G3915

Sigma-Aldrich

Gly-Gly

BioPerformance Certified, suitable for cell culture, ≥99%

Synonym(s):
Diglycine, Glycyl-glycine
Linear Formula:
NH2CH2CONHCH2COOH
CAS Number:
Molecular Weight:
132.12
Beilstein/REAXYS Number:
1765223
EC Number:
MDL number:
PubChem Substance ID:
NACRES:
NA.25
Pricing and availability is not currently available.

grade

BioPerformance Certified

assay

≥99%

form

powder

application(s)

cell culture | mammalian: suitable

impurities

endotoxin and total aerobic microbial count, tested

color

white

useful pH range

7.5 - 8.9

pKa (25 °C)

8.2

mp

255-260 °C

cation traces

heavy metals (as Pb): ≤5 ppm

Featured Industry

Diagnostic Assay Manufacturing

foreign activity

DNase, RNase, NICKase and protease, none detected

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

Gene Information

human ... SLC15A1(6564)

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Personal Protective Equipment

dust mask type N95 (US),Eyeshields,Gloves

Hazard Codes

Xi

Risk Statement

36

Safety Statement

26

RIDADR

NONH for all modes of transport

WGK Germany

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

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...
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...
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...
Woong Kim et al.
Molecular cell, 44(2), 325-340 (2011-09-13)
Despite the diverse biological pathways known to be regulated by ubiquitylation, global identification of substrates that are targeted for ubiquitylation has remained a challenge. To globally characterize the human ubiquitin-modified proteome (ubiquitinome), we utilized a monoclonal antibody that recognizes diglycine...
Sartaj Tabassum et al.
Dalton transactions (Cambridge, England : 2003), 41(16), 4955-4964 (2012-03-13)
To evaluate the biological preference of metallopeptide drugs in cancer cells, a new dinuclear copper(II) complex [Cu(2)(glygly)(2)(ppz)(H(2)O)(4)]·2H(2)O (1) (glygly = glycyl glycine anion and ppz = piperazine), was designed and synthesized as topoisomerase I inhibitor. The structural elucidation of the...

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