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Merck

608297

ISOGRO®-13C,15N,D Powder -Growth Medium

98 atom % 15N, 97-99 atom % D, 99 atom % 13C

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UNSPSC Code:
12352200
NACRES:
NA.12
MDL number:
Isotopic purity:
99 atom % 13C, 98 atom % 15N, 97-99 atom % D
Form:
solid
Servicio técnico
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Quality Level

isotopic purity

99 atom % 13C, 98 atom % 15N, 97-99 atom % D

form

solid

technique(s)

bio NMR: suitable, protein expression: suitable

storage temp.

−20°C

General description

ISOGRO® media is required for overcoming the growth limitations of minimal media. ISOGRO products are lysates of algae grown with stable isotopes (13C, 15N, and/or D). ISOGRO®-13C,15N,D powder -growth medium gives uniform labeling for protein expression NMR (nuclear magnetic resonance) studies.
A typical algal lysate (ISOGRO medium) contains: 30% salts, 3% water, 2% glucose and 65% amino acids/peptides.

Application

ISOGRO®-13C,15N,D Powder -Growth Medium has been used for the generation of isotopically labeled recombinant tau to identify multiple phosphorylations in tau by NMR (nuclear magnetic resonance) spectroscopy.

Packaging

This product may be available from bulk stock and can be packaged on demand. For information on pricing, availability and packaging, please contact Stable Isotopes Customer Service.

Legal Information

ISOGRO is a registered trademark of Merck KGaA, Darmstadt, Germany


Clase de almacenamiento

11 - Combustible Solids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable



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Contenido relacionado

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Instructions

ISOGRO Complex Growth Media


Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins.
Danis C, et al.
Journal of Visualized Experiments, 118, doi: 10-doi: 10 (2016)
Alexandria N Richart et al.
The Journal of biological chemistry, 287(22), 18730-18737 (2012-04-12)
The chromoshadow domain (CSD) of heterochromatin protein 1 (HP1) was recently shown to contribute to chromatin binding and transcriptional regulation through interaction with histone H3. Here, we demonstrate the structural basis of this interaction for the CSD of HP1α. This
Christian Koehler et al.
The Journal of biological chemistry, 286(17), 14842-14851 (2011-03-04)
NarE is a 16 kDa protein identified from Neisseria meningitidis, one of the bacterial pathogens responsible for meningitis. NarE belongs to the family of ADP-ribosyltransferases (ADPRT) and catalyzes the transfer of ADP-ribose moieties to arginine residues in target protein acceptors.