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Merck

50200

Gly-Gly

≥99.0% (NT), suitable for ligand binding assays, BioXtra

Synonym(s):

Diglycine, Glycyl-glycine

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About This Item

Linear Formula:
NH2CH2CONHCH2COOH
CAS Number:
Molecular Weight:
132.12
NACRES:
NA.25
PubChem Substance ID:
UNSPSC Code:
12161700
EC Number:
209-127-8
MDL number:
Beilstein/REAXYS Number:
1765223
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Product Name

Gly-Gly, BioXtra, ≥99.0% (NT)

product line

BioXtra

Quality Level

assay

≥99.0% (NT)

form

powder

technique(s)

ligand binding assay: suitable

ign. residue

≤0.1% (as SO4)

loss

≤1% loss on drying, 110 °C

color

white

useful pH range

7.5-8.9

pKa (25 °C)

8.2

mp

220-240 °C (dec.)

solubility

H2O: 1 M at 20 °C, clear, colorless

anion traces

chloride (Cl-): ≤50 mg/kg, sulfate (SO42-): ≤50 mg/kg

cation traces

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 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

Biochem/physiol Actions

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.


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Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

dust mask type N95 (US), Eyeshields, Gloves



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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)
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