>Fern&#225;ndez-Calvo, P., N&#228;ke, C., Rivas, L. A., Garc&#237;a-Villadangos, M., G&#243;mez-Elvira, J., Parro, V. <a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Search&doptcmdl=Citation&defaultField=Title+Word&term=A+multi-array+competitive+immunoassay+for+the+detection+of+broad-range+molecular+size+organic+compounds+relevant+for+astrobiology.">A multi-array competitive immunoassay for the detection of broad-range molecular size organic compounds relevant for astrobiology.</a> Planet. Space Sci. 54 (815), 1612-1621 (2006).</li><li>Parro, V. <a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Search&doptcmdl=Citation&defaultField=Title+Word&term=.">.</a> Antibody microarrays for environmental monitoring. Handbook of Hydrocarbon and Lipid Microbiology. , 2699-2710 (2010).</li><li>Fan, Z., Keum, Y. S., Li, Q. X., Shelver, W. L., Guo, L. H. <a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Search&doptcmdl=Citation&defaultField=Title+Word&term=Sensitive+immunoassay+detection+of+multiple+environmental+chemicals+on+protein+microarrays+using+DNA/dye+conjugate+as+a+fluorescent+label.">Sensitive immunoassay detection of multiple environmental chemicals on protein microarrays using DNA/dye conjugate as a fluorescent label.</a> J. Environ. Monit. 14 (5), 1345-1352 (2012).</li><li>Rivas, L. A., Garc&#237;a-Villadangos, M., Moreno-Paz, M., Patricia Cruz-Gil, P., G&#243;mez-Elvira, J., Parro, V. <a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Search&doptcmdl=Citation&defaultField=Title+Word&term=A+200-Antibody+microarray+biochip+for+environmental+monitoring:+Searching+for+universal+microbial+biomarkers+through+immunoprofiling.">A 200-Antibody microarray biochip for environmental monitoring: Searching for universal microbial biomarkers through immunoprofiling.</a> Anal. Chem. 80 (21), 7970-7979 (2008).</li><li>Delehanty, J. B., Ligler, F. S. <a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Search&doptcmdl=Citation&defaultField=Title+Word&term=A+microarray+immunoassay+for+simultaneous+detection+of+proteins+and+bacteria.">A microarray immunoassay for simultaneous detection of proteins and bacteria.</a> Anal. Chem. 74 (21), 5681-5687 (2002).</li><li>Ligler, F. S., Taitt, C. R., Shriver-Lake, L. C., Sapsford, K. E., Shubin, Y., Golden, J. P. <a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Search&doptcmdl=Citation&defaultField=Title+Word&term=Array+biosensor+for+detection+of+toxins.">Array biosensor for detection of toxins.</a> Anal. Bioanal. Chem. 377 (3), 469-477 (2003).</li><li>Rucker, V. C., Havenstrite, K. L., Herr, A. E. <a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Search&doptcmdl=Citation&defaultField=Title+Word&term=Antibody+microarrays+for+native+toxin+detection.">Antibody microarrays for native toxin detection.</a> Anal. Biochem. 339 (2), 262-270 (2005).</li><li>Kang, J., Kim, S., Kwon, Y. <a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Search&doptcmdl=Citation&defaultField=Title+Word&term=Antibody-based+biosensors+for+environmental+monitoring.">Antibody-based biosensors for environmental monitoring.</a> Toxicol. Environ. Health. Sci. 1 (3), 145-150 (2009).</li><li>Herranz, S., Marazuela, M. D., Moreno-Bondi, M. C. <a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Search&doptcmdl=Citation&defaultField=Title+Word&term=Automated+portable+array+biosensor+for+multisample+microcystin+analysis+in+freshwater+samples.">Automated portable array biosensor for multisample microcystin analysis in freshwater samples.</a> Biosens. Bioelectron. 33 (1), 50-55 (2012).</li><li>Shlyapnikov, Y., et al. <a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Search&doptcmdl=Citation&defaultField=Title+Word&term=Rapid+simultaneous+ultrasensitive+immunodetection+of+five+bacterial+toxins.">Rapid simultaneous ultrasensitive immunodetection of five bacterial toxins.</a> Anal. Chem. 84 (13), 5596-5603 (2012).