V900403
双甘肽
99%, Vetec™
别名:
二甘氨酸, 甘氨酰-甘氨酸
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线性分子式:
NH2CH2CONHCH2COOH
化学文摘社编号:
分子量:
132.12
UNSPSC Code:
12352209
PubChem Substance ID:
EC Number:
209-127-8
Beilstein/REAXYS Number:
1765223
MDL number:
产品名称
双甘肽, Vetec™, reagent grade, 99%
form
powder
InChI key
YMAWOPBAYDPSLA-UHFFFAOYSA-N
InChI
1S/C4H8N2O3/c5-1-3(7)6-2-4(8)9/h1-2,5H2,(H,6,7)(H,8,9)
SMILES string
NCC(=O)NCC(O)=O
grade
reagent grade
product line
Vetec™
assay
99%
technique(s)
ligand binding assay: suitable
color
white
useful pH range
7.5-8.9
pKa (25 °C)
8.2
mp
255-260 °C
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Legal Information
Vetec is a trademark of Merck KGaA, Darmstadt, Germany
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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
P B Armentrout et al.
Journal of the American Society for Mass Spectrometry, 23(4), 632-643 (2011-09-29)
We present a full molecular description of fragmentation reactions of protonated diglycine (H(+)GG) by studying their collision-induced dissociation (CID) with Xe using a guided ion beam tandem mass spectrometer (GIBMS). Analysis of the kinetic energy-dependent CID cross sections provides the
Daisy Bustos et al.
Molecular & cellular proteomics : MCP, 11(12), 1529-1540 (2012-06-26)
Advances in high resolution tandem mass spectrometry and peptide enrichment technologies have transformed the field of protein biochemistry by enabling analysis of end points that have traditionally been inaccessible to molecular and biochemical techniques. One field benefitting from this research
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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