HGH fragment 176-191 peptide (TFA removed)

HGH fragment 176-191 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-YLRIVQCRSVEGSCGF-OH

H-Tyr-Leu-Arg-Ile-Val-Gln-Cys-Arg-Ser-Val-Glu-Gly-Ser-Cys-Gly-Phe-OH

16

95.86%

C₇₈H₁₂₅N₂₃O₂₃S₂

1817.09

Synthetic

Powder

The synthetic peptides corresponding to amino acids 172-191, 176-191, 177-191, 178-191, 179-191, and 180-191 of human growth hormone (hGH) have been studied for their in vivo effects in normal rats. Four of the peptides (hGH 172-191, 176-191, 177-191, and 178-191) produced a short-lived rise in blood glucose and a more sustained rise in plasma insulin, whereas the other two (hGH 179-191 and 180-191) were inert in the systems tested. A single dose (5 nmol/kg body wt) of the peptides containing the amino acids sequence 178-191 of the hGH molecule significantly reduced insulin sensitivity of the animals in intravenous insulin tolerance tests. The findings also indicate that the biologically active peptides must not only have the minimum of the informational sequence but also that this must be in correct physical configuration.

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

• Ng FM, Bornstein J. Hyperglycemic action of synthetic C-terminal fragments of human growth hormone. Am J Physiol. 1978 May;234(5):E521-6. doi: 10.1152/ajpendo.1978.234.5.E521. PMID: 645904.

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.