</li><li>Szkola, A., et al. <a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Search&doptcmdl=Citation&defaultField=Title+Word&term=Rapid+and+simultaneous+detection+of+ricin,+staphylococcal+enterotoxin+B+and+saxitoxin+by+chemiluminescence-based+microarray+immunoassay.">Rapid and simultaneous detection of ricin, staphylococcal enterotoxin B and saxitoxin by chemiluminescence-based microarray immunoassay.</a> Analyst. 139, 5885-5892 (2014).</li><li>Blanco, Y., Quesada, A., Gallardo-Carre&#241;o, I., Jacobo Aguirre, ., Parro, J., V, <a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Search&doptcmdl=Citation&defaultField=Title+Word&term=CYANOCHIP:+An+antibody+microarray+for+high-taxonomical-resolution+cyanobacterial+monitoring.">CYANOCHIP: An antibody microarray for high-taxonomical-resolution cyanobacterial monitoring.</a> Environ. Sci. Technol. 49 (3), 1611-1620 (2015).</li><li>Bradford, M. M. <a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Search&doptcmdl=Citation&defaultField=Title+Word&term=A+Rapid+and+Sensitive+Method+for+the+Quantitation+of+Microgram+Quantities+of+Protein+Utilizing+the+Principle+of+Protein-Dye+Binding.">A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye Binding.</a> Anal. Chem. 72, 248-254 (1976).</li><li>Lowry, O. H., Rosebrough, N. J., Farr, A. L., Randall, R. J. <a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Search&doptcmdl=Citation&defaultField=Title+Word&term=Protein+measurement+with+the+Folin+phenol+reagent.">Protein measurement with the Folin phenol reagent.</a> J. Biol. Chem. 193 (1), 265-275 (1951).</li><li>Smith, P. K., et al. <a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Search&doptcmdl=Citation&defaultField=Title+Word&term=Measurement+of+protein+using+Bicinchoninic+acid.">Measurement of protein using Bicinchoninic acid.</a> Anal. Biochem. 150 (1), 76-85 (1985).</li><li>Rivas, L. A., Aguirre, J., Blanco, Y., Gonz&#225;lez-Toril, E., Parro, V. <a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Search&doptcmdl=Citation&defaultField=Title+Word&term=Graph-based+deconvolution+analysis+of+multiplex+sandwich+microarray+immunoassays:+applications+for+environmental+monitoring.">Graph-based deconvolution analysis of multiplex sandwich microarray immunoassays: applications for environmental monitoring.</a> Environ. Microbiol. 13 (6), 1421-1432 (2011).</li><li>Blanco, Y., et al. <a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Search&doptcmdl=Citation&defaultField=Title+Word&term=Deciphering+the+prokaryotic+community+and+metabolisms+in+south+african+deep-mine+biofilms+through+antibody+microarrays+and+graph+theory.">Deciphering the prokaryotic community and metabolisms in south african deep-mine biofilms through antibody microarrays and graph theory.</a> PloS One. 9 (2), e114180 (2014).</li><li>Gas, F., Baus, B., Quer&#233;, J., Chapelle, A., Dreanno, C. <a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Search&doptcmdl=Citation&defaultField=Title+Word&term=Rapid+detection+and+quantification+of+the+marine+toxic+algae,+Alexandrium+minutum,+using+a+super-paramagnetic+immunochromatographic+strip+test.">Rapid detection and quantification of the marine toxic algae, Alexandrium minutum, using a super-paramagnetic immunochromatographic strip test.</a> Talanta. 147, 581-589 (2016).</li><li>Parro, V., et al. <a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Search&doptcmdl=Citation&defaultField=Title+Word&term=SOLID3:+a+multiplex+antibody+microarray-based+optical+sensor+instrument+for+in+situ+life+detection+in+planetary+exploration.">SOLID3: a multiplex antibody microarray-based optical sensor instrument for in situ life detection in planetary exploration.</a> Astrobiology. 11, 15-28 (2011).</li><li>McKay, C. P., et al. <a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Search&doptcmdl=Citation&defaultField=Title+Word&term=The+Icebreaker+Life+Mission+to+Mars:+a+search+for+biomolecular+evidence+for+life.">The Icebreaker Life Mission to Mars: a search for biomolecular evidence for life.</a> Astrobiology. 13, 334-353 (2013).</li></ol>

