st-Ht31 peptide

st-Ht31 peptide

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

Stearyl-DLIEEAASRIVDAVIEQVKAAGAY

Stearyl-Asp-Leu-Ile-Glu-Glu-Ala-Ala-Ser-Arg-Ile-Val-Asp-Ala-Val-Ile-Glu-Gln-Val-Lys-Ala-Ala-Gly-Ala-Tyr-OH

24

95.25%

C₁₂₉H₂₁₇N₂₉O₃₉

2798.27

Synthetic

Powder

st-Ht31 is a stearated and cell permeable version of the peptide Ht-31, which inhibits the interaction between the RII subunits of cAMP-dependent PKA and A-kinase anchoring protein (AKAP). The sequence of st-Ht31 is derived from human thyroid RII anchoring protein Ht31, comprising residues 493-515, and is the minimum region of Ht 31 required for RII binding. Disruption of the AKAP-PKA interaction by st-Ht31 alters human airway smooth muscle proliferation and enhances contractile force generation with upregulation of the contractile protein α-sm-actin. st-Ht31 also increases cytosolic PKA activity and is able to reverse foam cell formation and restore metabolic health in otherwise dysfunctional macrophages.

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

• Carr (1992) Association of the type II cAMP-dependent protein kinase with a human thyroid RII-anchoring protein. Cloning and characterization of the RII-binding domain. J Biol Chem. 267(19) 13376 PMID: 1618839
• Ma et al (2011) Ht31, a protein kinase A anchoring inhibitor, induces robust cholesterol efflux and reverses macrophage foam cell formation through ATP-binding cassette transporter A1. J Biol Chem. 286(5) 3370 PMID: 21106522
• Baarsma et al (2020) Disruption of AKAP-PKA Interaction Induces Hypercontractility With Concomitant Increase in Proliferation Markers in Human Airway Smooth Muscle. Front Cell Dev Biol. 8 165 PMID: 32328490

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.