BAM (8-22) peptide

BAM (8-22) peptide

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

Batch to batch variation of the purity

H-VGRPEWWMDYQKRYG-OH

H-Val-Gly-Arg-Pro-Glu-Trp-Trp-Met-Asp-Tyr-Gln-Lys-Arg-Tyr-Gly-OH

15

95.85%

C₉₁H₁₂₇N₂₅O₂₃S

1971.19

Synthetic

Powder

BAM (8-22), also known as bovine adrenal medulla 8-22, is an endogenous peptide that was first isolated from bovine adrenal medulla and is a potent agonist for sensory neuron specific receptors, primate-specific proteins that are exclusively expressed in primary sensory neurons, with EC50 values of 28 and 14 nM for SNSR3 and SNSR4 respectively. BAM (8-22) inhibits development of morphine tolerance in rats and exerts spinal analgesic effects by an interaction with NMDA receptors. It also blocks inflammatory pain, chemical pain and downregulates the expression of spinal c-fos gene in an opioid-independent manner. In humans BAM (8-22) produces itch and nociceptive sensations in a histamine independent manner.

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

• Simonin and Kieffer (2002) Two faces for an opioid peptide - and more receptors for pain research. Nat.Neurosci. 5 185 PMID: 11865303
• Chen and Ikeda (2004) Modulation of ion channels and synaptic transmission by a human sensory neuron-specific G-protein-coupled receptor, SNSR4/mrgX1, heterologously expressed in cultured rat neurons. J.Neurosci. 24 5044 PMID: 15163697
• Solinski et al (2014) Pharmacology and signaling of MAS-related G protein-coupled receptors. Pharmacol.Rev. 66 570 PMID: 24867890

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.