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
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
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
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
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
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