The authors have nothing to disclose.

ここでは、CYANOCHIP、シアノバクテリア属の広い範囲の検出および同定のための17-抗体マイクロアレイを用いて、多重蛍光サンドイッチ免疫測定法は、22に記載されています。これらのシアノバクテリアは、そのうちのいくつかは毒素生産され、淡水生息地の中で最も頻繁に底生やプランクトンの属を表します。最近、蛍光サンドイッチイムノアッセ?...

複雑な自然の微生物群集中の微生物の検出と監視は生物医学、環境、エコロジー、そして宇宙生物学などの多くの分野で重要です。淡水中の細胞の花（過剰増殖）を形成する能力についてよく知られている原核微生物はシアノバクテリアです。彼らは遍在している、と多くの種は、ヒトの健康に対する潜在的なリスクに、だけでなく、生態系への影響のみならず大手、毒素を産生することができます。この点では、 シアノバクテリアおよび/または土壌及び水中のそれらの毒素の早期検出のための迅速かつ高感度な方法を開発することが不可欠です。水管理者が適切な水管理プログラムを実施する際に、結果的に、決定にそれらを助けるために、この目的のために、多重蛍光サンドイッチマイクロアレイイムノアッセイ（FSMI）のツールとして開発されました。 方法の多様な範囲は、シアンを検出および同定するために開発されています光学顕微鏡、分子生物学、および免疫学的技術を含む土壌や水にobacterial細胞およびシアノトキシン、。これらの方法は、それらが提供する情報に大きく異なります。顕微鏡技術は、細胞の形態や、フィコシアニンやクロロフィル1とシアノバクテリア顔料、からの生体内蛍光の検出に基づいています。彼らは、試料中に存在するシアノバクテリアの種類と数をお知らせリアルタイムおよび頻繁なモニタリングのための迅速かつ安価な方法であるが、それらは潜在的な毒性に関する情報を与えることはありません。さらに、彼らは、しばしば密接に関連した種2を区別することは非常に困難であることを考慮して、専門知識の特定のレベルを必要とします。これらの制限を克服するために、光学顕微鏡は、生物学的および生化学的スクリーニングアッセイおよびシアノトキシンの同定および定量のための物理化学的方法の両方を添付しなければなりません。 <pクラス= &quot;jove_content&quot;&gt;酵素結合免疫吸着検定法（ELISA）、タンパク質リン阻害アッセイ（PPIA）、およびマウスにおける神経化学的試験は、シアノトキシンを検出するための生化学的スクリーニングアッセイの例です。最初の二つは、迅速かつ高感度な方法論であるが、使用してELISAおよびPPIAテストは毒素の3種類に制限されている場合、偽陽性が記載されています。マウスバイオアッセイは、低感度および精度の質的な技術であり、特別なライセンスやトレーニングが必要です。また、試料中に存在する毒素の種類についての情報を与えません。シアノトキシン例えば、高速液体クロマトグラフィー（HPLC）などの他の分析方法によって同定及び定量することができる、液体クロマトグラフィー - 質量分析（LC-MS）、ガスクロマトグラフィー（GC）、ガスクロマトグラフィー - 質量分析（GC-MS）またはマトリックス支援レーザー脱離/イオン化飛行時間（MALDI-TOF）。参照標準、必要とされる場合は、これが唯一の可能性であります複雑なサンプル中の個々の毒素濃度を決定するためのedは、3、4ご利用いただけます。また、これらの方法は時間がかかります。高価な機器、消耗品、およびサンプル調製を必要とします。そして、経験豊富な専門スタッフによって行われなければなりません。 分子ベースの方法は、ゲノムデータベースに公開された配列情報のおかげで、検出、同定、およびシアノバクテリアとそれらに対応するシアノトキシンを定量化するために数十年にわたって適用されている（ 例えば、バイオテクノロジー情報、NCBIのための国立センター）。これらの方法の中でDNAの増幅のためのプライマーセットの設計を必要とし、別のシアノバクテリア種のDNA配列の予備知識に依存してポリメラーゼ連鎖反応（PCR）に基づくものです。遺伝子の検出は、フィコシアニンオペロンのように、属レベルでの正確な同定をもたらす一方で、一部の種や菌株がで検出されませんこの方法。しかしながら、このようなミクロオペロンに属するものとして毒素をコードする遺伝子は、プロデューサ5不足しているサンプル中の毒素の同定を容易にします。それにもかかわらず、PCRによる毒素マーカーの検出は、必ずしも環境に毒性を示すものではありません。また、 シアノバクテリアの種と試料中に存在する毒素生産の全範囲を分析するために開発されたプライマーのセットは、まだ不完全であり、更なる研究は、未知の種を同定するために行われなければなりません。他の分子技術は、 蛍光in situハイブリダイゼーション（FISH）およびDNAマイクロアレイなどの非PCRベースです。 過去20年間では、マイクロアレイ技術は、特に環境モニタリングでは、アプリケーションの多くの分野で重要性を増しています。 DNAマイクロアレイは、種との検体4の間の識別、6、7を可能に</SUP&gt;、8、9、10、それらは非常に面倒で時間がかかる複数のステップ（ 例えば、マイクロアレイの性能、DNA抽出、PCR増幅、およびハイブリダイゼーション）を伴う作業を考えています。そのため、例えば、サンドイッチおよび競合免疫学的マイクロアレイのような抗体に基づいてより少ない時間のかかるアッセイは、多数の環境の分析物11、12、13の検出のために不可欠で信頼性の高いハイスループット法となっています。抗体の能力は、特に、それらの標的化合物を認識し、ほとんどすべての物質に対する抗体を産生する可能性とともに、検体およびタンパク質の少量を検出するために、抗体マイクロアレイを環境目的のための強力な技術を作ります。また、複数を達成する能力は、として分析しますイングルアッセイは、ppmのppbの範囲の検出限界で、この方法14の主な利点の1つです。 抗体ベースのバイオセンサーは、環境モニタリング15、16、17、18、19、20、21中の病原体および毒素の広い範囲を検出するための高感度かつ迅速なツールであることが判明しています。 DNA法は、いくつかのステップを含むが、抗体ベースのマイクロアレイは、主に適切なソリューションバッファ内の短い溶解段階に基づいて、小さなサンプル調製を必要とします。 DelehantyとLigler 15 4 PPBのANのタンパク質濃度を検出することができる抗体サンドイッチ免疫測定法に基づいて、複雑な混合物中のタンパク質および細菌分析物の同時検出を報告しD 10細胞の4 CFU / mLです。 Szkola ら。 21は生物兵器に使用されるかもしれないproteotoxinsと小さな毒素、化合物の同時検出のための安価で信頼性の高いマルチプレックスマイクロアレイを開発しました。彼らは20分未満で、3 ppbでの検出限界で、リシン毒素の濃度を検出しました。最近、CYANOCHIP、毒性および非毒性のシアノバクテリアのin situ検出のための抗体マイクロアレイベースのバイオセンサーは、22に記載されています。このマイクロアレイは、主に顕微鏡的に識別することが困難である水生環境で、潜在的なシアノバクテリアブルームの同定を可能にします。でも、種レベルで、多重検出およびシアノバクテリアの同定のための費用対効果の高いツールにこのバイオセンサーを回すほとんどの種のために10 3細胞、 -マイクロアレイの検出限界は10 2です。これらのプロパティはすべてantiboを作りますDYマイクロアレイ技術、およびこの仕事で提示特に方法、前述の技術に比べて迅速かつ簡単な方法。 この作品は、土壌と水のサンプル中のシアノバクテリアの存在を検出するために抗体マイクロアレイベースのバイオセンサーを使用した実験の2つの例を示します。これは、非常に少量の試料と非常に基本的なサンプル調製を必要とするサンドイッチイムノアッセイフォーマットに基づいて簡単かつ信頼できる方法です。この方法は、短い時間を必要とし、容易フィールドで行うことができます。

