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Citations & References (6)
Invitrogen™
Tetramethylrhodamine Cadaverine, 5-(and-6)-((N-(5-Aminopentyl) Amino) Carbonyl) Tetramethylrhodamine, mixed isomers
テトラメチルローダミンカダベリン、5-（および-6）-（（N-（5-アミノメチル）アミノ）カルボニル）テトラメチルローダミン、混合異性体
| 製品番号（カタログ番号） | 数量 |
|---|---|
| A1318 または、製品番号A-1318 | 10 mg |
製品番号（カタログ番号） A1318
または、製品番号A-1318
価格（JPY）
39,000
キャンペーン価格
Ends: 25-Dec-2026
65,000割引額 26,000 (40%)
Each
数量:
10 mg
The primary aliphatic amine of tetramethylrhodamine cadaverine can be reversibly coupled to aldehydes and ketones to form a Schiff base - which can be reduced to a generate stable amine derivative by sodium borohydride (NaBH4) or sodium cyanoborohydride (NaCNH3). Carboxylic acids of proteins and other water-soluble biopolymers can be coupled to this molecule in aqueous solution using water-soluble carbodiimides such as EDAC (E2247). This material consists of the 5- and 6- isomer. Please see the structure for additional details.
テトラメチルローダミンカダベリンの第一脂肪族アミンは、アルデヒドおよびケトンと可逆的に結合してシッフ塩基を形成できます。シッフ塩基は、水素化ホウ素ナトリウム（NaBH4）またはシアノ水素化ホウ素ナトリウム（NaCNH3）によって安定したアミン誘導体に還元できます。タンパク質や他の水溶性バイオポリマーのカルボン酸は、EDAC（E2247）などの水溶性カルボジイミドを使用して水溶液中のこの分子に結合できます。この材料は、5および6異性体で構成されています。詳細については、構造を参照してください。
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
化学反応性カルボン酸、ケトン、アルデヒド
標識または色素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カダベリン
数量10 mg
反応性部分アミン、カダベリン
出荷条件室温
標識タイプ従来の色素
Unit SizeEach
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 (6)
引用および参考文献
Abstract
Antagonistic effects of cofilin, beryllium fluoride complex, and phalloidin on subdomain 2 and nucleotide-binding cleft in F-actin.
Journal:Biophys J
PubMed ID:16997870
'Cofilin/ADF, beryllium fluoride complex (BeFx), and phalloidin have opposing effects on actin filament structure and dynamics. Cofilin/ADF decreases the stability of F-actin by enhancing disorder in subdomain 2, and by severing and accelerating the depolymerization of the filament. BeFx and phalloidin stabilize the subdomain 2 structure and decrease the critical
Dynamic polymorphism of single actin molecules in the actin filament.
Journal:Nat Chem Biol
PubMed ID:16415860
'Actin filament dynamics are critical in cell motility. The structure of actin filament changes spontaneously and can also be regulated by actin-binding proteins, allowing actin to readily function in response to external stimuli. The interaction with the motor protein myosin changes the dynamic nature of actin filaments. However, the molecular
Synthesis and characterization of conjugates formed between periodate-oxidized ribonucleotides and amine-containing fluorophores.
Journal:Bioconjug Chem
PubMed ID:7849074
The synthesis and purification of new fluorescently labeled derivatives of GDP and ATP are described. The fluorescent groups are coupled initially through amine-containing linker arms to periodate-oxidized nucleotides. Reduction of the initial product yields primarily a six-membered morpholine-like ring. Fluorescein-labeled GDP, rhodamine-labeled GDP, and fluorescein-labeled ATP were characterized by absorbance
The mitogen-activated protein kinase kinase kinase dual leucine zipper-bearing kinase (DLK) acts as a key regulator of keratinocyte terminal differentiation.
Journal:J Biol Chem
PubMed ID:15695824
In the skin, epithelial cells undergo a terminal differentiation program leading to the formation of the stratum corneum. Although it is expected that the last phases of this process must be tightly regulated since it results in cell death, the signaling pathways involved in this induction remain ill defined. We
Orientation of actin monomer in the F-actin filament: radial coordinate of glutamine-41 and effect of myosin subfragment 1 binding on the monomer orientation.
Journal:Biochemistry
PubMed ID:3166995
We have employed the method of radial distance measurements in order to orient the actin monomer in the F-actin filament. This method utilizes fluorescence resonance energy transfer measurements of the distance between two equivalent chemical points located on two different monomers. The interprobe distance obtained this way is used to