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  • Brand : BIOFRON

  • Catalogue Number : BF-G3003

  • Specification : 98%

  • CAS number : 56-40-6

  • Formula : C2H5NO2

  • Molecular Weight : 75.07

  • PUBCHEM ID : 750

  • Volume : 100mg

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Catalogue Number


Analysis Method






Molecular Weight



White crystal

Botanical Source

Structure Type



Standards;Natural Pytochemical;API




1-aminomethyl-2-hydroxymethylbenzene/aminomethylbenzyl alcohol/2-Aminomethyl-1-hydroxymethylbenzene/aminomethylcarboxylic acid/carboxymethylamine/Glycine/1-hydroxymethyl-2-aminomethylbenzene/H-Gly-OH


2-aminoacetic acid


1.3±0.1 g/cm3



Flash Point

99.5±22.6 °C

Boiling Point

240.9±23.0 °C at 760 mmHg

Melting Point

240 °C (dec.)(lit.)


InChl Key

WGK Germany


HS Code Reference


Personal Projective Equipment

Correct Usage

For Reference Standard and R&D, Not for Human Use Directly.

Meta Tag

provides coniferyl ferulate(CAS#:56-40-6) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate




Glycine consists of a single carbon molecule attached to an amino and a carboxyl group. Its small size helps it to function as a flexible link in proteins and allows for the formation of helices, an extracellular signaling molecule, recognition sites on cell membranes and enzymes, a modifier of molecular activity via conjugation and glycine extension of hormone precursors, and an osmoprotectant. There is substantial experimental evidence that free glycine may have a role in protecting tissues against insults such as ischemia, hypoxia, and reperfusion. This impressive catalogue of functions makes an interesting contrast with glycine’s perceived metabolic role as a nonessential amino acid. Glycine interconverts with serine to provide a mechanism for the transfer of activated one-carbon groups. Glycine has just been viewed as a convenient source of nitrogen to add to solutions of nutrients. Although this may have unexpected benefits when such solutions are used in clinical practice, it does raise the specter of a possible confounding effect in experiments when glycine is added to control solutions to make them isonitrogenous.




Hall JC1.

Publish date

1998 Nov-Dec




The origin and early evolution of neurotransmitter signaling in animals are unclear due to limited comparative information, primarily about prebilaterian animals. Here, we performed the comparative survey of signal molecules in placozoans – the simplest known free-living animals without canonical synapses, but with complex behaviors. First, using capillary electrophoresis with laser-induced fluorescence detection, we performed microchemical analyses of transmitter candidates in Trichoplax adhaerens – the classical reference species in comparative biology. We showed that the endogenous level of glycine (about 3 mM) was significantly higher than for other candidates such as L-glutamate, L-aspartate, or gamma-aminobutyric acid. Neither serotonin nor dopamine were detected. The absolute glycine concentrations in Trichoplax were even higher than we measured in ctenophores (Beroe) and cnidarians (Aequorea). We found that at millimolar concentrations of glycine (similar to the endogenous level), induced muscle-like contractions in free behaving animals. But after long incubation (24 h), 10 M of glycine could induce cytotoxicity and cell dissociation. In contrast, micromolar concentrations (10-10 M) increased Trichoplax ciliated locomotion, suggesting that glycine might act as an endogenous signal molecule. However, we showed than glycine (10 M) can also be a chemoattractant (a guiding factor for food sources), and therefore, act as the exogenous signal. These findings provide an evolutionary base for the origin of transmitters as a result of the interplay between exogenous and endogenous signaling systems early in animal evolution.


Glycine as a signaling molecule and chemoattractant in Trichoplax (Placozoa): insights into the early evolution of neurotransmitters.


Romanova DY1,2, Heyland A3, Sohn D4, Kohn AB4, Fasshauer D1, Varoqueaux F1, Moroz LL4,5.

Publish date

2020 Apr 8




Glycine betaine (GB) is a naturally occurring osmolyte that has been widely recognized as a protein protectant. Since GB consists of a methylated ammonium moiety, it can engage in strong cation-π interactions with aromatic amino acid sidechains. We hypothesize that such specific binding interactions would allow GB to decrease the stability of proteins that are predominantly stabilized by a cluster of aromatic amino acids. To test this hypothesis, we investigate the effect of GB on the stability of two β-hairpins (or mini-proteins) that contain such a cluster. We find that for both systems the stability of the folded state first decreases and then increases with increasing GB concentration. Such non-monotonic dependence not only confirms that GB can act as a protein denaturant, but also underscores the complex interplay between GB’s stabilizing and destabilizing forces toward a given protein. While stabilizing osmolytes all have the tendency to be excluded from the protein surface which is the action underlying their stabilizing effect, our results suggest that in order to quantitatively assess the effect of GB on the stability of any given protein, specific cation-π binding interactions need to be explicitly considered. Moreover, our results show, consistent with other studies, that cation methylation can strengthen the respective cation-π interactions. Taken together, these findings provide new insight into the mechanism by which amino acid-based osmolytes interact with proteins.


Can glycine betaine denature proteins?


Acharyya A1, Shin D1, Troxler T1, Gai F1.

Publish date

2020 Apr 3

Description :

Glycine is an inhibitory neurotransmitter in the CNS and also acts as a co-agonist along with glutamate, facilitating an excitatory potential at the glutaminergic N-methyl-D-aspartic acid (NMDA) receptors.