<table><tbody><tr><td>0.22 mm pore diameter filters</td><td>Millipore</td><td>GSWP04700</td><td>For preparation of immunogens</td></tr><tr><td>Eppendorf&amp;nbsp; 5424R microcentrifuge</td><td>Fisher Scientific</td><td></td><td>For preparation of immunogens</td></tr><tr><td>Phosphate buffer saline (PBS) pH 7.4 (10x)</td><td>Thermo Fisher Scientific</td><td>70011036</td><td>50 mM potassium phosphate, 150 mM NaCl, pH 7.4</td></tr><tr><td>Ultrasonic processor UP50H</td><td>Hielscher</td><td></td><td>For preparation of immunogens</td></tr><tr><td>Complete Freund&#039;s adjuvant&amp;nbsp;</td><td>Sigma-Aldrich</td><td>F5881</td><td>Immunopotentiator</td></tr><tr><td>Incomplete Freud&#039;s adjuvant</td><td>Sigma-Aldrich&amp;nbsp;</td><td>F5506</td><td>For boost injections</td></tr><tr><td>Protein A antibody purification kit&amp;nbsp;&amp;nbsp;</td><td>Sigma-Aldrich</td><td>PURE1A&amp;nbsp;</td><td>For isolation of IgG</td></tr><tr><td>Centrifugal filter devices MWCO&amp;lt;100 kDa</td><td>Millipore</td><td>UFC510096-96K</td><td>For isolation of IgG</td></tr><tr><td>Dialysis tubings, benzoylated</td><td>Sigma-Aldrich</td><td>D7884-10FT</td><td>For isolation of IgG</td></tr><tr><td>Illustra Microspin G-50 columns&amp;nbsp;</td><td>GE-HealthCare</td><td>GE27-5330-02</td><td>For isolation of IgG</td></tr><tr><td>Bradford reagent</td><td>Sigma-Aldrich</td><td>B6916-500 mL</td><td>To quantify the antibody concentration</td></tr><tr><td>MicroBCA protein assay kit&amp;nbsp;</td><td>Thermo Scientific</td><td>23235</td><td>To quantify the antibody concentration</td></tr><tr><td>Protein arraying buffer 2x</td><td>Whatman (Sigma Aldrich)&amp;nbsp;</td><td>S00537</td><td>Printing buffer; 30 - 40% glycerol in 1x PBS with 0.01% Tween 20</td></tr><tr><td>Tween 20&amp;nbsp;</td><td>Sigma-Aldrich&amp;nbsp;</td><td>P9416</td><td>Non-ionic detergent</td></tr><tr><td>Bovine serum albumin (BSA)</td><td>Sigma-Aldrich&amp;nbsp;</td><td>A9418</td><td>Control&amp;nbsp; for printing; blocking reagent</td></tr><tr><td>384-wells microplate</td><td>Genetix</td><td>X6004</td><td>For antibody printing</td></tr><tr><td>Robot arrayer for multiple slides</td><td>MicroGrid II TAS arrayer from Digilab</td><td></td><td>For antibody printing</td></tr><tr><td>Epoxy substrate glass slides</td><td>Arrayit corporation</td><td>VEPO25C</td><td>Solid support for antibody printing</td></tr><tr><td>Alexa Fluor-647 Succinimidyl-ester&amp;nbsp;</td><td>Molecular probes</td><td>A20006</td><td>Fluorochrome</td></tr><tr><td>DMSO&amp;nbsp;</td><td>Sigma-Aldrich&amp;nbsp;</td><td>D8418</td><td>Fluorochrome dissolvent</td></tr><tr><td>Heidolph Titramax vibrating platform shaker</td><td>Fisher Scientific</td><td></td><td>For antibody labeling&amp;nbsp;</td></tr><tr><td>Illustra Microspin G-50 columns&amp;nbsp;</td><td>Healthcare</td><td>27-5330-01</td><td>For purification of labeled antibodies</td></tr><tr><td>Safe seal brown 0.5 mL tubes</td><td>Sarstedt</td><td>72,704,001</td><td>For labeled antibodies storage&amp;nbsp;</td></tr><tr><td>Nanodrop 1000 spectrophotometer</td><td>Thermo Scientific</td><td></td><td>To quantify antibody concentration and labeling efficiency</td></tr><tr><td>3 &amp;micro;m pore size polycarbonate 47 mm diameter filter</td><td>Millipore</td><td>TMTP04700</td><td>To concentrate cells</td></tr><tr><td>1 M Trizma hydrochloride solution pH 8</td><td>Sigma-Aldrich&amp;nbsp;</td><td>T3038</td><td>For TBSTRR preparation; to block slides</td></tr><tr><td>Sodium chloride</td><td>Sigma-Aldrich&amp;nbsp;</td><td>S7653</td><td>For TBSTRR preparation</td></tr><tr><td>20 &amp;micro;m nylon filters&amp;nbsp;</td><td>Millipore</td><td>NY2004700</td><td>For environmental extract preparation</td></tr><tr><td>10 - 12 mm filter holders</td><td>Millipore</td><td>SX0001300</td><td>For environmental extract preparation</td></tr><tr><td>Protease inhibitor cocktail</td><td>Sigma-Aldrich&amp;nbsp;</td><td>P8340</td><td>For environmental extract storage</td></tr><tr><td>1 M Trizma hydrochloride solution pH 9</td><td>Sigma-Aldrich&amp;nbsp;</td><td>T2819</td><td>To block slides</td></tr><tr><td>Heidolph Duomax 1030 rocking platform shaker</td><td>VWR</td><td></td><td>To block slides; for incubation processes&amp;nbsp;</td></tr><tr><td>VWR Galaxy miniarray microcentrifuge</td><td>VWR</td><td>C1403-VWR</td><td>To dry slides</td></tr><tr><td>Multi-Well microarray hybridization cassette</td><td>Arrayit corporation</td><td>AHC1X24</td><td>Cassette for 24 assays per slide</td></tr><tr><td>GenePix 4100A microarray scanner&amp;nbsp;</td><td>Molecular Devices</td><td></td><td>Scanner for fluorescence</td></tr><tr><td>GenePix Pro Software</td><td>Molecular Devices</td><td></td><td>Software for image analysis and quantification</td></tr></tbody></table>

