SOR-C13 peptide

SOR-C13 peptide

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

Batch to batch variation of the purity

H-KEFLHPSKVDLPR-OH

H-Lys-Glu-Phe-Leu-His-Pro-Ser-Lys-Val-Asp-Leu-Pro-Arg-OH

13

95.15%

C₇₂H₁₁₆N₂₀O₁₉

1565.81

Synthetic

Powder

SOR-C13 is a carboxy terminal truncated peptide derived from the 54 residue paralytic peptide soricidin, found in the paralytic venom of the short-tailed shrew Blarina brevicauda. SOR-C13 is a high affinity, use dependent antagonist of human transient receptor potential vanilloid 6 (TRPV6) channels with an IC50 of 14 nM. TRPV6 is a non-voltage gated calcium channel implicated in malignancies and poor prognosis in breast cancer. In vivo, SOR-C13 reduces the growth of human ovarian xenografts in NOD/SCID mouse models.

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

• Bowen et al (2013) In vivo detection of human TRPV6-rich tumors with anti-cancer peptides derived from soricidin. PLoS One 8(3) e58866 PMID: 23554944
• Xue et al (2018) Inhibition of Transient Receptor Potential Vanilloid 6 channel, elevated in human ovarian cancers, reduces tumour growth in a xenograft model. J Cancer 9(17) 3196 PMID: 30210643

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.