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

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Physical properties
Molecular weight1309.30
SolventDMSO
Spectral properties
Correction Factor (260 nm)0.32
Correction Factor (280 nm)0.178
Extinction coefficient (cm -1 M -1)90000
Excitation (nm)552
Emission (nm)578
Storage, safety and handling
H-phraseH303, H313, H333
Hazard symbolXN
Intended useResearch Use Only (RUO)
R-phraseR20, R21, R22
StorageFreeze (< -15 °C); Minimize light exposure
UNSPSC12352200

OverviewpdfSDSpdfProtocol


Molecular weight
1309.30
Correction Factor (260 nm)
0.32
Correction Factor (280 nm)
0.178
Extinction coefficient (cm -1 M -1)
90000
Excitation (nm)
552
Emission (nm)
578
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.

0.1 mg0.5 mg1 mg5 mg10 mg
1 mM76.377 µL381.883 µL763.767 µL3.819 mL7.638 mL
5 mM15.275 µL76.377 µL152.753 µL763.767 µL1.528 mL
10 mM7.638 µL38.188 µL76.377 µL381.883 µL763.767 µL

Molarity calculator

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Spectrum


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spectrum

Spectral properties

Correction Factor (260 nm)0.32
Correction Factor (280 nm)0.178
Extinction coefficient (cm -1 M -1)90000
Excitation (nm)552
Emission (nm)578

Product Family


NameExcitation (nm)Emission (nm)Extinction coefficient (cm -1 M -1)Correction Factor (260 nm)Correction Factor (280 nm)
ATP-TAMRA conjugate [5-TAMRA-eda-ATP]552578900000.320.178

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References


View all 32 references: Citation Explorer
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 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
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
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
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
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