Crustacean hyperglycemic hormone precursor-related peptide CPRP 2

Crustacean hyperglycemic hormone precursor-related peptide CPRP 2

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

H-ALSSGHHSLS-OH

H-Ala-Leu-Ser-Ser-Gly-His-His-Ser-Leu-Ser-OH

10

95.67%

C₄₁H₆₆N₁₄O₁₅

995.04

Synthetic

Powder

Crustacean hyperglycemic hormone precursor-related peptide CPRP 2 is found in the water flea Daphnia pulex and is part of the CHHITP isoform. The CHHITP isoform is a member of the arthropod-specific neuropeptide family and is classified under the CHH subfamily, which contains a precursor-related peptide in its prepro-hormone. The CHH subfamily includes peptides involved in various physiological processes, such as ion transport and hyperglycemic activity.
The presence of a signal peptide and a Lys-Arg prohormone convertase cleavage sequence suggests that the precursor protein undergoes processing to produce the Crustacean hyperglycemic hormone precursor-related peptide CPRP 2.

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

• Gard AL, Lenz PH, Shaw JR, Christie AE. Identification of putative peptide paracrines/hormones in the water flea Daphnia pulex (Crustacea; Branchiopoda; Cladocera) using transcriptomics and immunohistochemistry. Gen Comp Endocrinol. 2009;160(3):271-87.

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.