推荐产品
产品名称
双甘肽, BioXtra, ≥99.0% (NT)
产品线
BioXtra
质量水平
方案
≥99.0% (NT)
表单
powder
技术
ligand binding assay: suitable
灼烧残渣
≤0.1% (as SO4)
缺失
≤1% loss on drying, 110 °C
颜色
white
有效pH范围
7.5-8.9
pKa (25 °C)
8.2
mp
220-240 °C (dec.)
溶解性
H2O: 1 M at 20 °C, clear, colorless
痕量阴离子
chloride (Cl-): ≤50 mg/kg
sulfate (SO42-): ≤50 mg/kg
痕量阳离子
Ca: ≤10 mg/kg
Cd: ≤5 mg/kg
Co: ≤5 mg/kg
Cr: ≤5 mg/kg
Cu: ≤5 mg/kg
Fe: ≤5 mg/kg
K: ≤50 mg/kg
Mg: ≤5 mg/kg
Mn: ≤5 mg/kg
Na: ≤50 mg/kg
Ni: ≤5 mg/kg
Pb: ≤5 mg/kg
Zn: ≤5 mg/kg
SMILES字符串
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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生化/生理作用
Glycine is a non-essential amino acid. Influx of calcium through the cell membrane is mediated by glycine-gated channel. Glycine participates in the synthesis of porphyrins, purine and serine. It also serves as a competitive agonist for glutamate in binding to the NMDA (N-methyl-D-aspartate) receptors. Glycine synthesis might be increased in rapidly proliferating cancer cells, due to increased demand for the amino acid. Diglycine is known to catalyze the formation of homo- and hetero dipeptides more efficiently than glycine.
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
dust mask type N95 (US), Eyeshields, Gloves
Glycine and diglycine as possible catalytic factors in the prebiotic evolution of peptides.
Plankensteiner K
Origins of Life and Evolution of the Biosphere : the Journal of the International Society For the Study of the Origin of Life, 32(3), 225-236 (2002)
Metabolite Profiling Identifies a Key Role for Glycine in Rapid Cancer Cell Proliferation
Mohit Jain
Science, 336(6084), 1040-1044 (2012)
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
Francis Impens et al.
Proceedings of the National Academy of Sciences of the United States of America, 111(34), 12432-12437 (2014-08-13)
SUMOylation is an essential ubiquitin-like modification involved in important biological processes in eukaryotic cells. Identification of small ubiquitin-related modifier (SUMO)-conjugated residues in proteins is critical for understanding the role of SUMOylation but remains experimentally challenging. We have set up a
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
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