Fmoc-D-Pen(Acm)-OH
97%
- Product Code: 54889
CAS:
201531-77-3
| Molecular Weight: | 442.53 g./mol | Molecular Formula: | C₂₃H₂₆N₂O₅S |
|---|---|---|---|
| EC Number: | MDL Number: | MFCD00151934 | |
| Melting Point: | Boiling Point: | 709.3°C at 760 mmHg | |
| Density: | Storage Condition: | 2-8°C, dry and sealed |
Product Description:
This compound is primarily utilized in peptide synthesis, particularly in solid-phase peptide synthesis (SPPS) methods. It serves as a protected amino acid derivative, where the Fmoc (fluorenylmethyloxycarbonyl) group acts as a temporary protecting group for the amino functionality, and the Acm (acetamidomethyl) group protects the thiol side chain of the penicillamine residue. This protection strategy is crucial for the stepwise assembly of peptides, ensuring that the desired sequence is achieved without unwanted side reactions. It is especially valuable in the synthesis of peptides containing cysteine or cysteine-like residues, where selective deprotection and disulfide bond formation are required. Its application is common in the development of therapeutic peptides, research peptides, and biochemical studies involving peptide structure and function.
Sizes / Availability / Pricing:
| Size (g) | Availability | Price | Quantity |
|---|---|---|---|
| 0.250 | 10-20 days | ฿2,808.00 |
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| 1.000 | 10-20 days | ฿7,029.00 |
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| 5.000 | 10-20 days | ฿28,854.00 |
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Fmoc-D-Pen(Acm)-OH
This compound is primarily utilized in peptide synthesis, particularly in solid-phase peptide synthesis (SPPS) methods. It serves as a protected amino acid derivative, where the Fmoc (fluorenylmethyloxycarbonyl) group acts as a temporary protecting group for the amino functionality, and the Acm (acetamidomethyl) group protects the thiol side chain of the penicillamine residue. This protection strategy is crucial for the stepwise assembly of peptides, ensuring that the desired sequence is achieved without unwanted side reactions. It is especially valuable in the synthesis of peptides containing cysteine or cysteine-like residues, where selective deprotection and disulfide bond formation are required. Its application is common in the development of therapeutic peptides, research peptides, and biochemical studies involving peptide structure and function.
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