BODIPY™ TMR C5-Maleimide
BODIPY&trade; TMR C<sub>5</sub>-Maleimide
Citas y referencias (4)
Invitrogen™

BODIPY™ TMR C5-Maleimide

La maleimida BODIPY™ TMR reactiva al tiol produce conjugados de colorante electrónicamente neutros que son espectralmente similares al colorante deMás información
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Número de catálogoCantidad
B304661 mg
Número de catálogo B30466
Precio (CLP)
-
Cantidad:
1 mg
La maleimida BODIPY™ TMR reactiva al tiol produce conjugados de colorante electrónicamente neutros que son espectralmente similares al colorante de tetrametilrodamina con carga positiva. La falta de carga iónica de este colorante produce efectos mínimos en los puntos isoeléctricos de las proteínas estándar conjugadas con este fluoróforo. El colorante BODIPY™ TMR de tamaño pequeño y vida útil de estado de excitación relativamente larga ha demostrado ser útil para estudiar la interacción ligando-receptor por polarización de fluoresencia.
Para uso exclusivo en investigación. No apto para uso en procedimientos diagnósticos.
Especificaciones
Reactividad químicaTiol
Etiqueta o tinteBODIPY™ TMR
Tipo de productoMaleimida
Cantidad1 mg
Fracción reactivaMaleimida
Condiciones de envíoTemperatura ambiente
Tipo de etiquetaColorantes BODIPY
Línea de productosBODIPY
Unit SizeEach
Contenido y almacenamiento
Almacenar en el congelador (de – 5 a – 30 °C) y proteger de la luz.

Citations & References (4)

Citations & References
Abstract
Family of pH (low) insertion peptides for tumor targeting.
Authors:Weerakkody D, Moshnikova A, Thakur MS, Moshnikova V, Daniels J, Engelman DM, Andreev OA, Reshetnyak YK,
Journal:Proc Natl Acad Sci U S A
PubMed ID:23530249
'Cancer is a complex disease with a range of genetic and biochemical markers within and among tumors, but a general tumor characteristic is extracellular acidity, which is associated with tumor growth and development. Acidosis could be a universal marker for cancer imaging and the delivery of therapeutic molecules, but its ... More
The crystal structure of the C-terminus of adseverin reveals the actin-binding interface.
Authors:Chumnarnsilpa S, Lee WL, Nag S, Kannan B, Larsson M, Burtnick LD, Robinson RC,
Journal:Proc Natl Acad Sci U S A
PubMed ID:19666531
Adseverin is a member of the calcium-regulated gelsolin superfamily of actin severing and capping proteins. Adseverin comprises 6 homologous domains (A1-A6), which share 60% identity with the 6 domains from gelsolin (G1-G6). Adseverin is truncated in comparison to gelsolin, lacking the C-terminal extension that masks the F-actin binding site in ... More
Ca2+ binding by domain 2 plays a critical role in the activation and stabilization of gelsolin.
Authors:Nag S, Ma Q, Wang H, Chumnarnsilpa S, Lee WL, Larsson M, Kannan B, Hernandez-Valladares M, Burtnick LD, Robinson RC,
Journal:Proc Natl Acad Sci U S A
PubMed ID:19666512
Gelsolin consists of six homologous domains (G1-G6), each containing a conserved Ca-binding site. Occupation of a subset of these sites enables gelsolin to sever and cap actin filaments in a Ca-dependent manner. Here, we present the structures of Ca-free human gelsolin and of Ca-bound human G1-G3 in a complex with ... More
Detecting changes in the thiol redox state of proteins following a decrease in oxygen concentration using a dual labeling technique.
Authors:Lui JK, Lipscombe R, Arthur PG,
Journal:J Proteome Res
PubMed ID:19894774
Cells are routinely exposed to hyperoxic conditions when cultured in the presence of 95% air and 5% carbon dioxide. Hyperoxic conditions can increase the generation of reactive oxygen species and cause oxidative stress. Oxidative stress has been proposed to cause cells in culture to behave differently from cells in vivo. ... More