CXCL9(74–103) peptide

CXCL9(74–103) peptide

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

H-KKKQKNGKKHQKKKVLKVRKSQRSRQKKTT-OH

H-Lys-Lys-Lys-Gln-Lys-Asn-Gly-Lys-Lys-His-Gln-Lys-Lys-Lys-Val-Leu-Lys-Val-Arg-Lys-Ser-Gln-Arg-Ser-Arg-Gln-Lys-Lys-Thr-Thr-OH

30

95.28%

C₁₅₈H₂₉₅N₅₉O₄₀

3661.39

Synthetic

Powder

CXCL9(74–103) is a peptide corresponding to the C-terminal amino acids of the chemokine CXCL9. CXCL9(74–103) does not signal through or act as an antagonist for CXCR3, the CXCL9 receptor, or influence the neutrophil chemotactic activity of CXCL8 in vitro, but it does display high affinity for glycosaminoglycans (GAGs), and can displace chemokines bound to GAGs. CXCL8 and CXCL9 drive leukocyte migration to inflammation sites and through this inhibition of the chemokine-GAG interaction, CXCL9(74–103) can block neutrophil migration. In vivo, CXCL9(74-103) ameliorates joint inflammation in a murine model of antigen induced arthritis, reducing neutrophil accumulation and joint and cartilage damage, and is also effective in a murine model of gout.

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

• Vanheule et al (2015) The Positively Charged COOH-terminal Glycosaminoglycan-binding CXCL9(74-103) Peptide Inhibits CXCL8-induced Neutrophil Extravasation and Monosodium Urate Crystal-induced Gout in Mice. J Biol Chem. 290(35) 21292 PMID: 26183778
• Boff (2018) The chemokine fragment CXCL9(74-103) diminishes neutrophil recruitment and joint inflammation in antigen-induced arthritis. J Leukoc Biol. 104(2) 413 PMID: 29733455
• De Zutter et al (2021) The Chemokine-Based Peptide, CXCL9(74-103), Inhibits Angiogenesis by Blocking Heparan Sulfate Proteoglycan-Mediated Signaling of Multiple Endothelial Growth Factors. Cancers 13(20) 5090 PMID: 34680238

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.