γ glu phe

γ-Glu-Phe can be synthesized by Bacillus amyloliquefaciens (GBA) and Aspergillus oryzae (GAO). γ-Glu-Phe or the enzymatic reaction mixture effectively enhances the umami intensity of commercial soy sauce and simulated chicken soup.

γ-Glu-Phe TFA(7432-24-8 free base) is a dipeptide composed of gamma-glutamate and phenylalanine and is a proteolytic breakdown product of larger proteins. It is probably formed by transpeptidation between glutathione and the corresponding amino acid, catalyzed by gamma-glutamyl transpeptidase.

H-Pro-Thr-Glu-Phe-p-nitro-Phe-Arg-Leu-OH is a water-soluble polypeptide that serves as a substrate for the enzymes cathepsin D, pepsin, and pepsinogen, with potential applications in biochemical analysis [1] [2].

γ-Glu-(Phe-13C9,15N) trifluoroacetic acid is a version of γ-Glu-Phe trifluoroacetic acid labeled with 13C and 15N isotopes. It is synthesized by Bacillus amyloliquefaciens (GBA) and Aspergillus oryzae (GAO). γ-Glu-Phe trifluoroacetic acid or its enzyme reaction mixtures can enhance the umami taste of commercial soy sauce and simulated chicken broth.

Lys-Phe-Glu-Arg-Gln promotes cytosolic protein degradation in serum-deprived human diploid fibroblasts [1].

Suc-Ala-Glu-Pro-Phe-pNA (Suc-AEPF-pNA) TFA is a chromogenic substrate for the enzyme peptidyl-prolyl isomerase Pin1. It can be utilized to assess the inhibitory effects of target compounds on Pin1, as well as to evaluate the catalytic activity of Pin1.

Arg-Glu(edans)-Ile-His-Pro-Phe-His-Pro-Phe-His-Leu-Val-Ile-His-Thr-Lys(dabcyl)-Arg is a fluorescent renin substrate based on the N-terminal tetrapeptide sequence of human angiotensinogen (hTDP).

Ac-c[Cys-Glu-His-d-Phe-Arg-Trp-d-Cys]-Pro-Pro-Lys-Asp-NH2 (compound 5) is a selective hMC5R antagonist ligand with an IC50 of 10 nM.

Ac-Glu-Asp(EDANS)-Lys-Pro-Ile-Leu-Phe-Phe-Arg-Leu-Gly-Lys(DABCYL)-Glu-NH2 acetate is a substrate for Cathepsin D and can be utilized in Cathepsin D FRET assays.

M-2420 is a fluorogenic substrate specifically designed for the β-secretase site associated with the Swedish mutation of the amyloid precursor protein (APP).