5(6)-TAMRA Maleimide [Tetramethylrhodamine-5-(and-6)-maleimide] Mixed isomers

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Physical properties

Molecular weight	481.51
Solvent	DMSO

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-phrase	H303, H313, H333
Hazard symbol	XN
Intended use	Research Use Only (RUO)
R-phrase	R20, R21, R22
Storage	Freeze (< -15 °C); Minimize light exposure
UNSPSC	12171501

Overview SDS Protocol

Molecular weight

481.51

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

Tetramethylrhodamine-5-(and-6)-maleimide is an excellent reagent for preparing orange fluorescent bioconjugates through thiol modifications of peptides, nucleotides, nucleic acids and proteins. Maleimides are among the most frequently used reagents for thiol modification. In most proteins, the sites of reactions are at cysteine residues that either are intrinsically present or result from reduction of cystines. Unlike iodoacetamides, maleimides do not react with histidines and methionines under physiological conditions.

Calculators

Common stock solution preparation

Table 1. Volume of DMSO needed to reconstitute specific mass of 5(6)-TAMRA Maleimide [Tetramethylrhodamine-5-(and-6)-maleimide] *Mixed isomers* 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	207.68 µL	1.038 mL	2.077 mL	10.384 mL	20.768 mL
5 mM	41.536 µL	207.68 µL	415.36 µL	2.077 mL	4.154 mL
10 mM	20.768 µL	103.84 µL	207.68 µL	1.038 mL	2.077 mL

Molarity calculator

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Mass (Calculate)		Molecular weight		Volume (Calculate)		Concentration (Calculate)		Moles
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Spectrum

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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

Name	Excitation (nm)	Emission (nm)	Extinction coefficient (cm ^-1 M ^-1)	Correction Factor (260 nm)	Correction Factor (280 nm)
5(6)-TAMRA, SE [5-(and-6)-Carboxytetramethylrhodamine, succinimidyl ester] CAS 246256-50-8	552	578	90000	0.32	0.178
5(6)-TAMRA ethylenediamine	552	578	90000	0.32	0.178
5(6)-TAMRA cadaverine	552	578	90000	0.32	0.178
5-TAMRA C6 maleimide	552	578	90000	0.32	0.178
6-TAMRA C6 maleimide	552	578	90000	0.32	0.178

Images

Figure 1. Chemical structure for 5(6)-TAMRA Maleimide [Tetramethylrhodamine-5-(and-6)-maleimide] *Mixed isomers*

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