experimental protocol for detecting cyanobacteria in liquid and solid samples with an antibody microarray chip

地球温暖化や富栄養化は、いくつかの水生生態系が急速かつ大規模なシアノバクテリアの成長をトリガとして、真のバイオリアクターを動作させます。これは、関連する健康と経済的な影響を持っています。多くのシアノバクテリア菌株は毒素生産者である、とだけ少数の細胞は、環境に取り返しのつかない損傷を誘発するために必要です。したがって、水体当局との投与は、それらの予防的もしくは治療的な意思決定をサポートするために信頼できるデータを提供する迅速かつ効率的な早期警報システムを必要とします。この原稿は、分類学上の解像度（CYANOCHIP）で17抗体（ABS）を有する抗体マイクロアレイチップを使用して、毒素産生シアノバクテリア株のインフィールド検出のための実験プロトコルを報告します。ここでは、17シアノバクテリア株の同時モニタリングのための多重蛍光サンドイッチマイクロアレイイムノアッセイ（FSMI）が頻繁に淡水生態系に咲く発見、それらのいくつかの毒素生産者は、記載されています。マルチでのマイクロアレイPLE CYANOCHIPの（24まで）同一の複製を同時にサンプルの同様の数をテストするために、単一の顕微鏡スライド上に印刷しました。液体試料は、1〜3ミクロンのフィルターを通して濾過することにより、抗体との直接的インキュベーション（ABS）または細胞濃度後のいずれかで試験することができます。そのような堆積物とグランド石のような固体サンプルを、最初のインキュベーション緩衝液中のハンドヘルド超音波処理によって均質化し、分散しています。粗物質を除去し、ろ液をABSでインキュベートする - それらは、次いで、（20ミクロン5）濾過します。免疫反応は、17蛍光標識Abの混合物で最終インキュベーションによって明らかにされており、可搬型蛍光検出器によって読み取られます。全体のプロセスは、そのほとんどが、インキュベーションの2 1時間の期間に対応し、約3時間かかります。出力は、明るいスポットは、シアノバクテリアマーカーの陽性検出に対応した画像です。

この作品はCYANOCHIP抗体マイクロアレイを用いて、最も関連性の高い淡水シアノバクテリア種の同時同定（ 表1）のためのマルチプレックスイムノアッセイテストを説明します。マイクロアレイは、顕微鏡スライド上に印刷された3×8マイクロアレイフォーマットすることができます。各マイクロアレイは、陰性対照としてトリプリケートスポットパターン?...

Watch this Scientific Journal Video about Experimental Protocol for Detecting Cyanobacteria in Liquid and Solid Samples with an Antibody Microarray Chip at JoVE.com

Experimental Protocol for Detecting Cyanobacteria in Liquid and Solid Samples with an Antibody Microarray Chip

The presence of cyanobacterial toxins in fresh water reservoirs for human consumption is a major concern for water management authorities. To evaluate the risk of water contamination, this article describes an protocol for the in-field detection of cyanobacterial strains in liquid and solid samples by using an antibody microarray chip.

検出するための実験プロトコール<em&gt;シアノバクテリア</em&gt;抗体マイクロアレイチップと液体と固体試料中の

Global warming and eutrophication make some aquatic ecosystems behave as true bioreactors that trigger rapid and massive cyanobacterial growth; this has ...

experimental-protocol-for-detecting-cyanobacteria-liquid-solid

Research

JoVE Journal

Environment

Experimental Protocol for Detecting Cyanobacteria in Liquid and Solid Samples with an Antibody Microarray Chip

9.1K ビュー.  Centro de Astrobiología (CAB, INTA-CSIC). The presence of cyanobacterial toxins in fresh water reservoirs for human consumption is a major concern for water management authorities. To evaluate the risk of water contamination, this article describes an protocol for the in-field detection of cyanobacterial strains in liquid and solid samples by using an antibody microarray chip.

ビデオ: Experimental Protocol for Detecting Cyanobacteria in Liquid and Solid Samples with an Antibody Microarray Chip

Bacterial Detection &amp; Identification Using Electrochemical Sensors

Electrochemical sensors are widely used for rapid and accurate measurement of blood glucose and can be adapted for detection of a wide variety of analytes. Electrochemical sensors operate by transducing a biological recognition event into a useful electrical signal. Signal transduction occurs by coupling the activity of a redox enzyme to an amperometric electrode. Sensor specificity is either an inherent characteristic of the enzyme, glucose oxidase in the case of a glucose sensor, or a product of linkage between the enzyme and an antibody or probe.
Here, we describe an electrochemical sensor assay method to directly detect and identify bacteria. In every case, the probes described here are DNA oligonucleotides. This method is based on sandwich hybridization of capture and detector probes with target ribosomal RNA (rRNA). The capture probe is anchored to the sensor surface, while the detector probe is linked to horseradish peroxidase (HRP). When a substrate such as 3,3',5,5'-tetramethylbenzidine (TMB) is added to an electrode with capture-target-detector complexes bound to its surface, the substrate is oxidized by HRP and reduced by the working electrode. This redox cycle results in shuttling of electrons by the substrate from the electrode to HRP, producing current flow in the electrode.

