Ac-Tyr-NH2

Ac-Tyr-NH2 is an N-acetylated tyrosine amide derivative featuring a tyrosyl side chain with a phenolic hydroxyl and a terminal carboxamide (-CONH2) rather than a free carboxylic acid. The molecule contains an acetylated amino terminus (Ac-) and a phenolic group capable of hydrogen bonding and acid-base-dependent behavior, with the stereochemistry at the α-carbon not specified in the name. As a peptide-related intermediate, Ac-Tyr-NH2 is used in synthesis and structure-activity or chemical biology studies where a tyrosine residue analog with a protected/modified termini pattern is required for controlled coupling, labeling, or analytical reference standards.

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.

CAT No: CP26594

CAS No:1948-71-6

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M.F/Formula
C11H14N2O3
M.W/Mr.
222.24

Ac-Tyr-NH2 is an N-acetylated tyrosine amide designed as a short, protected peptide-like building block featuring the phenolic side chain of tyrosine. The acetylated N-terminus and C-terminal primary amide reduce free-ion functionality and make the compound a convenient, well-defined reference structure for studying tyrosine-containing peptide motifs in chemical biology and analytical workflows. Its aromatic phenol enables selective derivatization or targeted reactivity when downstream assay chemistry requires a tyrosine handle.

1. Peptide Motif Reference

Ac-Tyr-NH2 is used by peptide chemists and chemical biology groups as a defined tyrosine-containing motif reference during method development for peptide synthesis and characterization. Because the N-terminus is acetylated and the C-terminus is an amide, it models a common peptide microenvironment more realistically than free tyrosine, supporting comparisons in LC-MS profiling, fragmentation behavior, and derivatization efficiency for tyrosine-bearing sequences. Researchers often employ it to validate analytical workflows that distinguish tyrosine phenol reactivity or to benchmark retention and ionization patterns for short peptide-like standards.

2. Tyrosine Derivatization Studies

Ac-Tyr-NH2 is frequently selected for chemical biology and materials chemistry experiments that require a controlled tyrosine phenol functional group within a peptide-like scaffold. The phenolic side chain allows downstream labeling, conjugation, or controlled chemical modification while the acetylated amino terminus and terminal amide help maintain a consistent reactivity profile relative to unprotected amino acid forms. This makes the compound useful for developing and screening tyrosine-targeted labeling chemistries, including workflows where researchers need a small, soluble model substrate to optimize conditions before applying them to longer peptides.

3. Analytical Standards For LC-MS

Ac-Tyr-NH2 serves as an analytical standard and calibration reference for quantitative and qualitative mass spectrometry workflows involving tyrosine-containing peptide fragments or acetylated peptide termini. Its defined acetylation and amide end-group provide a stable, unambiguous target for monitoring in LC-MS method development, in-process analytics, and impurity/fragment tracking during peptide synthesis or peptide library studies. Analytical teams commonly use it to confirm identity and to support method robustness when tyrosine-containing species are expected to appear as specific fragments or derivatized forms.

4. Pharmaceutical Intermediate Building Block

Ac-Tyr-NH2 is also used in pharmaceutical intermediate development and specialty chemical manufacturing as a peptide-like intermediate for constructing tyrosine-containing fragments. Synthetic teams leverage its pre-installed acetylated N-terminus and terminal amide to streamline downstream assembly of larger peptidomimetic or peptide-derived structures where a tyrosine phenol must be preserved for later functionalization. In development settings, the compound provides a practical starting point for producing defined intermediates used in SAR-oriented synthesis campaigns and in the preparation of reference materials for characterization.

Size
1 g;5 g;

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