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606863

Sigma-Aldrich

ISOGRO®-13C Powder -Growth Medium

99 atom % 13C

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About This Item

Numéro MDL:
MFCD00197703
Code UNSPSC :
12352200
Nomenclature NACRES :
NA.12

Pureté isotopique

99 atom % 13C

Niveau de qualité

200

Forme

solid

Technique(s)

bio NMR: suitable
protein expression: suitable

Température de stockage

−20°C

Description générale

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 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.

Conditionnement

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.

Informations légales

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

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

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Certificats d'analyse (COA)

Lot/Batch Number
CC0069
CX1137
TJ1748
10556AE

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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
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
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
I Kilpelainen et al.
The Journal of biological chemistry, 275(18), 13564-13570 (2000-05-02)
Heparin-binding growth-associated molecule (HB-GAM) is an extracellular matrix-associated protein implicated in the development and plasticity of neuronal connections of brain. Binding to cell surface heparan sulfate is indispensable for the biological activity of HB-GAM. In the present paper we have
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Articles

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

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

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