InChI
1S/C5H10N2O3/c1-3(5(9)10)7-4(8)2-6/h3H,2,6H2,1H3,(H,7,8)(H,9,10)/t3-/m0/s1
InChI key
VPZXBVLAVMBEQI-VKHMYHEASA-N
SMILES string
C[C@H](NC(=O)CN)C(O)=O
storage temp.
−20°C
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存储类别
13 - Non Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
法规信息
新产品
此项目有
Sebastien Apcher et al.
PLoS pathogens, 6(10), e1001151-e1001151 (2010-10-27)
Viruses are known to employ different strategies to manipulate the major histocompatibility (MHC) class I antigen presentation pathway to avoid recognition of the infected host cell by the immune system. However, viral control of antigen presentation via the processes that
Juraj Bujdák et al.
Journal of peptide science : an official publication of the European Peptide Society, 10(12), 731-737 (2005-01-07)
Mechanisms of the reactions of representative dipeptides (Gly2, Gly-Ala), oligopeptides (Gly3, Gly4) and the polypeptide (poly-Gly)n) in solution and clay suspensions at 85 degrees C were investigated. The reaction products and their yields were analysed and determined by means of
Stijn Heessen et al.
Proceedings of the National Academy of Sciences of the United States of America, 99(3), 1532-1537 (2002-01-24)
Functional inactivation of the tumor suppressor protein p53 by accelerated ubiquitin/proteasome-dependent proteolysis is a common event in tumor progression. Proteasomal degradation is inhibited by the Gly-Ala repeat (GAr) of the Epstein-Barr virus nuclear antigen-1, which acts as a transferable element
J Rabone et al.
Science (New York, N.Y.), 329(5995), 1053-1057 (2010-08-28)
Porous materials find widespread application in storage, separation, and catalytic technologies. We report a crystalline porous solid with adaptable porosity, in which a simple dipeptide linker is arranged in a regular array by coordination to metal centers. Experiments reinforced by
P R Tulip et al.
The Journal of chemical physics, 131(1), 015103-015103 (2009-07-10)
We investigate the structure of the glycyl-l-alanine dipeptide in aqueous solution at a 1:20 peptide:water concentration via classical, atomistic molecular dynamics simulations using the CHARMM22 force field, and compare to recent neutron diffraction data [S. E. McLain, A. K. Soper
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