24787-87-9

Usage

Uses

Used in Pharmaceutical Industry:
Z-SER-ALA-OH is used as a building block for the development of peptide-based drugs, leveraging its amino acid composition and carboxylic acid group to facilitate peptide bond formation and enhance drug efficacy.
Used in Biochemistry Research:
Z-SER-ALA-OH serves as a valuable tool in biochemical research, enabling scientists to study protein synthesis, peptide bond formation, and the role of specific amino acids in various biological processes.
Used in Molecular Biology Applications:
In molecular biology, Z-SER-ALA-OH is utilized as a component in the design of novel bioactive peptides, exploring its potential to modulate biological functions and develop new therapeutic agents.

InChI:InChI=1/C14H18N2O6/c1-9(13(19)20)15-12(18)11(7-17)16-14(21)22-8-10-5-3-2-4-6-10/h2-6,9,11,17H,7-8H2,1H3,(H,15,18)(H,16,21)(H,19,20)

Upstream product

• 38428-20-5 methyl ((benzyloxy)carbonyl)-L-seryl-L-alaninate 
• 130380-51-7 N-Benzyloxycarbonyl-L-seryl-L-alanin-heptylester 
• 56-41-7 L-alanin 
• 26582-86-5 benzyl (1S)-2-hydrazino-1-(hydroxymethyl)-2-oxoethylcarbamate 

Downstream Products

• 54647-75-5 Z-Ser-AlaNHNH-Boc 
• 6403-17-4 L-ser-L-ala 

Relevant academic research and scientific papers

Selective Enzymatic Removal of Protecting Groups: n-Heptyl Esters as Carboxy Protecting Functions in Peptide Synthesis

Amino acid heptyl (Hep) esters are accessible as generally crystalline hydro tosylates 3 from the amino acids by azeotropic esterification with 1-heptanol in high yields.They can be condensed with Z-, Boc-, and Aloc-protected amino acids to give the dipep

Synthesis of phenolic group containing analogues of porcine secretin and their immunological properties

Syntheses by the conventional method are described of Nα-tyrosylsecretin, [Tyr1]secretin, and Nα-β-(4-hydroxyphenyl)propionylsecretin. Secretin and [Tyr6] secretin were also prepared by the synthetic route identical with those employed for construction of the above analogues. Purification of secretin and the analogues was conducted by ion-exchange column chromatography on CM-Sephadex and gel filtration. Immunological reactivities of these analogues were examined in the radioimmunoassay system for secretin using two different antisera raised against synthetic secretin in rabbits. The tracers used in this study were [125I]-[Tyr1] secretin and [125I]-[Tyr6]secretin. The dose-response curves of Nα-tyrosylsecretin, [Tyr1]secretin, and Nα-β-(4-hydroxyphenyl) propionylsecretion were essentially superimposable upon those of natural and synthetic preparations of porcine secretin in the systems used, while [Tyr6]secretin showed discrepancy in the curve. In addition, biological activities of the synthetic polypeptides were compared with that of natural porcine secretin in terms of exocrine pancreatic secretory response in anesthetized dogs.