JP6168497B2 - 抗体検出用試薬の製造方法、及びその用途 - Google Patents
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Description
(2)前記抗原タンパク質が、全長タンパク質であることを特徴とする、(1)に記載の抗体検出用試薬の製造方法、
(3)前記抗原タンパク質が、膜タンパク質であることを特徴とする、(1)又は(2)に記載の抗体検出用試薬の製造方法、
(4)前記抗原タンパク質が、がん抗原タンパク質であることを特徴とする、(1)〜(3)のいずれか一つに記載の抗体検出用試薬の製造方法、
(5)前記カチオン化が、抗原タンパク質のチオール基にカチオン化剤を結合させることによって行われることを特徴とする、(1)〜(4)のいずれか一つに記載の抗体検出用試薬の製造方法。
(7)前記チオスルホナート化合物が、以下の式の化合物である
(6)に記載の抗体検出用試薬の製造方法(式中、R1は、炭素原子数2〜20の直鎖アルキレン基を表し、R2は、炭素原子数1〜3のアルキル基を表し、nは1〜3のいずれかの整数である)、
(8)前記化合物が、R1が−(CH2)3−であり、R2がCH3−であり、nが1で表されるTAPS-Sulfonateであることを特徴とする、(7)に記載の製造方法、
(9)前記化合物が、R1が−(CH2)3−であり、R2がCH3−であり、nが3で表されるTAP3S-Sulfonateであることを特徴とする、(7)に記載の抗体検出用試薬の製造方法、
(10)前記ハロゲン化アルキル系カチオン化剤が、TAP−Brであることを特徴とする、(6)に記載の抗体検出用試薬の製造方法、
(11)前記担体が、磁気ビーズであることを特徴とする、(1)〜(10)のいずれか一つに記載の抗体検出用試薬の製造方法。
(14)前記サンプルが、単離された体液であることを特徴とする、(13)に記載の抗体検出方法。
更に、かかる抗体検出用試薬は従来方法で製造された試薬に比べ安定性にすぐれ、長期の保存が可能である。
・被験者の生体内抗体の解析により、被験者のアレルギー反応性を判定する。
・治療の前後において抗体の解析を行い、治療の効果や治療後の経過と相関関係を有する抗体を見出す。見出した抗体を指標として治療方針の決定、予後の予測・判定を行う。
・免疫細胞療法において、患者血清中に抗原特異的抗体が検出された抗原を治療に用いることにより、治療効果の向上を図る。
・放射線療法の前後に、抗体の解析を行うことで、アブスコパル効果等の免疫機能が関与するとされている治療効果の予測を行う。
まず、抗体検出に使用する抗原タンパク質の調製を行った。
TAPS化したMAGE-A4、WT-1に対し逆相HPLCを用いて精製を行った。精製図を図4、5に示す。
COOHビーズの容器をボルテックスミキサーで30秒間振盪し、超音波を30秒かけて、懸濁した。
COOHビーズ懸濁液を14,000×gで4分間遠心し、上清を除去した。
COOHビーズ懸濁液を14,000×gで4分間遠心し、上清を除去した。
2名のがん患者(Donor1及びDonor2)から血液を採取し、血清を取得した。
腎細胞がん患者8名(Donor2〜Donor9)から、EP-DC治療の前後で、血清を取得した。
EP-DC治療は、がん患者から手術によって除去した腫瘍組織を凍結融解法などによりライセートとして調製し、エレクトロポレーション法により樹状細胞に取り込ませ、樹状細胞ワクチンを調製したものを、当該患者へ投与する治療方法である。
ニワトリ卵白リゾチーム(配列番号13、以下、単にリゾチームとも記す、キューピー社製)をサンプルとして、カチオン化試薬のSH基保護能の評価を行った。
タンパク質のSH基がすべて保護されていない状態で抗体検出用試薬を調製・保存した場合には、保護されずに残ったSH基がSS結合を形成し、タンパク質の凝集や抗体検出用試薬の凝集が起こることが想定される。そこで、抗体検出用試薬の保存安定性を、以下の手順により確認した。
ナス型フラスコに上記アフィニティー精製後のXAGE1b又はNY-ESO-1を加え、水分を凍結乾燥機で除去したものを3mLの6M グアニジン,0.1M Tris-HCl pH8で溶解した。脱気・窒素置換後に30mMのDTT(固体)を加え、37℃で1時間ほど処理した。XAGE1b又はNY-ESO-1の含まれる溶液に70mM TAP-Brを添加し、37℃で60分ほど処理した。
Claims (8)
- 抗原タンパク質とビーズとで構成される抗体検出用試薬の製造方法であって、抗原タンパク質のチオール基にカチオン化剤を結合させることによって抗原タンパク質をカチオン化して可溶化する工程と、カチオン化した抗原タンパク質をビーズに固定化させる工程と、を含む抗体検出用試薬の製造方法であって;
