BMP-2 knuckle epitope 73-92 peptide

• Handling and Storage of Synthetic Peptides
• Material Safety Data Sheets (MSDS)

Batch to batch variation of the purity

• KIPKASSVPTELSAISTLYL polypeptide is a highly promising bioactive peptide with significant potential in the field of bone tissue engineering. Derived from the knuckle epitope of bone morphogenetic protein 2 (BMP - 2), it exhibits a remarkable ability to induce osteogenic differentiation. This peptide has been shown to enhance the expression of osteogenic markers such as osteocalcin (OCN) and collagen I, making it a potent activator of the osteogenic signaling pathway.
• It offers several advantages over native proteins, including improved stability, cost - effectiveness, and ease of modification and immobilization onto scaffolds. With its dose - dependent effect on osteogenic gene expression, it provides a tunable approach for promoting bone formation. Overall, KIPKASSVPTELSAISTLYL polypeptide holds great promise as a therapeutic agent for bone regeneration and repair, and is a valuable tool for advancing research and applications in tissue engineering and regenerative medicine.

• Lukasova V, Buzgo M, Sovkova V, Dankova J, Rampichova M, Amler E. Osteogenic differentiation of 3D cultured mesenchymal stem cells induced by bioactive peptides. Cell Prolif. 2017 Aug;50(4):e12357. doi: 10.1111/cpr.12357. PMID: 28714176; PMCID: PMC6529093.

Trifluoroacetic acid (TFA) has a significant impact on peptides due to its role in the peptide synthesis process.

TFA is essential for the protonation of peptides that lack basic amino acids such as Arginine (Arg), Histidine (His), and Lysine (Lys), or ones that have blocked N-termini. As a result, peptides often contain TFA salts in the final product.

TFA residues, when present in custom peptides, can cause unpredictable fluctuations in experimental data. At a nanomolar (nM) level, TFA can influence cell experiments, hindering cell growth at low concentrations (as low as 10 nM) and promoting it at higher doses (0.5–7.0 mM). It can also serve as an allosteric regulator on the GlyR of glycine receptors, thereby increasing receptor activity at lower glycine concentrations.

In an in vivo setting, TFA can trifluoroacetylate amino groups in proteins and phospholipids, inducing potentially unwanted antibody responses. Moreover, TFA can impact structure studies as it affects spectrum absorption.