GIP (porcine) peptide

GIP (porcine) peptide

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

H-YAEGTFISDYSIAMDKIRQQDFVNWLLAQKGKKSDWKHNITQ-OH

H-Tyr-Ala-Glu-Gly-Thr-Phe-Ile-Ser-Asp-Tyr-Ser-Ile-Ala-Met-Asp-Lys-Ile-Arg-Gln-Gln-Asp-Phe-Val-Asn-Trp-Leu-Leu-Ala-Gln-Lys-Gly-Lys-Lys-Ser-Asp-Trp-Lys-His-Asn-Ile-Thr-Gln-OH

42

95.14%

C₂₂₅H₃₄₂N₆₀O₆₆S

4975.52

Synthetic

Powder

GIP is a member of a family of structurally related hormones that includes secretin, glucagon, and vasoactive intestinal peptide. GIP (human) differs from GIP (porcine) at residues 18 and 34. GIP is secreted from specific endocrine cells (K-cells) in the epithelium of the upper part of small intestine after ingestion of food. Once released, GIP is subjected to NH2-terminal degradation by dipeptidyl peptidase-IV (DPP-IV), yielding GIP (3-42) as the primary metabolite which acts as a GIP receptor antagonist.

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

• Wolffbrandt et al (1986) The effects of porcine GIP on insulin secretion and glucose clearance in the pig. Horm Metab Res. 18(3) 159 PMID: 3516832
• Yamada et al (2006) Pancreatic and Extrapancreatic Effects of Gastric Inhibitory Polypeptide. Diabetes 55 (Supplement 2) S86 DOI: 10.2337/db06-S011
• Marks (2020) The early history of GIP 1969–2000: From enterogastrone to major metabolic hormone. Peptides 125 170276 PMID: 32081451

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.