カチオン化剤が、TAPS-Sulfonate又はTAP−Brである、上記製造方法。 - 前記抗原タンパク質が、全長タンパク質であることを特徴とする、請求項1に記載の抗体検出用試薬の製造方法。
- 前記抗原タンパク質が、膜タンパク質であることを特徴とする、請求項1又は2に記載の抗体検出用試薬の製造方法。
- 前記抗原タンパク質が、がん抗原タンパク質であることを特徴とする、請求項1乃至3のいずれか一項に記載の抗体検出用試薬の製造方法。
- 前記ビーズが、磁気ビーズであることを特徴とする、請求項1乃至4のいずれか一項に記載の抗体検出用試薬の製造方法。
- 請求項1乃至5のいずれか一項に記載の製造方法によって製造された抗体検出用試薬であって;
チオール基にTAPS基又はTAP基が結合してカチオン化した抗原タンパク質が固定されたビーズである、抗体検出用試薬。 - サンプル中に含まれる抗原特異的な抗体の検出方法であって、請求項6に記載の抗体検出用試薬とサンプルとを接触させる工程と、抗体に結合する標識した二次抗体を添加し、抗体と結合させる工程と、抗体検出用試薬を回収する工程と、抗体が結合した抗体検出用試薬を検出する工程とを含む、抗体検出方法。
- 前記サンプルが、単離された体液であることを特徴とする、請求項7に記載の抗体検出方法。
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CA2794217C (en) * | 2010-03-25 | 2018-01-02 | National University Corporation Okayama University | Thiosulfonate compound, reversible cationization agent for protein and/or peptide, and method for solubilization |
US10822384B2 (en) * | 2012-03-30 | 2020-11-03 | Junichiro Futami | Method for producing reagent for antibody detection and use thereof |
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2013
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- 2013-03-29 SG SG11201406160QA patent/SG11201406160QA/en unknown
- 2013-03-29 EP EP13768100.3A patent/EP2833143B1/en active Active
- 2013-03-29 TW TW102111632A patent/TWI582424B/zh active
- 2013-03-29 CN CN201380028339.6A patent/CN104380106B/zh active Active
- 2013-03-29 JP JP2013531595A patent/JP6168497B2/ja active Active
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US10822384B2 (en) | 2020-11-03 |
CN104380106B (zh) | 2017-02-22 |
AU2013240942B2 (en) | 2018-07-05 |
US20150064801A1 (en) | 2015-03-05 |
SG11201406160QA (en) | 2014-11-27 |
CN104380106A (zh) | 2015-02-25 |
EP2833143A4 (en) | 2015-11-11 |
EP2833143B1 (en) | 2019-04-24 |
JPWO2013147233A1 (ja) | 2015-12-14 |
AU2013240942A1 (en) | 2014-11-13 |
TWI582424B (zh) | 2017-05-11 |
EP2833143A1 (en) | 2015-02-04 |
US20210032302A1 (en) | 2021-02-04 |
WO2013147233A1 (ja) | 2013-10-03 |
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