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Sigma-Aldrich

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

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

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About This Item

MDL number:
UNSPSC Code:
12352200
NACRES:
NA.12

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

Related Categories

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

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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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)
Ara Celi DiCostanzo et al.
The Journal of biological chemistry, 287(33), 27997-28006 (2012-06-29)
Light chain amyloidosis is an incurable protein misfolding disease where monoclonal immunoglobulin light chains misfold and deposit as amyloid fibrils, causing organ failure and death. Previously, we determined that amyloidogenic light chains AL-09 and AL-103 do not form fibrils at
Nicholas C Fitzkee et al.
The Journal of biological chemistry, 285(23), 18072-18084 (2010-04-07)
The human immunodeficiency virus type 1 (HIV-1) integrase (IN) is a critical enzyme involved in infection. It catalyzes two reactions to integrate the viral cDNA into the host genome, 3' processing and strand transfer, but the dynamic behavior of the
J L Urbauer et al.
The Journal of biological chemistry, 276(44), 41128-41132 (2001-08-24)
The association of the bacteriophage T4-encoded AsiA protein with the final sigma(70) subunit of the Escherichia coli RNA polymerase is one of the principal events governing transcription of the T4 genome. Analytical ultracentrifugation and NMR studies indicate that free AsiA
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

Articles

Utilizing ISOGRO® Supplementation of M9 Minimal Media to Enhance Recombinant Protein Expression.

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