N-Fmoc-N-methyl-3-(2-naphthyl)-L-alanine
97%
- Product Code: 50853
CAS:
2138482-09-2
| Molecular Weight: | 451.52 g./mol | Molecular Formula: | C₂₉H₂₅NO₄ |
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| EC Number: | MDL Number: | ||
| Melting Point: | Boiling Point: | 665.9±44.0 °C at 760 mmHg | |
| Density: | Storage Condition: | 2-8°C |
Product Description:
This chemical is primarily used in peptide synthesis, particularly in solid-phase peptide synthesis (SPPS) methodologies. It serves as a protected amino acid derivative, where the Fmoc (fluorenylmethyloxycarbonyl) group acts as a temporary protecting group for the amine functionality during the synthesis process. The naphthyl group introduces aromaticity and hydrophobicity, which can be crucial for modifying the peptide's interaction with biological targets or for enhancing its stability. This compound is especially valuable in the development of peptides with specific structural or functional properties, such as those used in drug discovery, biochemical research, and the study of protein-protein interactions. Its application allows for precise control over the peptide sequence, enabling the creation of complex and tailored peptide structures.
Sizes / Availability / Pricing:
| Size (g) | Availability | Price | Quantity |
|---|---|---|---|
| 0.250 | 10-20 days | $450.23 |
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| 1.000 | 10-20 days | $1,356.10 |
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N-Fmoc-N-methyl-3-(2-naphthyl)-L-alanine
This chemical is primarily used in peptide synthesis, particularly in solid-phase peptide synthesis (SPPS) methodologies. It serves as a protected amino acid derivative, where the Fmoc (fluorenylmethyloxycarbonyl) group acts as a temporary protecting group for the amine functionality during the synthesis process. The naphthyl group introduces aromaticity and hydrophobicity, which can be crucial for modifying the peptide's interaction with biological targets or for enhancing its stability. This compound is especially valuable in the development of peptides with specific structural or functional properties, such as those used in drug discovery, biochemical research, and the study of protein-protein interactions. Its application allows for precise control over the peptide sequence, enabling the creation of complex and tailored peptide structures.
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