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Citations & References (151)
Invitrogen™
CPM (7-Diethylamino-3-(4'-Maleimidylphenyl)-4-Methylcoumarin)
チオール反応性クマリンであるCPMは、チオールと反応するまで蛍光性が非常に弱く、約384/470 nmの励起／最大発光を持つコンジュゲートを生成します。詳細を見る
| 製品番号（カタログ番号） | 数量 |
|---|---|
| D346 | 25 mg |
製品番号（カタログ番号） D346
価格（JPY）お問い合わせください ›
57,100
온라인 행사
Ends: 27-Mar-2026
95,300割引額 38,200 (40%)
Each
数量:
25 mg
チオール反応性クマリンであるCPMは、チオールと反応するまで蛍光性が非常に弱く、約384/470 nmの励起／最大発光を持つコンジュゲートを生成します。
研究用途にのみご使用ください。診断目的には使用できません。
仕様
化学反応性チオール
発光470 nm
励起384 nm
標識または色素メチルクマリン
製品タイプCPM
数量25 mg
反応性部分マレイミド
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 (151)
引用および参考文献
Abstract
Fluorescence resonance energy transfer mapping of the fourth of six nucleotide-binding sites of chloroplast coupling factor 1.
Journal:J Biol Chem
PubMed ID:1832671
Equilibrium dialysis measurements of adenine nucleotide binding to chloroplast coupling factor 1 suggest that the enzyme has six binding sites for ADP, adenylyl-beta,gamma-imidodiphosphate (AMP-PNP), and 2'(3')-O-2,4,6-trinitrophenyl-ATP (TNP-ATP). High affinity binding at all six sites requires the divalent cation, Mg2+. Three of the nucleotide-binding sites, sites 1, 2, and 3, have
Arrangement of the COOH-terminal and NH2-terminal domains of caldesmon bound to actin.
Journal:Biochemistry
PubMed ID:9092808
'Smooth muscle caldesmon is a single polypeptide chain with its NH2- and COOH-terminal domains separated by a long alpha-helix. Caldesmon was labeled at either Cys-153 in the NH2 domain or Cys-580 in the COOH domain with a variety of fluorescence probes. Fluorescence intensity, peak position, and polarization of probes on
The pleckstrin homology domain of phospholipase Cbeta transmits enzymatic activation through modulation of the membrane-domain orientation.
Journal:Biochemistry
PubMed ID:16669615
'Phospholipase Cbeta (PLCbeta) enzymes are activated by Galpha q and Gbetagamma subunits and catalyze the hydrolysis of the minor membrane lipid phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2]. Activation of PLCbeta2 by Gbetagamma subunits has been shown to be conferred through its N-terminal pleckstrin homology (PH) domain, although the underlying mechanism is unclear. Also
Structural organization of chloroplast coupling factor.
Journal:Biochemistry
PubMed ID:2859887
'Fluorescence resonance energy transfer measurements have been used to construct spatial maps for the accessible sulfhydryl of the gamma subunit (dark site) and the essential tyrosine residue of the beta subunits relative to previously mapped sites on the H+-ATPase from chloroplasts. The extent of energy transfer was measured between a
Signaling through a G Protein-coupled receptor and its corresponding G protein follows a stoichiometrically limited model.
Journal:J Biol Chem
PubMed ID:17420253
'The bradykinin receptor is a G protein-coupled receptor (GPCR) that is coupled to the Galpha(q) family of heterotrimeric G proteins. In general, a GPCR can exert intracellular signals either by transiently associating with multiple diffusing G protein subunits or by activating a G protein that is stably bound to the