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Pro-Phe, N-L-Prolyl-L-phenylalanine, N-Prolylphenylalanine, L-Prolyl-L-phenylalanine, Proline phenylalanine dipeptide, Proline-phenylalanine dipeptide, Prolyl-phenylalanine
C14H18N2O3
Recommended Products
Quality Level
Assay
≥95% (HPLC)
form
solid
color
white to beige
mp
250—251 °C
storage temp.
2-8°C
SMILES string
OC(=O)C(Cc1ccccc1)NC(=O)C2CCCN2
General description
Prolylphenylalanine, a dipeptide composed of proline and phenylalanine, exhibits considerable potential for diverse applications in both biochemical and biomedical research. It is an incomplete breakdown product of protein digestion or protein catabolism, found in urine. In biochemical studies, it serves as a substrate for various enzymes, including dipeptidyl peptidase-4 (DPP-4) and prolylcarboxypeptidase (PCP), shedding light on essential biochemical pathways related to protein digestion and metabolism. Moreover, prolylphenylalanine functions as a versatile tool for exploring protein interactions with other molecules, probing enzyme active sites, and identifying potential drug targets. Furthermore, it can also be used for polypeptide synthesis, where phenylalanine is an aromatic amino acid that can inhibit the activity of Angiotensin-converting enzyme (ACE, HY-P2983). Within biomedical research, prolylphenylalanine is the focus of extensive exploration as a potential therapeutic agent for a range of conditions, including hypertension, cardiovascular disease, and Alzheimer′s disease.
Application
Prolylphenylalanine can be used in biochemical and metabolomics research applications
Features and Benefits
- Suitable for Metabolomics and Biochemical research
- High-quality compound suitable for multiple research applications
Other Notes
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WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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Angiotensin I converting enzyme inhibitory peptides from simulated in vitro gastrointestinal digestion of cooked eggs
Journal of Agricultural and Food Chemistry, 57, 471-477 (2009)
Prolinase and non-specific dipeptidase of human kidney.
The Biochemical Journal, 231, 689-694 (1985)
Journal of chromatography, 382, 39-45 (1986-10-31)
Fractions of dipeptides, obtained from human urine by a combination of cation-exchange chromatography, ligand-exchange chromatography and reversed-phase chromatography, were transformed into their N-heptafluorobutyryl methyl ester derivatives and then subjected to capillary gas chromatography. The profiles obtained indicate the presence of
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