Ziptide peptide

Ziptide peptide

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

Batch to batch variation of the purity

H-KKLNRTLSFAEPG-OH

H-Lys-Lys-Leu-Asn-Arg-Thr-Leu-Ser-Phe-Ala-Glu-Pro-Gly-OH

13

95.33%

C₆₅H₁₀₉N₁₉O₁₉

1460.67

Synthetic

Powder

Ziptide is a substrate peptide used routinely as a substrate for zipper interacting protein kinase (ZIPK), also known as death-associated protein kinase 3 (DAPK3), a serine/threonine kinase that functions in programmed cell death. Ziptide can also be used as a substrate for the other serine/threonine-protein kinases BRSK2, and maternal embryonic leucine zipper kinase (MELK).

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

• Witczak et al (2010) CaMKII regulates contraction- but not insulin-induced glucose uptake in mouse skeletal muscle. Am. J. Physiol. Endocrinol. Metab. 298(6) E1150 PMID: 20215576
• Yoshida and Goedert (2012) Phosphorylation of microtubule-associated protein tau by AMPK-related kinases. J. Neurochem. 120 165 PMID: 21985311

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.