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引用資料與參考文獻 (151)
Invitrogen™
CPM (7-Diethylamino-3-(4'-Maleimidylphenyl)-4-Methylcoumarin)
The thiol-reactive coumarin, CPM is very weakly fluorescent until reacted with thiols producing a conjugate with excitation/emission maxima of ∼384/470深入閱讀
| 產品號碼 | Quantity |
|---|---|
| D346 | 25 mg |
產品號碼 D346
價格 (TWD)
16,730.00
Online offer
Ends: 31-Dec-2025
23,900.00您節省 7,170.00 (30%)
Each
Quantity:
25 mg
價格 (TWD)
16,730.00
Online offer
Ends: 31-Dec-2025
23,900.00您節省 7,170.00 (30%)
Each
The thiol-reactive coumarin, CPM is very weakly fluorescent until reacted with thiols producing a conjugate with excitation/emission maxima of ∼384/470 nm.
For Research Use Only. Not for use in diagnostic procedures.
規格
Chemical ReactivityThiol
Emission470 nm
Excitation384 nm
Label or DyeMethylcoumarin
Product TypeCPM
Quantity25 mg
Reactive MoietyMaleimide
Shipping ConditionRoom Temperature
Label TypeClassic Dyes
Unit SizeEach
內容物與存放
Store in freezer (-5°C to -30°C) and protect from light.
引用資料與參考文獻 (151)
引用資料與參考文獻
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