Bacterial Detection & Identification Using Electrochemical Sensors

We describe an electrochemical sensor assay method for rapid bacterial detection and identification. The assay involves a sensor array functionalized with DNA oligonucleotide capture probes for ribosomal RNA (rRNA) species-specific sequences. Sandwich hybridization of target rRNA with the capture probe and a horseradish peroxidase-linked DNA oligonucleotide detector probe produces a measurable amperometric current.

電気化学センサを用いた細菌検出＆識別

Electrochemical  sensors are widely used for rapid and accurate measurement of blood glucose and  can be adapted for detection of a wide variety of ...

生物工学

A Microfluidic Chip for the Versatile Chemical Analysis of Single Cells

We present a microfluidic device that enables the quantitative determination of intracellular biomolecules in multiple single cells in parallel. For this purpose, the cells are passively trapped in the middle of a microchamber. Upon activation of the control layer, the cell is isolated from the surrounding volume in a small chamber. The surrounding volume can then be exchanged without affecting the isolated cell. However, upon short opening and closing of the chamber, the solution in the chamber can be replaced within a few hundred milliseconds. Due to the reversibility of the chambers, the cells can be exposed to different solutions sequentially in a highly controllable fashion, e.g. for incubation, washing, and finally, cell lysis. The tightly sealed microchambers enable the retention of the lysate, minimize and control the dilution after cell lysis. Since lysis and analysis occur at the same location, high sensitivity is retained because no further dilution or loss of the analytes occurs during transport. The microchamber design therefore enables the reliable and reproducible analysis of very small copy numbers of intracellular molecules (attomoles, zeptomoles) released from individual cells. Furthermore, many microchambers can be arranged in an array format, allowing the analysis of many cells at once, given that suitable optical instruments are used for monitoring. We have already used the platform for proof-of-concept studies to analyze intracellular proteins, enzymes, cofactors and second messengers in either relative or absolute quantifiable manner.

In this article we present a microfluidic chip for single cell analysis. It allows the quantification of intracellular proteins, enzymes, cofactors, and second messengers by means of fluorescent assays or immunoassays.&#160;

単一細胞の多彩な化学分析マイクロ流体チップ

We present a microfluidic device that enables the quantitative determination of intracellular biomolecules in multiple single cells in parallel. For this ...

Early Detection of Cyanobacterial Blooms and Associated Cyanotoxins using Fast Detection Strategy

Fast detection of cyanobacteria and cyanotoxins is achieved using a Fast Detection Strategy (FDS). Only 24 h are needed to unravel the presence of cyanobacteria and related cyanotoxins in water samples and in an organic matrix, such as bivalve extracts. FDS combines remote/proximal sensing techniques with analytical/bioinformatics analyses. Sampling spots are chosen through multi-disciplinary, multi-scale, and multi-parametric monitoring in a three-dimensional physical space, including remote sensing. Microscopic observation and taxonomic analysis of the samples are performed in the laboratory setting, which allows for the identification of cyanobacterial species. Samples are then extracted with organic solvents and processed with LC-MS/MS. Data obtained by MS/MS are analyzed using a bioinformatic approach using the online platform Global Natural Products Social (GNPS) to create a network of molecules. These networks are analyzed to detect and identify toxins, comparing data of the fragmentation spectra obtained by mass spectrometry with the GNPS library. This allows for the detection of known toxins and unknown analogues that appear related in the same molecular network.

A fast-multidisciplinarystrategy for early detection of cyanobacterial blooms and associated cyanotoxins is described here. It allows for the detection of cyanobacteria and related cyanotoxins in water samples and in organic matrices, such as bivalve samples, in 24 h.

高速検出戦略を用いたシアノバクテリアブルームと関連サイアノトキシンの早期発見

Fast detection of cyanobacteria and cyanotoxins is achieved using a Fast Detection Strategy (FDS). Only 24 h are needed to unravel the presence of ...

化学

Chemically-blocked Antibody Microarray for Multiplexed High-throughput Profiling of Specific Protein Glycosylation in Complex Samples

