추천 제품
제품명
Gly-Gly, Vetec™, reagent grade, 99%
Grade
reagent grade
제품 라인
Vetec™
분석
99%
양식
powder
기술
ligand binding assay: suitable
색상
white
유용한 pH 범위
7.5-8.9
pKa(25 °C)
8.2
mp
255-260 °C
SMILES string
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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법적 정보
Vetec is a trademark of Merck KGaA, Darmstadt, Germany
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point (°F)
Not applicable
Flash Point (°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
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
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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