mCRAMP (mouse) peptide

mCRAMP (mouse) peptide

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

Batch to batch variation of the purity

H-GLLRKGGEKIGEKLKKIGQKIKNFFQKLVPQPEQ-OH

H-Gly-Leu-Leu-Arg-Lys-Gly-Gly-Glu-Lys-Ile-Gly-Glu-Lys-Leu-Lys-Lys-Ile-Gly-Gln-Lys-Ile-Lys-Asn-Phe-Phe-Gln-Lys-Leu-Val-Pro-Gln-Pro-Glu-Gln-OH

34

95.04%

C₁₇₈H₃₀₂N₅₀O₄₆

3878.59

Synthetic

Powder

mCRAMP (mouse) or mouse calethicidin-related antimicrobial peptide, is the sole murine cathelicidin and intestinal homologue of human LL-37. mCRAMP expression in the intestinal tract is restricted to surface epithelial cells in the colon where it exhibits antimicrobial activity against enteric pathogens and it is established as a component of the innate antimicrobial defense in mice. mCRAMP deficiency has been linked to alcoholic liver disease (ALD) in mice and it also produces viral-induced responses in mouse cells. mCRAMP synergises wirh rifamycin for intracellular killing of mycobacteria.

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

• Gupta et al (2015) Short, Synthetic Cationic Peptides Have Antibacterial Activity against Mycobacterium smegmatis by Forming Pores in Membrane and Synergizing with Antibiotics. Antibiotics 4(3) 358 PMID: 27025629
• Yoo et al (2015) Antifibrogenic Effects of the Antimicrobial Peptide Cathelicidin in Murine Colitis-Associated Fibrosis. CMGH Cellular and Molecular Gastroenterology and Hepatology. 1(1) 55 PMID: 25729764
• Singh et al (2013) The human antimicrobial peptide LL-37, but not the mouse ortholog, mCRAMP, can stimulate signaling by poly(I:C) through a FPRL1-dependent pathway. J. Biol. Chem. 288(12) 8258 PMID: 23386607

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.