Tetramethylrhodamine-5-Maleimide, single isomer
Invitrogen™

Tetramethylrhodamine-5-Maleimide, single isomer

Tetramethylrhodamin-5-Maleimid ist ein Thiol-reaktiver Farbstoff, der lichtbeständige, pH-unempfindliche, rot-orange—fluoreszierende Konjugate liefert.Weitere Informationen
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KatalognummerMenge
T60275 mg
Katalognummer T6027
Preis (EUR)
716,00
5 mg
Menge:
5 mg
Preis (EUR)
716,00
5 mg
Tetramethylrhodamin-5-Maleimid ist ein Thiol-reaktiver Farbstoff, der lichtbeständige, pH-unempfindliche, rot-orange—fluoreszierende Konjugate liefert.
Nur für Forschungszwecke. Nicht zur Verwendung bei diagnostischen Verfahren.
Specifications
Chemische ReaktivitätThiol
Marker oder FarbstoffTMR (Tetramethylrhodamin)
ProdukttypTetramethylrhodamin-5-Maleimid
Menge5 mg
Reaktiver TeilMaleimid
VersandbedingungRaumtemperatur
MarkertypKlassische Farbstoffe
Unit Size5 mg
Inhalt und Lagerung
Bei -5 bis -30 °C lagern und vor Licht schützen.

Zitierungen und Referenzen (75)

Zitierungen und Referenzen
Abstract
Nuclear import of the ran exchange factor, RCC1, is mediated by at least two distinct mechanisms.
Authors:Nemergut ME, Macara IG
Journal:J Cell Biol
PubMed ID:10811825
'RCC1, the only known guanine-nucleotide exchange factor for the Ran GTPase, is an approximately 45-kD nuclear protein that can bind chromatin. An important question concerns how RCC1 traverses the nuclear envelope. We now show that nuclear RCC1 is not exported readily in interphase cells and that the import of RCC1 ... More
Evidence that translocation of the proteinase precedes its acylation in the serpin inhibition pathway.
Authors:Mellet P, Bieth JG
Journal:J Biol Chem
PubMed ID:10753871
'The inhibition of proteinases by serpins involves cleavage of the serpin, acylation, and translocation of the proteinase. To see whether acylation precedes or follows translocation, we have investigated the pH dependence of the interaction of fluorescein isothiocyanate-elastase with rhodamine alpha(1)-proteinase inhibitor (alpha(1)PI) using two independent methods: (i) kinetics of fluorescence ... More
Differential behavior of two cysteine residues on the myosin head in muscle fibers.
Authors:Miyanishi T, Borejdo J
Journal:Biochemistry
PubMed ID:2523734
'We have previously shown that the orientation of (iodoacetamido)tetramethylrhodamine labels on SH1 thiol of S-1 moieties changes when MgADP is added to the fibers in rigor [Borejdo, J., Assulin, O., Ando, T., & Putnam, S. (1982) J. Mol. Biol. 158, 391-414. Burghardt, T.P., Ando, T., & Borejdo, J. (1983) Proc. ... More
Subunit interactions of GTP-binding proteins.
Authors:Heithier H, Fröhlich M, Dees C, Baumann M, Häring M, Gierschik P, Schiltz E, Vaz WL, Hekman M, Helmreich EJ
Journal:Eur J Biochem
PubMed ID:1312936
'Fluorescence energy transfer [cf. Förster, T. (1948) Ann. Phys. 6, 55-75] was tested for its suitability to study quantitative interactions of subunits of G0 with each other and these subunits or trimeric G0 with the beta 1-adrenoceptor in detergent micelles or after reconstitution into lipid vesicles [according to Feder, D., ... More
Myosin II filament assemblies in the active lamella of fibroblasts: their morphogenesis and role in the formation of actin filament bundles.
Authors:Verkhovsky AB, Svitkina TM, Borisy GG
Journal:J Cell Biol
PubMed ID:7490299
'The morphogenesis of myosin II structures in active lamella undergoing net protrusion was analyzed by correlative fluorescence and electron microscopy. In rat embryo fibroblasts (REF 52) microinjected with tetramethylrhodamine-myosin II, nascent myosin spots formed close to the active edge during periods of retraction and then elongated into wavy ribbons of ... More