Product Name
双甘肽, Vetec™, reagent grade, 99%
等级
reagent grade
产品线
Vetec™
方案
99%
表单
powder
技术
ligand binding assay: suitable
颜色
white
有效pH范围
7.5-8.9
pKa (25 °C)
8.2
mp
255-260 °C
SMILES字符串
NCC(=O)NCC(O)=O
InChI
1S/C4H8N2O3/c5-1-3(7)6-2-4(8)9/h1-2,5H2,(H,6,7)(H,8,9)
InChI key
YMAWOPBAYDPSLA-UHFFFAOYSA-N
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法律信息
Vetec is a trademark of Merck KGaA, Darmstadt, Germany
储存分类代码
11 - Combustible Solids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
Sebastian A Wagner et al.
Molecular & cellular proteomics : MCP, 11(12), 1578-1585 (2012-07-14)
Posttranslational modifications of proteins increase the complexity of the cellular proteome and enable rapid regulation of protein functions in response to environmental changes. Protein ubiquitylation is a central regulatory posttranslational modification that controls numerous biological processes including proteasomal degradation of
Daniel H Haft et al.
PloS one, 6(12), e28886-e28886 (2011-12-24)
The rhomboid family of serine proteases occurs in all domains of life. Its members contain at least six hydrophobic membrane-spanning helices, with an active site serine located deep within the hydrophobic interior of the plasma membrane. The model member GlpG
Namrata D Udeshi et al.
Molecular & cellular proteomics : MCP, 12(3), 825-831 (2012-12-26)
Detection of endogenous ubiquitination sites by mass spectrometry has dramatically improved with the commercialization of anti-di-glycine remnant (K-ε-GG) antibodies. Here, we describe a number of improvements to the K-ε-GG enrichment workflow, including optimized antibody and peptide input requirements, antibody cross-linking
P B Armentrout et al.
Journal of the American Society for Mass Spectrometry, 23(4), 621-631 (2011-09-29)
We present a full computational description of the fragmentation reactions of protonated diglycine (H(+)GG). Relaxed potential energy surface scans performed at B3LYP/6-31 G(d) or B3LYP/6-311 + G(d,p) levels are used to map the reaction coordinate surfaces and identify the transition states (TSs) and
Lasse Jenner et al.
Proceedings of the National Academy of Sciences of the United States of America, 110(10), 3812-3816 (2013-02-23)
Here we present an X-ray crystallography structure of the clinically relevant tigecycline antibiotic bound to the 70S ribosome. Our structural and biochemical analysis indicate that the enhanced potency of tigecycline results from a stacking interaction with nucleobase C1054 within the
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