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G8898

Sigma-Aldrich

Glycine

≥99%, suitable for western blotting

Synonym(s):

Aminoacetic acid, Aminoethanoic acid, Glycocoll

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About This Item

Linear Formula:
NH2CH2COOH
CAS Number:
Molecular Weight:
75.07
Beilstein/REAXYS Number:
635782
EC Number:
MDL number:
UNSPSC Code:
12352209
eCl@ss:
32160406
PubChem Substance ID:
NACRES:
NA.28

product name

Glycine, suitable for electrophoresis, ≥99%

assay

≥99%

form

powder

technique(s)

electrophoresis: suitable
western blot: suitable

impurities

≤0.01% Insoluble matter

color

white to off-white

pKa (25 °C)

(1) 2.35, (2) 9.60
2.35

mp

240 °C (dec.) (lit.)

solubility

H2O: 200 mg/mL, clear, colorless to faintly yellow

anion traces

chloride (Cl-): ≤70 ppm

cation traces

heavy metals (as Pb): ≤20 ppm

absorption

≤0.15 at 280 at 1 M

functional group

amine
carboxylic acid

storage temp.

room temp

SMILES string

NCC(O)=O

InChI

1S/C2H5NO2/c3-1-2(4)5/h1,3H2,(H,4,5)

InChI key

DHMQDGOQFOQNFH-UHFFFAOYSA-N

Gene Information

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General description

Glycine is a molecule with pI of 6.7, which is similar to the pH of stacking gel. It has advantage of low mobility, hydrophobicity and it does not associate with proteins. Glycine is a component of Tris-glycine and Tris-glycine-SDS (sodium dodecyl sulfate) running buffers for polyacrylamide gel electrophoresis. Glycine is also a component of Towbin′s transfer buffer for Western blots.
Glycine, an achiral proteinogenic amino acid, serves diverse roles in biochemistry and physiology. As a non-essential, non-polar glucogenic amino acid, it acts as an inhibitory neurotransmitter in the central nervous system and co-agonist at NMDA receptors with glutamate. Serving as a precursor, glycine is a crucial building block for macromolecules, playing a vital role in cellular processes.

In addition to its biological functions, glycine exhibits versatility in research applications. Its role as a biochemical reagent makes it valuable in assays and procedures, while its buffering capacity is essential in techniques like SDS-PAGE, Western Blotting, chromatography, and cell culture. Glycine′s zwitterionic nature makes it an effective buffer across various pH values, widely used in immunology research for buffer preparation in techniques such as Western Blotting. Compatible with enzymes, glycine is useful in enzymatic assays like lactate determination. Moreover, glycine contributes to buffer formulations for protein stabilization, pH control, and enzymatic reactions.

Application

  • Glycine has been used for the preparation of gelatin composites scaffold.
  • It has been used in the elution buffer to extract protein using HiTrap protein G column.
  • It has been used in the SDS-sample, running and transfer buffers prepared for SDS-PAGE (sodium dodecyl sulfate polyacrylamide gel electrophoresis) and western blotting.

Biochem/physiol Actions

Inhibitory neurotransmitter in spinal cord, allosteric regulator of NMDA receptors.

Features and Benefits

  • Suitable for Cell Biology and Biochemical studies
  • High-quality compound suitable for multiple research applications

Analysis Note

Tested for use in electrode buffers for PAGE and in transfer buffers for Western blots.

Other Notes

For additional information on our range of Biochemicals, please complete this form.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


Certificates of Analysis (COA)

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Quantitative immunofluorescent blotting of the multidrug resistance-associated protein 2 (MRP2).
Gerk PM
Journal of Pharmacological and Toxicological Methods, 63, 279-279 (2011)
Hames, B.D. and Rickwood, D.
Gel Electrophoresis of Proteins: A Practical Approach, 32-35 (1990)
The role of muscle-derived stem cells in bone tissue engineering.
Sun JS et al.
Biomaterials, 26, 3953-3953 (2005)
The newly developed monoclonal antibody SA7D6 exhibits potential for detection of Staphylococcus aureus.
Senevirathne A and Kim K-P
Food Science and Biotechnology, 24, 1177-1184 (2015)
H Towbin et al.
Proceedings of the National Academy of Sciences of the United States of America, 76(9), 4350-4354 (1979-09-01)
A method has been devised for the electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets. The method results in quantitative transfer of ribosomal proteins from gels containing urea. For sodium dodecyl sulfate gels, the original band pattern was

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