In this study, we describe an effective protocol for use in a multiplexed high-throughput antibody microarray with glycan binding protein detection that allows for the glycosylation profiling of specific proteins. Glycosylation of proteins is the most prevalent post-translational modification found on proteins, and leads diversified modifications of the physical, chemical, and biological properties of proteins. Because the glycosylation machinery is particularly susceptible to disease progression and malignant transformation, aberrant glycosylation has been recognized as early detection biomarkers for cancer and other diseases. However, current methods to study protein glycosylation typically are too complicated or expensive for use in most normal laboratory or clinical settings and a more practical method to study protein glycosylation is needed. The new protocol described in this study makes use of a chemically blocked antibody microarray with glycan-binding protein (GBP) detection and significantly reduces the time, cost, and lab equipment requirements needed to study protein glycosylation. In this method, multiple immobilized glycoprotein-specific antibodies are printed directly onto the microarray slides and the N-glycans on the antibodies are blocked. The blocked, immobilized glycoprotein-specific antibodies are able to capture and isolate glycoproteins from a complex sample that is applied directly onto the microarray slides. Glycan detection then can be performed by the application of biotinylated lectins and other GBPs to the microarray slide, while binding levels can be determined using Dylight 549-Streptavidin. Through the use of an antibody panel and probing with multiple biotinylated lectins, this method allows for an effective glycosylation profile of the different proteins found in a given human or animal sample to be developed.
Introduction
Glycosylation of protein, which is the most ubiquitous post-translational modification on proteins, modifies the physical, chemical, and biological properties of a protein, and plays a fundamental role in various biological processes1-6. Because the glycosylation machinery is particularly susceptible to disease progression and malignant transformation, aberrant glycosylation has been recognized as early detection biomarkers for cancer and other diseases 7-12. In fact, most current cancer biomarkers, such as the L3 fraction of &alpha;-1 fetoprotein (AFP) for hepatocellular carcinoma 13-15, and CA199 for pancreatic cancer 16, 17 are all aberrant glycan moieties on glycoproteins. However, methods to study protein glycosylation have been complicated, and not suitable for routine laboratory and clinical settings. Chen et al. has recently invented a chemically blocked antibody microarray with a glycan-binding protein (GBP) detection method for high-throughput and multiplexed profile glycosylation of native glycoproteins in a complex sample 18. In this affinity based microarray method, multiple immobilized glycoprotein-specific antibodies capture and isolate glycoproteins from the complex mixture directly on the microarray slide, and the glycans on each individual captured protein are measured by GBPs. Because all normal antibodies contain N-glycans which could be recognized by most GBPs, the critical step of this method is to chemically block the glycans on the antibodies from binding to GBP. In the procedure, the cis-diol groups of the glycans on the antibodies were first oxidized to aldehyde groups by using NaIO4 in sodium acetate buffer avoiding light. The aldehyde groups were then conjugated to the hydrazide group of a cross-linker, 4-(4-N-MaleimidoPhenyl)butyric acid Hydrazide HCl (MPBH), followed by the conjugation of a dipeptide, Cys-Gly, to the maleimide group of the MPBH. Thus, the cis-diol groups on glycans of antibodies were converted into bulky none hydroxyl groups, which hindered the lectins and other GBPs bindings to the capture antibodies. This blocking procedure makes the GBPs and lectins bind only to the glycans of captured proteins. After this chemically blocking, serum samples were incubated with the antibody microarray, followed by the glycans detection by using different biotinylated lectins and GBPs, and visualized with Cy3-streptavidin. The parallel use of an antibody panel and multiple lectin probing provides discrete glycosylation profiles of multiple proteins in a given sample 18-20. This method has been used successfully in multiple different labs 1, 7, 13, 19-31. However, stability of MPBH and Cys-Gly, complicated and extended procedure in this method affect the reproducibility, effectiveness and efficiency of the method. In this new protocol, we replaced both MPBH and Cys-Gly with one much more stable reagent glutamic acid hydrazide (Glu-hydrazide), which significantly improved the reproducibility of the method, simplified and shorten the whole procedure so that the it can be completed within one working day. In this new protocol, we describe the detailed procedure of the protocol which can be readily adopted by normal labs for routine protein glycosylation study and techniques which are necessary to obtain reproducible and repeatable results.

In this study, we describe an improved protocol for a multiplexed high-throughput antibody microarray with lectin detection method that can be used in glycosylation profiling of specific proteins. This protocol features new reliable reagents and significantly reduces the time, cost, and lab equipment requirements as compared to the previous procedure.

複雑なサンプル中の特定のタンパク質のグリコシル化の多重化ハイスループットプロファイリングのための化学的にブロックされた抗体マイクロアレイ

 In this study, we describe an effective protocol for use in a multiplexed high-throughput antibody microarray with glycan binding protein detection that ...

生物学

Human Serum Anti-aquaporin-4 Immunoglobulin G Detection by Cell-based Assay

Anti-aquaporin-4 (AQP4) immunoglobulin G (IgG) is the core diagnostic biomarker for neuromyelitis optica spectrum disorders (NMOSD). The cell-based assay (CBA) is a widely used method to detect anti-AQP4 IgG in human serum with high sensitivity and specificity. Briefly, serum anti-AQP4 IgG is captured by AQP4-transfected cell that is fixed on the biochip then detected by a fluorescein-labelled secondary antibody. Fluorescence microscopy is utilized to visualize the fluorescence, and the intensity of fluorescence is evaluated by at least two experienced clinicians. A final diagnosis of NMOSD can be made based on the combination of anti-AQP4 IgG detection results, clinical manifestations, and neuroradiological findings. According to previous studies, CBA is more sensitive and specific than other anti-AQP4 IgG detection methods, and it can be applied to both clinical diagnosis and studies of NMOSD. The method has limitations; for example, an international scale to evaluate serum anti-AQP4 IgG titers is still lacking. Here, a detailed protocol for human serum anti-AQP4 IgG detection using CBA is described.

Cell-based assay is a widely used method to detect serum anti-aquaporin-4 immunoglobulin G. This method could be applied to clinical diagnosis and scientific researches of neuromyelitis optical spectrum disorders.

細胞ベースのアッセイによるひと血清抗アクアポリン 4 免疫グロブリン G の検出

Anti-aquaporin-4 (AQP4) immunoglobulin G (IgG) is the core diagnostic biomarker for neuromyelitis optica spectrum disorders (NMOSD). The cell-based assay ...

