L-Phenylalanine (Standard)

L-Phenylalanine (Standard) is the analytical standard of L-Phenylalanine. This product is intended for research and analytical applications. L-Phenylalanine ((S) -2-Amino-3-phenylpropionic acid) is an essential amino acid isolated from Escherichia coli. L-Phenylalanine is a α2δ subunit of voltage-dependent Ca+ channels antagonist with a Ki of 980 nM. L-phenylalanine is a competitive antagonist for the glycine- and glutamate-binding sites of N-methyl-D-aspartate receptors (NMDARs) (KB of 573 μM) and non-NMDARs, respectively. L-Phenylalanine is widely used in the production of food flavors and pharmaceuticals[1][2][3][4].

Product Specifications

CAS Number

[63-91-2]

Product Name Alternative

(S) -2-Amino-3-phenylpropionic acid (Standard)

UNSPSC

12352005

Target

Calcium Channel; Endogenous Metabolite; iGluR; Reference Standards

Type

Reference Standards

Related Pathways

Membrane Transporter/Ion Channel; Metabolic Enzyme/Protease; Neuronal Signaling; Others

Applications

Metabolism-protein/nucleotide metabolism

Field of Research

Metabolic Disease

Assay Protocol

https://www.medchemexpress.com/l-phenylalanine-standard.html

Purity

99.99

Smiles

N[C@@H](CC1=CC=CC=C1)C(O)=O

Molecular Formula

C9H11NO2

Molecular Weight

165.19

References & Citations

[1]Glushakov AV, et al. Long-term changes in glutamatergic synaptic transmission in phenylketonuria. Brain. 2005 Feb;128 (Pt 2) :300-7.|[2]Glushakov AV, et al. L-phenylalanine selectively depresses currents at glutamatergic excitatory synapses. J Neurosci Res. 2003 Apr 1;72 (1) :116-24.|[3]Glushakov AV, et al. Specific inhibition of N-methyl-D-aspartate receptor function in rat hippocampal neurons by L-phenylalanine at concentrations observed during phenylketonuria. Mol Psychiatry. 2002;7 (4) :359-67.|[4]Mortell KH, et al. Structure-activity relationships of alpha-amino acid ligands for the alpha2delta subunit of voltage-gated calcium channels. Bioorg Med Chem Lett. 2006 Mar 1;16 (5) :1138-41.|[5]Wu WB, et al. Enhancement of l-phenylalanine production in Escherichia coli by heterologous expression of Vitreoscilla hemoglobin. Biotechnol Appl Biochem. 2018 May;65 (3) :476-483.