Rockville, MD/Seattle, WA ?May 11, 2010 ?OriGene and the Institute for Systems Biology (ISB), announce plans to create a proteotypic PeptideAtlas and develop an SRM/MRM mass spectrometry standard database for 5,000 human proteins (Press Release)
> 80% as determined by SDS-PAGE and Coomassie blue staining
Concentration:
> 50 ug/ml as determined by BCA
Labeling Method:
Labeled with [U- 13C6, 15N4]-L-Arginine and [U- 13C6, 15N2]-L-Lysine
Labeling Efficiency:
> 90% incorporation
Buffer and Storage:
100 mM glycine, 25 mM Tris-HCl, pH 7.3. Store at -80C. Avoid repeated freeze-thaw cycles. Stable for 3 months from receipt of products under proper storage and handling conditions.
*: DDK-tag is the same as FLAG tag. Flag® is a registered trademark of Sigma-Aldrich
Summary: Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Because of their central role in linking amino acids with nucleotide triplets contained in tRNAs, aminoacyl-tRNA synthetases are thought to be among the first proteins that appeared in evolution. In metazoans, 9 aminoacyl-tRNA synthetases specific for glutamine (gln), glutamic acid (glu), and 7 other amino acids are associated within a multienzyme complex. Although present in eukaryotes, glutaminyl-tRNA synthetase (QARS) is absent from many prokaryotes, mitochondria, and chloroplasts, in which Gln-tRNA(Gln) is formed by transamidation of the misacylated Glu-tRNA(Gln). Glutaminyl-tRNA synthetase belongs to the class-I aminoacyl-tRNA synthetase family. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2013].
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