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5(6)-TAMRA C6 maleimide

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Physical properties
Molecular weight623.65
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
UNSPSC12171501

OverviewpdfSDSpdfProtocol


Molecular weight
623.65
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
5(6)-TAMRA C6 maleimide is an excellent replacement for tetramethylrhodamine-5-(and 6)-maleimide. It selectively reacts with thiol groups of peptides, proteins and other biological molecules (such as thiol-modified oligonucleotides and small thiol-containing organic molecules). It might give higher conjugation yield than tetramethylrhodamine-5-(and 6)-maleimide under similar conjugation conditions. 5(6)-TMR C6 maleimide has the spectral properties identical to those of tetramethylrhodamine-5-(and 6)-maleimide, thus all the instrument settings of the tetramethylrhodamine-5-(and 6)-maleimide would be applicable to the applications of 5-TMR C6 maleimide conjugates.

Calculators


Common stock solution preparation

Table 1. Volume of DMSO needed to reconstitute specific mass of 5(6)-TAMRA C6 maleimide 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 mM160.346 µL801.732 µL1.603 mL8.017 mL16.035 mL
5 mM32.069 µL160.346 µL320.693 µL1.603 mL3.207 mL
10 mM16.035 µL80.173 µL160.346 µL801.732 µL1.603 mL

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

Images


Citations


View all 1 citations: Citation Explorer
Detection and destruction of HER2-positive cancer cells by Ultra Quenchbody-siRNA complex
Authors: Dong, Jinhua and Oka, Yuya and Jeong, Hee-Jin and Ohmuro-Matsuyama, Yuki and Ueda, Hiroshi
Journal: Biotechnology and Bioengineering (2020): 1259--1269

References


View all 21 references: Citation Explorer
Severing of F-actin by yeast cofilin is pH-independent
Authors: Pavlov D, Muhlrad A, Cooper J, Wear M, Reisler E.
Journal: Cell Motil Cytoskeleton (2006): 533
Fluorometric measurements of intermolecular distances between the alpha and beta subunits of the Na+/K+-ATPase
Authors: Dempski RE, Hartung K, Friedrich T, Bamberg E.
Journal: J Biol Chem. (2006)
4-aminopyridine prevents the conformational changes associated with P/C-type inactivation in Shaker channels
Authors: Claydon TW, Vaid M, Rezazadeh S, Kehl SJ, Fedida D.
Journal: J Pharmacol Exp Ther. (2006)
Both rotor and stator subunits are necessary for efficient binding of F1 to F0 in functionally assembled Escherichia coli ATP synthase
Authors: Krebstakies T, Zimmermann B, Graber P, Altendorf K, Borsch M, Greie JC.
Journal: J Biol Chem (2005): 33338
The beta subunit of the Na+/K+-ATPase follows the conformational state of the holoenzyme
Authors: Dempski RE, Friedrich T, Bamberg E.
Journal: J Gen Physiol (2005): 505
Perturbation analysis of the voltage-sensitive conformational changes of the Na+/glucose cotransporter
Authors: Loo DD, Hirayama BA, Cha A, Bezanilla F, Wright EM.
Journal: J Gen Physiol (2005): 13
Cytochrome c conformations resolved by the photon counting histogram: watching the alkaline transition with single-molecule sensitivity
Authors: Perroud TD, Bokoch MP, Zare RN.
Journal: Proc Natl Acad Sci U S A (2005): 17570
Membrane topology of loop 13-14 of the Na+/glucose cotransporter (SGLT1): a SCAM and fluorescent labelling study
Authors: Gagnon DG, Holt A, Bourgeois F, Wallendorff B, Coady MJ, Lapointe JY.
Journal: Biochim Biophys Acta (2005): 173
Distances between tropomyosin sites across the muscle thin filament using luminescence resonance energy transfer: evidence for tropomyosin flexibility
Authors: Chen Y, Lehrer SS.
Journal: Biochemistry (2004): 11491
Crystal structure of monomeric actin in the ATP state. Structural basis of nucleotide-dependent actin dynamics
Authors: Graceffa P, Dominguez R.
Journal: J Biol Chem (2003): 34172