Calculator
ADP-TAMRA conjugate [5-TAMRA-eda-ADP]
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 mg | 0.5 mg | 1 mg | 5 mg | 10 mg | |
| 1 mM | 76.377 µL | 381.883 µL | 763.767 µL | 3.819 mL | 7.638 mL |
| 5 mM | 15.275 µL | 76.377 µL | 152.753 µL | 763.767 µL | 1.528 mL |
| 10 mM | 7.638 µL | 38.188 µL | 76.377 µL | 381.883 µL | 763.767 µL |
Molarity calculator
Enter any two values (mass, volume, concentration) to calculate the third.
| Mass (Calculate) | Molecular weight | Volume (Calculate) | Concentration (Calculate) | Moles | ||||
| / | = | x | = |
Spectrum
Product family
| Name | Excitation (nm) | Emission (nm) | Extinction coefficient (cm -1 M -1) | Correction Factor (260 nm) | Correction Factor (280 nm) |
| ATP-TAMRA conjugate [5-TAMRA-eda-ATP] | 552 | 578 | 90000 | 0.32 | 0.178 |
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
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
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
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
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
Authors: Sen B, Chakraborty A, Datta R, Bhattacharyya D, Datta AK.
Journal: Biochemistry (2006): 263
Page updated on December 17, 2024
Safety data sheet