SHLP2 peptide (TFA removed)

SHLP2 peptide (TFA removed)

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

Batch to batch variation of the purity

H-MGVKFFTLSTRFFPSVQRAVPLWTNS-OH

H-Met-Gly-Val-Lys-Phe-Phe-Thr-Leu-Ser-Thr-Arg-Phe-Phe-Pro-Ser-Val-Gln-Arg-Ala-Val-Pro-Leu-Trp-Thr-Asn-Ser-OH

26

98.42%

C₁₄₂H₂₁₄N₃₆O₃₅S

3017.49

Synthetic

Powder

SHLP2 is a bioactive peptide derived from mitochondria that has been shown to modulate cell function and enhance cell viability. SHLP2 has been found to increase mitochondrial oxygen consumption rate (OCR) and cellular ATP levels, indicating that it enhances mitochondrial metabolism. SHLP2 has also been shown to activate the ERK and STAT3 signaling pathways, which are involved in cellular protection. In addition, SHLP2 has been found to have a protective effect against cytotoxicity in neurons and can prevent neuronal cell death caused by amyloid beta toxicity.

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

• Cobb LJ, Lee C, Xiao J, Yen K, Wong RG, Nakamura HK, Mehta HH, Gao Q, Ashur C, Huffman DM, Wan J, Muzumdar R, Barzilai N, Cohen P. Naturally occurring mitochondrial-derived peptides are age-dependent regulators of apoptosis, insulin sensitivity, and inflammatory markers. Aging (Albany NY). 2016 Apr;8(4):796-809. doi: 10.18632/aging.100943. PMID: 27070352; PMCID: PMC4925829.

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.