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)
Citations & References (4)
Invitrogen™

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

BODIPY™ FL ATP-γ-S binds to ATP-binding proteins. To create this fluorescent nucleotide, the BODIPY FL fluorophore was linked through theRead more
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Catalog NumberQuantity
A2218450 μL
Catalog number A22184
Price (EUR)
1.018,00
Each
Add to cart
Quantity:
50 μL
Price (EUR)
1.018,00
Each
Add to cart
BODIPY™ FL ATP-γ-S binds to ATP-binding proteins. To create this fluorescent nucleotide, the BODIPY FL fluorophore was linked through the γ-thiol of ATP-γ-S. In addition to its potential use for binding studies, the BODIPY FL ATP-γ-S thioether is an important new substrate for Fhit, a member of the histidine triad superfamily of nucleotide-binding proteins.
For Research Use Only. Not for use in diagnostic procedures.
Specifications
Label or DyeBODIPY™ FL
Product TypeFL ATP-gamma-S Thioester
Quantity50 μL
Shipping ConditionWet Ice
Concentration5 mM
Product LineBODIPY
Unit SizeEach
Contents & Storage
Store in freezer -5°C to -30°C and protect from light.

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