608297
ISOGRO®-13C,15N,D Powder -Growth Medium
98 atom % 15N, 97-99 atom % D, 99 atom % 13C
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About This Item
Isotopic purity:
99 atom % 13C, 98 atom % 15N, 97-99 atom % D
Form:
solid
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
Quality Level
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.
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
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)
Brendan C Mullaney et al.
Cell metabolism, 12(4), 398-410 (2010-10-05)
Acyl-CoA synthases are important for lipid synthesis and breakdown, generation of signaling molecules, and lipid modification of proteins, highlighting the challenge of understanding metabolic pathways within intact organisms. From a C. elegans mutagenesis screen, we found that loss of ACS-3, a long-chain
Claire Rosnoblet et al.
The Journal of biological chemistry, 287(53), 44249-44260 (2012-11-16)
Nonstructural protein 5B (NS5B) is essential for hepatitis C virus (HCV) replication as it carries the viral RNA-dependent RNA polymerase enzymatic activity. HCV replication occurs in a membrane-associated multiprotein complex in which HCV NS5A and host cyclophilin A (CypA) have
Melanie H Smith et al.
The Journal of biological chemistry, 289(37), 25670-25677 (2014-08-03)
A substantial fraction of nascent proteins delivered into the endoplasmic reticulum (ER) never reach their native conformations. Eukaryotes use a series of complementary pathways to efficiently recognize and dispose of these terminally misfolded proteins. In this process, collectively termed ER-associated
Tobias S Ulmer et al.
The Journal of biological chemistry, 280(10), 9595-9603 (2004-12-24)
Misfolding of the protein alpha-synuclein (aS), which associates with presynaptic vesicles, has been implicated in the molecular chain of events leading to Parkinson's disease. Here, the structure and dynamics of micelle-bound aS are reported. Val3-Val37 and Lys45-Thr92 form curved alpha-helices
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