608297
ISOGRO®-13C,15N,D Powder -Growth Medium
98 atom % 15N, 97-99 atom % D, 99 atom % 13C
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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.
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 Code
11 - Combustible Solids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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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
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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
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
Articles
Utilizing ISOGRO® Supplementation of M9 Minimal Media to Enhance Recombinant Protein Expression.
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