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Citations & References (151)
Invitrogen™
Tetramethylrhodamine-5-Iodoacetamide Dihydroiodide (5-TMRIA), single isomer
チオール反応性テトラメチルローダミン-5-ヨードアセトアミドジヒドロヨウ化物（5-TMRIA）を使用して、励起／最大発光が約555/580の、明るいオレンジ色の赤色蛍光バイオコンジュゲートを作成できます。詳細を見る
| 製品番号（カタログ番号） | 数量 |
|---|---|
| T6006 | 5 mg |
製品番号（カタログ番号） T6006
価格（JPY）お問い合わせください ›
61,800
온라인 행사
Ends: 27-Mar-2026
103,100割引額 41,300 (40%)
5 mg
数量:
5 mg
チオール反応性テトラメチルローダミン-5-ヨードアセトアミドジヒドロヨウ化物（5-TMRIA）を使用して、励起／最大発光が約555/580の、明るいオレンジ色の赤色蛍光バイオコンジュゲートを作成できます。
研究用にのみ使用できます。診断用には使用いただけません。
仕様
化学反応性チオール
発光580
励起555
標識または色素ローダミン異性体、TMR(テトラメチルローダミン)
製品タイプテトラメチルローダミン-5-ヨードアセトアミドジヒドロヨウ化物
数量5 mg
反応性部分ハロゲン化アルキル、ヨードアセトアミド
出荷条件室温
標識タイプ従来の色素
Unit Size5 mg
組成および保存条件
フリーザー(-5∼-30度)に保存し、遮光してください。
引用および参考文献 (151)
引用および参考文献
Abstract
Rapid binding of synapsin I to F- and G-actin. A study using fluorescence resonance energy transfer.
Journal:FEBS Lett
PubMed ID:8365471
Synapsin I is a nerve terminal phosphoprotein which interacts with synaptic vesicles and actin in a phosphorylation-dependent manner. By using fluorescence resonance energy transfer between purified components labeled with fluorescent probes, we now show that the binding of synapsin I to actin is a rapid phenomenon. Binding of synapsin I
A non-radioactive automated method for DNA sequence determination.
Journal:J Biochem Biophys Methods
PubMed ID:3559035
A method and instrument for automated DNA sequencing without radioactivity have been developed. In spite of the success with radioactive labels there are drawbacks attached to the technique, such as hazards in the handling, storage and disposal of radioactive materials, and the considerable cost of the radiolabelled nucleoside triphosphates. In
Functional studies of the domains of talin.
Journal:J Cell Biol
PubMed ID:2110569
'The protein talin has two domains of approximately 200 and 47 kD, which can be cleaved apart by a variety of proteases. To examine the function of these two structural domains of talin, we have digested purified talin with a calcium-dependent protease and separated the resulting fragments chromatographically. Both fragments
Low molecular-weight G-actin binding proteins involved in the regulation of actin assembly during myofibrillogenesis.
Journal:Cell Struct Funct
PubMed ID:9113405
'We previously demonstrated that small G-actin binding proteins, cofilin, ADF and profilin, are involved in the actin dynamics during myofibrillogenesis (OBINATA, T. (1993). Int. Rev. Cytol., 143: 153-189.). To better understand how they are responsible for the regulation of actin assembly, the amounts of the actin-binding proteins were quantified by
Association of microinjected myosin and its subfragments with myofibrils in living muscle cells.
Journal:J Cell Biol
PubMed ID:3058721
'Purified skeletal muscle myosin was labeled with iodoacetamidofluorescein and microinjected into cultured chick myotubes. The fluorescent myosin analogue became incorporated within 10-15 min after injection, into either periodic (mean periodicity = 2.23 +/- 0.02 micron) bands or apparently continuous fibrillar structures. Comparison of rhodamine-labeled alpha-actinin with coinjected fluorescein-labeled myosin suggested