BODIPY™ FL ATP-γ-S, Thioester (Adenosine 5'-O-(3-Thiotriphosphate), BODIPY™ FL Thioester, Sodium Salt)
BODIPY&trade; FL ATP-&gamma;-S, Thioester (Adenosine 5'-<i>O</i>-(3-Thiotriphosphate), BODIPY&trade; FL Thioester, Sodium Salt)
Citas y referencias (4)
Invitrogen™

BODIPY™ FL ATP-γ-S, Thioester (Adenosine 5'-O-(3-Thiotriphosphate), BODIPY™ FL Thioester, Sodium Salt)

ATP-γ-S BODIPY™ FL se une a proteínas de unión a ATP. Para crear este nucleótido fluorescente, el fluoróforo BODIPY FLMás información
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Número de catálogoCantidad
A2218450 μl
Número de catálogo A22184
Precio (MXN)
-
Cantidad:
50 μl
ATP-γ-S BODIPY™ FL se une a proteínas de unión a ATP. Para crear este nucleótido fluorescente, el fluoróforo BODIPY FL se unió a través del γ-tiol de ATP-γ-S. Además de su uso potencial para estudios de unión, el tioéter ATP-γ-S BODIPY FL es un nuevo sustrato importante para Fhit, un miembro de la superfamilia de proteínas de unión a nucleótidos de la tríada de histidina.
Para uso exclusivo en investigación. No apto para uso en procedimientos diagnósticos.
Especificaciones
Etiqueta o tinteBODIPY™ FL
Tipo de productoFL ATP-gamma-S, tioéster
Cantidad50 μl
Condiciones de envíoHielo húmedo
Concentración5 mM
Línea de productosBODIPY
Unit SizeEach
Contenido y almacenamiento
Almacenar en el congelador de -5 °C a -30 °C y proteger de la luz.

Citations & References (4)

Citations & References
Abstract
Fhit-nucleotide specificity probed with novel fluorescent and fluorogenic substrates.
Authors:Draganescu A, Hodawadekar SC, Gee KR, Brenner C
Journal:J Biol Chem
PubMed ID:10671479
'Fhit, a member of the histidine triad superfamily of nucleotide-binding proteins, binds and cleaves diadenosine polyphosphates and functions as a tumor suppressor in human epithelial cancers. Function of Fhit in tumor suppression does not require diadenosine polyphosphate cleavage but correlates with the ability to form substrate complexes. As diadenosine polyphosphates ... More
Spontaneous nucleotide exchange in low molecular weight GTPases by fluorescently labeled gamma-phosphate-linked GTP analogs.
Authors:Korlach J, Baird DW, Heikal AA, Gee KR, Hoffman GR, Webb WW
Journal:Proc Natl Acad Sci U S A
PubMed ID:14973186
Regulated guanosine nucleotide exchange and hydrolysis constitute the fundamental activities of low molecular weight GTPases. We show that three guanosine 5'-triphosphate analogs with BODIPY fluorophores coupled via the gamma phosphate bind to the GTPases Cdc42, Rac1, RhoA, and Ras and displace guanosine 5'-diphosphate with high intrinsic exchange rates in the ... More
Crystal structure of the worm NitFhit Rosetta Stone protein reveals a Nit tetramer binding two Fhit dimers.
Authors:Pace HC, Hodawadekar SC, Draganescu A, Huang J, Bieganowski P, Pekarsky Y, Croce CM, Brenner C
Journal:Curr Biol
PubMed ID:10959838
BACKGROUND: The nucleotide-binding protein Fhit, among the earliest and most frequently inactivated proteins in lung cancer, suppresses tumor formation by inducing apoptosis. In invertebrates, Fhit is encoded as a fusion protein with Nit, a member of the nitrilase superfamily. In mice, the Nit1 and Fhit genes have nearly identical expression ... More
Exploration of the Effects of γ-Phosphate-Modified ATP Analogues on Histidine Kinase Autophosphorylation.
Authors:
Journal:Biochemistry
PubMed ID:29944360