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Bio-Synthesis provide two types of nitroxide spin labels. Short chain TEMPO and long linker TEMPO-TEG for site directed spin lableling (SDSL) application. These two compound can be conjugated to oligonucleotide via chick chemistry. Spin labels are molecules containing sites with unpaired electrons, usually stable nitroxide free radicals, and generate a paramagnetic center that can be probed using magnetic resonance spectroscopy. Electron Paramagnetic Resonance (EPR) spectroscopy is a sensitive technique for the characterization of materials and has been used to determine the molecular environment of spin labels1,2, including the location, orientation and motion of spin labels within biomolecules. Most naturally occurring biomolecules do not contain unpaired electrons. Consequently, spin labels localized within biomolecules can act as bioorthogonal chemical reporters for studying the structure and dynamics of biomolecules using EPR spectroscopy.

Recently, the spin label 2,2,6,6- tetramethylpiperidine 1-oxyl (TEMPO) has been used to determine RNA structure using paramagnetic relaxation enhancement (PRE).3 Spin labels can be easily incorporated into biomolecules by covalent attachment using Click Chemistry. The wide variety of alkyne modifications already available from Bio-Synthesis for site-specific conjugation of spin labels to oligonucleotides.

Product Information

 

Product Name:

TEMPO-TEG Spin Label Olligo Modification

Category:

Spin Label; click chemistry

Modification Code:

[TEMPO-TEG]

Purification:

HPLC or PAGE

Delivery Format:

Lyophilized

Shipping Conditions:

Room Temperature

Storage Conditions:

-20°C To -70°C
Oligonucleotides are stable in solution at 4°C for up to 2 weeks. Properly reconstituted material stored at -20°C should be stable for at least 6 months. Dried DNA (when kept at -20°C) in a nuclease-free environment should be stable for years.


References/Citations:

1. S.A. Shelke, and S. Sigurdsson, European Journal of Organic Chemistry, 2012, 2291-2301.

2. I.D. Sahu, R.M. McCarrick, and G.A. Lorigan, Biochemistry, 2013, 52, 5967-5984.

3. C.H. Wunderlich, et al., ACS Chem Biol, 2013, In Press.