推荐产品
方案
≥98.0%
表单
solid
反应适用性
reaction type: solution phase peptide synthesis
mp
149-151 °C
应用
peptide synthesis
储存温度
2-8°C
SMILES字符串
OC(=O)CNC=O
InChI
1S/C3H5NO3/c5-2-4-1-3(6)7/h2H,1H2,(H,4,5)(H,6,7)
InChI key
UGJBHEZMOKVTIM-UHFFFAOYSA-N
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储存分类代码
11 - Combustible Solids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, type N95 (US)
历史批次信息供参考:
分析证书(COA)
Lot/Batch Number
Annette Sievers et al.
Proceedings of the National Academy of Sciences of the United States of America, 101(21), 7897-7901 (2004-05-14)
To determine the effectiveness of the ribosome as a catalyst, we compared the rate of uncatalyzed peptide bond formation, by the reaction of the ethylene glycol ester of N-formylglycine with Tris(hydroxymethyl)aminomethane, with the rate of peptidyl transfer by the ribosome.
S Kumar et al.
Journal of enzyme inhibition, 13(5), 369-376 (1998-10-30)
N-formylglycine was developed as a dead-end inhibitor of the succinic semialdehyde dehydrogenase reaction. At 4 mM, it inhibited Aspergillus niger succinic semialdehyde dehydrogenase by 40%. N-formylglycine is a reversible, complete inhibitor; the inhibition is competitive with succinic semialdehyde and uncompetitive
Einar Sagstuen et al.
The journal of physical chemistry. A, 110(28), 8653-8662 (2006-07-14)
Single crystals of the 1:1 complex of the nucleic acid base cytosine and the dipeptide N-formylglycine (C.NFG) have been irradiated at 10 and 273 K to doses of about 70 kGy and studied at temperatures between 10 and 293 K
Stefanie Jonas et al.
Journal of molecular biology, 384(1), 120-136 (2008-09-17)
The alkaline phosphatase superfamily comprises a large number of hydrolytic metalloenzymes such as phosphatases and sulfatases. We have characterised a new member of this superfamily, a phosphonate monoester hydrolase/phosphodiesterase from Rhizobium leguminosarum (R/PMH) both structurally and kinetically. The 1.42 A
Brian L Carlson et al.
The Journal of biological chemistry, 283(29), 20117-20125 (2008-04-09)
Type I sulfatases require an unusual co- or post-translational modification for their activity in hydrolyzing sulfate esters. In eukaryotic sulfatases, an active site cysteine residue is oxidized to the aldehyde-containing C(alpha)-formylglycine residue by the formylglycine-generating enzyme (FGE). The machinery responsible
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