TLQP-62 peptide (TFA removed)

TLQP-62 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

TLQPPASSRRRHFHHALPPARHHPDLEAQARRAQEEADAEERRLQEQEELENYIEHVLLHRP

Thr-Leu-Gln-Pro-Pro-Ala-Ser-Ser-Arg-Arg-Arg-His-Phe-His-His-Ala-Leu-Pro-Pro-Ala-Arg-His-His-Pro-Asp-Leu-Glu-Ala-Gln-Ala-Arg-Arg-Ala-Gln-Glu-Glu-Ala-Asp-Ala-Glu-Glu-Arg-Arg-Leu-Gln-Glu-Gln-Glu-Glu-Leu-Glu-Asn-Tyr-Ile-Glu-His-Val-Leu-Leu-His-Arg-Pro

62

94.9%

C₃₁₈H₄₉₉N₁₀₉O₉₇

7401.01

Synthetic

Powder

The source of TLQP-62 is Rattus norvegicus. TLQP-62 belongs to VGF. TLQP-62 is expressed in Central and peripheral nervous systems, synthesized exclusively in neuronal and neuroendocrine cells.
The C-terminal peptide TLQP-62 is of particular relevance to maladaptive mechanisms of chronic pain as it is a known mediator of neuroplasticity in the hippocampus affecting learning, memory, depression, and adult neurogenesis.

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

• Moss A, Ingram R, Koch S, Theodorou A, Low L, Baccei M, et al. Origins, actions and dynamic expression patterns of the neuropeptide VGF in rat peripheral and central sensory neurones following peripheral nerve injury. Mol Pain. 2008
• Skorput AGJ, Zhang X, Waataja JJ, Peterson CD, Riedl MS, Kitto KF, Truong H, Huffman C, Salton SR, Fairbanks CA, Honda CN, Vulchanova L. Involvement of the VGF-derived peptide TLQP-62 in nerve injury-induced hypersensitivity and spinal neuroplasticity. Pain. 2018 Sep;159(9):1802-1813. doi: 10.1097/j.pain.0000000000001277.

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.