BMP-7 (110–120) peptide

BMP-7 (110–120) peptide

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

Batch to batch variation of the purity

H-KAISVLYFDDS-OH

H-Lys-Ala-Ile-Ser-Val-Leu-Tyr-Phe-Asp-Asp-Ser-OH

11

95.92%

C₅₈H₈₈N₁₂O₁₉

1257.38

Synthetic

Powder

KAISVLYFDDS peptide is a bioactive peptide originating from bone morphogenetic protein - 7 (BMP - 7). This peptide has demonstrated remarkable properties in relation to osteoblast functions. It significantly enhances calcium deposition by osteoblasts, which is a vital indicator of osteoblast differentiation and bone formation. In various experimental conditions, osteoblasts cultured with this peptide and its combinations with other peptides consistently showed increased calcium deposition over time. Additionally, it contributes to the enhancement of total collagen content in osteoblasts, further supporting its role in the bone formation process. KAISVLYFDDS peptide is thus a promising candidate for applications in bone regeneration. It could potentially be utilized in the development of new biomaterials or therapeutic strategies aimed at promoting bone growth and repair. By specifically targeting osteoblasts and enhancing their calcium deposition and collagen synthesis capabilities, it offers a valuable tool for improving orthopedic treatments and addressing bone - related disorders.

Normally, this peptide will be delivered in lyophilized form and should be stored in a freezer at or below -20 °C. For more details, please refer to the manual: Handling and Storage of Synthetic Peptides

• Chen Y, Webster TJ. Increased osteoblast functions in the presence of BMP-7 short peptides for nanostructured biomaterial applications. J Biomed Mater Res A. 2009 Oct;91(1):296-304. doi: 10.1002/jbm.a.32246. PMID: 18980196; PMCID: PMC2732755.

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.