Product Overview
TB-500 is a synthetic 43-amino-acid N-acetylated polypeptide. The peptide corresponds to a specific isoform of a naturally occurring peptide and features an N-terminal acetylation, a modification commonly employed to enhance stability in research settings.
Technical Specifications
| Sequence (1-Letter) | Ac-SDKPDMAEIEKFDKSKLKKTETQEKNPLPSKETIEQEKQAGES |
|---|---|
| Sequence (3-Letter) | Ac-Ser-Asp-Lys-Pro-Asp-Met-Ala-Glu-Ile-Glu-Lys-Phe-Asp-Lys-Ser-Lys-Leu-Lys-Lys-Thr-Glu-Thr-Gln-Glu-Lys-Asn-Pro-Leu-Pro-Ser-Lys-Glu-Thr-Ile-Glu-Gln-Glu-Lys-Gln-Ala-Gly-Glu-Ser |
| CAS Number | 77591-33-4 |
| Molecular Formula | C₂₁₂H₃₅₀N₅₆O₇₈S |
| Molecular Weight | ~4963 g/mol |
| Purity (HPLC) | ≥98% |
| Physical Form | Lyophilized powder |
| Vial Content | 10 mg |
Structural Context
TB-500 is a 43-amino-acid acetylated polypeptide. The structure incorporates a significant number of charged residues (Glutamic Acid, Aspartic Acid, and Lysine) interspersed throughout the sequence, which contribute to its solubility profile in aqueous buffers. The N-terminal acetylation provides a structurally defined endpoint, while the presence of a single Methionine and multiple hydrophobic residues (Leucine, Isoleucine, Phenylalanine, Alanine, Proline) interspersed within the hydrophilic domains creates a distinct amphipathic profile. The total residue count (43 amino acids) and defined primary sequence make this polypeptide suitable for analytical method development, chromatographic reference studies, and stability assessments in controlled laboratory environments.
Handling and Storage
The peptide is supplied in lyophilized (freeze-dried) powder form in a 10 mg vial. For optimal stability, store lyophilized material at or below -20°C. Protect from repeated freeze-thaw cycles, moisture, and prolonged exposure to light, heat, and humidity.
Research Applications
This product is manufactured and supplied as a chemical reference standard for in-vitro laboratory research applications including analytical method development, chromatographic reference studies, and stability assessments in controlled laboratory environments.






