ADP-TAMRA conjugate [5-TAMRA-eda-ADP]

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Chemical structure for ADP-TAMRA conjugate [5-TAMRA-eda-ADP]
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Unit Size: Cat No: Price (USD): Qty:
100 nmol 13606 $495


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Overview

Ex/Em (nm)552/578
MW1309.30
SolventDMSO
Storage Freeze (<-15 °C)
Minimize light exposure
Category Enzyme Detection
Phosphodiesterases
Related
Fluorescently labeled ADP molecules are used to screening ADP-binding enzymes and other protein targets for drug discovery. This ADP-TAMRA has been tested for binding kynurenine monooxygenase (KMO) with a K(d) value of 0.60 ± 0.05 ?M and to the NMOs from Aspergillus fumigatus and Mycobacterium smegmatis with K(d) values of 2.1 ± 0.2 and 4.0 ± 0.2 ?M, respectively (Anal Biochem. 2012, 425, 80-7). The assay was tested in competitive binding experiments with substrates and products of KMO and an NMO. NMOs are essential for pathogenesis in fungi and bacteria. NMOs catalyze the hydroxylation of sine and ornithine in the biosynthesis of hydroxamate-containing siderophores. Inhibition of KMO, which catalyzes the conversion of kynurenine to 3-hydroxykynurenine, alleviates neurodegenerative disorders such as Huntington's and Alzheimer's diseases and brain infections caused by the parasite Trypanosoma brucei.




Calculators
Common stock solution preparation

Table 1. Volume of DMSO needed to reconstitute specific mass of ADP-TAMRA conjugate [5-TAMRA-eda-ADP] to given concentration. Note that volume is only for preparing stock solution. Refer to sample experimental protocol for appropriate experimental/physiological buffers.



Molarity calculator

Table 2. Enter any two values (mass, volume, concentration) to calculate the third.

Mass Molecular weight Volume Concentration Moles
/ = x =
 






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References

Deciphering the catalysis-associated conformational changes of human adenylate kinase 1 with single-molecule spectroscopy
Authors: Lin CY, Huang JY, Lo LW.
Journal: J Phys Chem B (2013): 13947

The effect of NBD-Cl in nucleotide-binding of the major subunit alpha and B of the motor proteins F1FO ATP synthase and A1AO ATP synthase
Authors: Hunke C, Tadwal VS, Manimekalai MS, Roessle M, Gruber G.
Journal: J Bioenerg Biomembr (2010): 1

The Escherichia coli PriA helicase-double-stranded DNA complex: location of the strong DNA-binding subsite on the helicase domain of the protein and the affinity control by the two nucleotide-binding sites of the enzyme
Authors: Szymanski MR, Jezewska MJ, Bujalowski W.
Journal: J Mol Biol (2010): 344

ATP/ADP binding to a novel nucleotide binding domain of the reticulocyte-binding protein Py235 of Plasmodium yoelii
Authors: Ramalingam JK, Hunke C, Gao X, Gruber G, Preiser PR.
Journal: J Biol Chem (2008): 36386

Reversal of ADP-mediated aggregation of adenosine kinase by cyclophilin leads to its reactivation
Authors: Sen B, Chakraborty A, Datta R, Bhattacharyya D, Datta AK.
Journal: Biochemistry (2006): 263

ATPase mechanism of Eg5 in the absence of microtubules: insight into microtubule activation and allosteric inhibition by monastrol
Authors: Cochran JC, Gilbert SP.
Journal: Biochemistry (2005): 16633

Ca2+ binding to sarcoplasmic reticulum ATPase phosphorylated by Pi reveals four thapsigargin-sensitive Ca2+ sites in the presence of ADP
Authors: Vieyra A, Mintz E, Lowe J, Guillain F.
Journal: Biochim Biophys Acta (2004): 103

Evidence for proximal cysteine and lysine residues at or near the active site of arginine kinase of Stichopus japonicus
Authors: Guo Q, Chen B, Wang X.
Journal: Biochemistry (Mosc) (2004): 1336

Conformational dynamics of DnaB helicase upon DNA and nucleotide binding: analysis by intrinsic tryptophan fluorescence quenching
Authors: Flowers S, Biswas EE, Biswas SB.
Journal: Biochemistry (2003): 1910

D1 ring is stable and nucleotide-independent, whereas D2 ring undergoes major conformational changes during the ATPase cycle of p97-VCP
Authors: Wang Q, Song C, Yang X, Li CC.
Journal: J Biol Chem (2003): 32784


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