Tat-CIRP peptide

Tat-CIRP peptide

• COA/MS/HPLC Report
• Handling and Storage of Synthetic Peptides
• Material Safety Data Sheets (MSDS)

Batch to batch variation of the purity

H-YGRKKRRQRRRGRGFSRGGGDRGYGG-OH

H-Tyr-Gly-Arg-Lys-Lys-Arg-Arg-Gln-Arg-Arg-Arg-Gly-Arg-Gly-Phe-Ser-Arg-Gly-Gly-Gly-Asp-Arg-Gly-Tyr-Gly-Gly-OH

26

95.46%

C₁₂₃H₂₀₆N₅₆O₃₃

2997.29

Synthetic

Powder

Tat-CIRP is a peptide derived from the high affinity binding region of cold-inducible RNA binding protein (CIRP) which competitively binds to myeloid differentiation factor 2 (MD2) and blocks the MD2-CIRP interaction. MD2 is an essential accessory protein for Toll like receptor 4 (TLR4) activation and blocking the function of MD2 and TLR4 with Tat-CIRP is neuroprotective, reducing apoptosis and necroptosis in vitro. In vivo, Tat-CIRP is neuroprotective against ischemic and hemorrhagic stroke in mice and reduces brain infarct volume and preserves neurological function in rhesus monkeys 30 days after ischemic stroke.

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

• Fang et al (2021) An MD2-perturbing peptide has therapeutic effects in rodent and rhesus monkey models of stroke. Sci Transl Med. 13(597) eabb6716 PMID: 34108252

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.