Fmoc-Homoarg-OH

98%

  • Product Code: 105829
  Alias:    N-Fmoxy-Homoarginine
  CAS:    776277-76-0
Molecular Weight: 410.47 g./mol Molecular Formula: C₂₂H₂₆N₄O₄
EC Number: MDL Number:
Melting Point: Boiling Point:
Density: 1.35 g/cm3 Storage Condition: 2~8℃
Product Description: Fmoc-Homoarg-OH is widely used in peptide synthesis, particularly in solid-phase peptide synthesis (SPPS). It serves as a protected amino acid derivative, where the Fmoc (fluorenylmethyloxycarbonyl) group protects the amine functionality during the coupling reactions. This compound is especially valuable in the synthesis of peptides containing homoarginine, a non-natural amino acid that mimics the structure and function of arginine. Its application is crucial in the development of peptide-based drugs, bioactive peptides, and research tools for studying protein-protein interactions. Additionally, it is utilized in the preparation of peptide libraries for drug discovery and in the study of enzyme-substrate interactions due to its ability to introduce specific structural modifications in peptide chains.
Product Specification:
Test Specification
Purity (%) 97.5-100
Appearance White Powder Or Crystals
Sizes / Availability / Pricing:
Size (g) Availability Price Quantity
1.000 10-20 days ฿290.00
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5.000 10-20 days ฿950.00
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25.000 10-20 days ฿3,600.00
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100.000 10-20 days ฿10,330.00
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Fmoc-Homoarg-OH
Fmoc-Homoarg-OH is widely used in peptide synthesis, particularly in solid-phase peptide synthesis (SPPS). It serves as a protected amino acid derivative, where the Fmoc (fluorenylmethyloxycarbonyl) group protects the amine functionality during the coupling reactions. This compound is especially valuable in the synthesis of peptides containing homoarginine, a non-natural amino acid that mimics the structure and function of arginine. Its application is crucial in the development of peptide-based drugs, bioactive peptides, and research tools for studying protein-protein interactions. Additionally, it is utilized in the preparation of peptide libraries for drug discovery and in the study of enzyme-substrate interactions due to its ability to introduce specific structural modifications in peptide chains.
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