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詳細
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.
アプリケーション
Prolylphenylalanine can be used in biochemical and metabolomics research applications
特徴および利点
- Suitable for Metabolomics and Biochemical research
- High-quality compound suitable for multiple research applications
その他情報
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保管分類コード
11 - Combustible Solids
WGK
WGK 3
引火点(°F)
Not applicable
引火点(℃)
Not applicable
適用法令
試験研究用途を考慮した関連法令を主に挙げております。化学物質以外については、一部の情報のみ提供しています。 製品を安全かつ合法的に使用することは、使用者の義務です。最新情報により修正される場合があります。WEBの反映には時間を要することがあるため、適宜SDSをご参照ください。
Jan Code
SMB01352-10MG:
SMB01352-BULK:
SMB01352-50MG:
SMB01352-VAR:
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試験成績書（COA）
Lot/Batch Number
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Angiotensin I converting enzyme inhibitory peptides from simulated in vitro gastrointestinal digestion of cooked eggs
Majumder K, et al
Journal of Agricultural and Food Chemistry, 57, 471-477 (2009)
Prolinase and non-specific dipeptidase of human kidney.
Priestman DA, et al.
The Biochemical Journal, 231, 689-694 (1985)
J Jandke et al.
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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