免疫・感染学

Use of an Influenza Antigen Microarray to Measure the Breadth of Serum Antibodies Across Virus Subtypes

The influenza virus remains a significant cause of mortality worldwide due to the limited effectiveness of currently available vaccines. A key challenge to the development of universal influenza vaccines is high antigenic diversity resulting from antigenic drift. Overcoming this challenge requires novel research tools to measure the breadth of serum antibodies directed against many virus strains across different antigenic subtypes. Here, we present a protocol for analyzing the breadth of serum antibodies against diverse influenza virus strains using a protein microarray of influenza antigens.
This influenza antigen microarray is constructed by printing purified hemagglutinin and neuraminidase antigens onto a nitrocellulose-coated membrane using a microarray printer. Human sera are incubated on the microarray to bind antibodies against the influenza antigens. Quantum-dot-conjugated secondary antibodies are used to simultaneously detect IgG and IgA antibodies binding to each antigen on the microarray. Quantitative antibody binding is measured as fluorescence intensity using a portable imager. Representative results are shown to demonstrate assay reproducibility in measuring subtype-specific and cross-reactive influenza antibodies in human sera.
Compared to traditional methods such as ELISA, the influenza antigen microarray provides a high throughput multiplexed approach capable of testing hundreds of sera for multiple antibody isotypes against hundreds of antigens in a short time frame, and thus has applications in sero-surveillance and vaccine development. A limitation is the inability to distinguish binding antibodies from neutralizing antibodies.

We present a protocol for using a protein microarray constructed by printing influenza antigens onto nitrocellulose-coated slides to simultaneously probe serum for multiple antibody isotypes against over 250 antigens from different virus strains, thus allowing measurement of the breadth of serum antibodies across virus subtypes.

インフルエンザ抗原マイクロアレイを用いたウイルスサブタイプにわたる血清抗体の幅を測定

The influenza virus remains a significant cause of mortality worldwide due to the limited effectiveness of currently available vaccines. A key challenge ...

An Assay to Detect Serum Anti-aquaporin-4 Immunoglobulin G

Source: Liu, C. et al., <a href="https://app.jove.com/v/59014">Human Serum Anti-aquaporin-4 Immunoglobulin G Detection by Cell-based Assay.</a>&#160;J. Vis. Exp.&#160;(2019)
The video demonstrates a cell-based assay for detecting anti-aquaporin-4 immunoglobulin G using a biochip containing untransfected cells and transfected cells expressing aquaporin-4. This method has applications in diagnosing neuromyelitis optica spectrum disorders, confirmed by strong green fluorescence on the biochip.

血清抗アクアポリン-4免疫グロブリンGを検出するためのアッセイ

All procedures involving human participants have been performed in compliance with the institutional, national, and international guidelines for human ...

JoVE Encyclopedia of Experiments

免疫学

抗体ベースの技術

特性評価と機能分析

Antibody Microarray: A Technique to Study the Protein Expression of miRNA Treated Lung Cancer Cells

Source: Hossian, A. et. al. <a href="https://www.jove.com/v/59460/analysis-combinatorial-mirna-treatments-to-regulate-cell-cycle">Analysis of Combinatorial miRNA Treatments to Regulate Cell Cycle and Angiogenesis.</a> J. Vis. Exp. (2019).
This video describes the technique to study the protein expression in miRNA transfected lung cancer cells by using antibody microarray to measure specific gene expression. In the featured protocol, we perform antibody microarray for the identification of the activity of a combinatorial miRNA treatment in halting cell cycle and angiogenesis.

抗体マイクロアレイ:miRNA処理肺がん細胞のタンパク質発現を研究する技術

Source: Hossian, A. et. al. Analysis of Combinatorial miRNA Treatments to Regulate Cell Cycle and Angiogenesis. J. Vis. Exp. (2019).
This video describes ...

がん研究

肺がん

試験管研究

A Technique to Detect Cyanobacterial Strains Using an Antibody Microarray Chip

Source: Blanco, Y. et al., <a href="https://app.jove.com/v/54994">Experimental Protocol for Detecting Cyanobacteria in Liquid and Solid Samples with an Antibody Microarray Chip.</a>&#160;J. Vis. Exp. (2017)
This video demonstrates a method to detect the Cyanobacterial strains in an environmental sample using an antibody microarray chip. Samples carrying various bacteria interact with printed antibodies, and immunostaining with fluorophore-labeled anti-cyanobacterial-strain antibodies reveals the presence of specific cyanobacterial strains through fluorescence in distinct spots.

抗体マイクロアレイチップを用いたシアノバクテリア株検出技術

1. Preparation of the Immunogens

	Grow each cyanobacterial strain in the corresponding culture medium under conditions described in&#160;Table ...

抗体ベースのイメージングと検出方法

Viral Antigen Microarray Assay to Detect Antibody Isotypes in Serum Against Viral Antigen

Source: Khan, S., et al., <a href="https://app.jove.com/v/59973">Use of an Influenza Antigen Microarray to Measure the Breadth of Serum Antibodies Across Virus Subtypes.</a> J. Vis. Exp. (2019)
In this video, we demonstrate the process for detecting antibody isotypes in multiple human serum samples using a microarray slide printed with antigenic subtypes of influenza virus strains.

ウイルス抗原に対する血清中の抗体アイソタイプを検出するためのウイルス抗原マイクロアレイアッセイ

Source: Khan, S., et al., Use of an Influenza Antigen Microarray to Measure the Breadth of Serum Antibodies Across Virus Subtypes. J. Vis. Exp. (2019)
In ...

検出するための実験プロトコール

要約

さらに動画を探す