21435-27-8

Usage

Uses

Used in Pharmaceutical Research and Development:
H-SER-TYR-OH is used as a research compound for exploring its potential therapeutic effects and mechanisms of action in various medical conditions. The presence of serine and tyrosine in the peptide may contribute to its potential applications in the development of new drugs and therapies.
Used in Biochemical Research:
H-SER-TYR-OH serves as a valuable tool in biochemical research, allowing scientists to study the interactions between serine and tyrosine, as well as their roles in cellular processes and signaling pathways. This peptide can be used to investigate the functions of these amino acids and their potential impact on biological systems.
Used in Drug Design and Development:
H-SER-TYR-OH can be utilized in drug design and development, as its unique combination of serine and tyrosine may offer novel therapeutic targets or mechanisms for treating various diseases and conditions. Researchers can use this peptide to identify potential drug candidates or to develop new therapeutic agents with improved efficacy and safety profiles.
Used in Neurotransmitter and Hormone Research:
Given the involvement of tyrosine in the production of neurotransmitters and hormones, H-SER-TYR-OH can be employed in research focused on understanding the role of these molecules in mood regulation, energy levels, and cognitive function. This peptide may help scientists develop new treatments for neurological and endocrine disorders.

Upstream product

• 60-18-4 L-tyrosine 
• 201855-53-0 Ser-Tyr-MCA 
• 24008-82-0 L-seryl-L-tyrosyl-β-naphthylamide 
• 52885-18-4 Z-Ser-Tyr-OH 
• 24118-03-4 Z-L-Ser-L-Tyr-OMe 
• 5269-46-5 tyrosine trimethylsilyl ester 
• 13588-99-3 H-Tyr-Ser-OH 
• 7664-41-7 ammonia 

Downstream Products

• 103629-65-8 (S)-2-{(S)-2-[(S)-2-Benzyloxycarbonylamino-3-(1H-indol-3-yl)-propionylamino]-3-hydroxy-propionylamino}-3-(4-hydroxy-phenyl)-propionic acid 

Relevant academic research and scientific papers

Identification and characterization of prokaryotic dipeptidyl-peptidase 5 from porphyromonas gingivalis

Porphyromonas gingivalis, a Gram-negative asaccharolytic anaerobe, is a major causative organism of chronic periodontitis. Because the bacterium utilizes amino acids as energy and carbon sources and incorporates them mainly as dipeptides, a wide variety of dipeptide production processes mediated by dipeptidyl-peptidases (DPPs) should be beneficial for the organism. In the present study, we identified the fourth P. gingivalis enzyme, DPP5. In a dpp4-7-11-disrupted P. gingivalis ATCC 33277, a DPP7-like activity still remained. PGN-0756 possessed an activity indistinguishable from that of the mutant, and was identified as a bacterial orthologue of fungal DPP5, because of its substrate specificity and 28.5% amino acid sequence identity with an Aspergillus fumigatus entity. P. gingivalis DPP5 was composed of 684 amino acids with a molecular mass of 77,453, and existed as a dimer while migrating at 66 kDa on SDS-PAGE. It preferred Ala and hydrophobic residues, had no activity toward Pro at the P1 position, and no preference for hydrophobic P2 residues, showed an optimal pH of 6.7 in the presence of NaCl, demonstrated Km and kcat/Km values for Lys-Ala-MCA of 688 μM and 11.02 μM-1 s-1, respectively, and was localized in the periplasm. DPP5 elaborately complemented DPP7 in liberation of dipeptides with hydrophobic P1 residues. Examinations of DPP- and gingipain gene-disrupted mutants indicated that DPP4, DPP5, DPP7, and DPP11 together with Arg- and Lys-gingipains cooperatively liberate most dipeptides from nutrient oligopeptides. This is the first study to report that DPP5 is expressed not only in eukaryotes, but also widely distributed in bacteria and archaea.

SOY SAUCE HAVING HYPOTENSIVE EFFECTS AND METHOD FOR PRODUCING THE SAME

The present invention provides soy sauce that comprises significant amounts of peptides, and, in particular, hypotensive peptide Gly-Tyr and hypotensive peptide Ser-Tyr, exhibiting a high degree of angiotensin-I-converting enzyme-inhibitory activity and has hypotensive effects while containing no hypotensive agent. Target soy sauce is obtained by mixing soy sauce koji having protease activity of 20 to 300 U/g koji with an aqueous common salt solution and subjecting the mixture to heated digestion, followed by compression filtration. Target soy sauce with a good flavor is obtained by adding soy sauce lactic acid bacteria and soy sauce yeast cells to the moromi mash after heated digestion, and subjecting the resultant to fermentation and maturation, followed by compression filtration.

TRIMETHYLSILYL CYANIDE IN PEPTIDE STRATEGIES. PART III. NEEDLESSNESS FOR COMPLEMENTARY HYDROXYL SIDE-CHAIN PROTECTION

No extra side-chain protection is needed for Ser, Thr, Tyr, and Cys (nor for Asp and Glu) in peptide syntheses that are mediated by TMS-CN, whereby silylesters and ethers are formed and are stable enough even during activation of carboxylic components.Thi

EXPERIENCES IN Z-DEPROTECTION. SIMPLE PREPARATIONS OF Z-His and diZ-His.

A systematic investigation about the possibilities of removing benzyloxycarbonyl groupings in some model peptides acids that resist easy deprotection, have led to some interesting and efficient modified procedures.One-pot synthetic methods for Zα-His-OH and Zα,ZIm-His-OH are also reported.