CAMP Human

Cathelicidin Antimicrobial Peptide Human Recombinant
Cat. No.
BT29249
Source
Escherichia Coli.
Synonyms
CAP-18, CAP18, CRAMP, FALL-39, FALL39, HSD26, LL37, 18 kDa cationic antimicrobial protein, FALL-39 peptide antibiotic, Cathelicidin antimicrobial peptide.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description

CAMP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 163 amino acids (34-173 a.a.) and having a molecular mass of 18.4kDa.
CAMP is fused to a 23 amino acid His-tag at N-terminus.

Product Specs

Introduction
CAMP, a member of the antimicrobial peptide family, is characterized by a highly conserved N-terminal signal peptide, a cathelin domain, and a structurally diverse cationic antimicrobial peptide. Generated via extracellular proteolysis from the C-terminus, CAMP exhibits a range of functions beyond its antimicrobial properties, including cell chemotaxis, immune mediator induction, and the regulation of inflammatory responses.
Description
Recombinant Human CAMP, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 163 amino acids (34-173 a.a.) with a molecular mass of 18.4 kDa. This CAMP variant includes a 23 amino acid His-tag fused to its N-terminus.
Physical Appearance
A clear solution, sterilized by filtration.
Formulation
The CAMP protein solution (0.5 mg/ml) is formulated in a buffer containing 20 mM Tris-HCl (pH 8.0), 0.4 M urea, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), the solution should be kept at 4°C. For extended periods, storage at -20°C in a frozen state is advised. The addition of a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Repeated freeze-thaw cycles should be avoided.
Purity
Purity exceeding 90.0% as assessed by SDS-PAGE.
Synonyms
CAP-18, CAP18, CRAMP, FALL-39, FALL39, HSD26, LL37, 18 kDa cationic antimicrobial protein, FALL-39 peptide antibiotic, Cathelicidin antimicrobial peptide.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSQVLSYKE AVLRAIDGIN QRSSDANLYR LLDLDPRPTM DGDPDTPKPV SFTVKETVCP RTTQQSPEDC DFKKDGLVKR CMGTVTLNQA RGSFDISCDK DNKRFALLGD FFRKSKEKIG KEFKRIVQRI KDFLRNLVPR TES.

Product Science Overview

Introduction

Cathelicidin antimicrobial peptides (CAMPs) are a family of peptides that play a crucial role in the innate immune system of many organisms. The only human cathelicidin, known as LL-37, is derived from the precursor protein hCAP-18. This peptide is known for its broad-spectrum antimicrobial activity and its ability to modulate immune responses .

Discovery and Structure

The discovery of cathelicidins dates back to the 1980s when they were first isolated from bovine neutrophils. Human cathelicidin, hCAP-18, was later identified in 1995 from neutrophils . The active form, LL-37, consists of 37 amino acids and is characterized by a net positive charge and amphiphilic properties, which allow it to interact with and disrupt microbial membranes .

Production and Recombinant Technology

Recombinant production of LL-37 has been explored to meet the demand for this peptide in research and potential therapeutic applications. One method involves expressing the peptide in Escherichia coli using a fusion protein system. This approach has shown promise in producing high yields of the peptide, although challenges remain in ensuring the antimicrobial activity of the recombinant product .

Mechanism of Action

LL-37 exerts its antimicrobial effects through several mechanisms:

  1. Membrane Disruption: The peptide binds to the negatively charged bacterial membranes, leading to membrane destabilization and cell lysis .
  2. Immune Modulation: LL-37 can modulate the host immune response by promoting chemotaxis, enhancing the production of cytokines, and influencing the activity of various immune cells .
Therapeutic Potential

The therapeutic potential of LL-37 is significant, particularly in the treatment of infections caused by multi-drug resistant bacteria. Its ability to disrupt biofilms and promote wound healing makes it a promising candidate for treating chronic wounds and other infections . Additionally, LL-37 has been studied for its potential role in cancer therapy due to its immunomodulatory effects .

Challenges and Future Directions

Despite its potential, several challenges need to be addressed to fully harness the therapeutic benefits of LL-37:

  • Stability: Ensuring the stability of the peptide in biological environments is crucial.
  • Cytotoxicity: High concentrations of LL-37 can be cytotoxic, necessitating careful dosing and delivery strategies .
  • Resistance: Although resistance to antimicrobial peptides is less common, it remains a concern that needs ongoing monitoring .

Future research is focused on overcoming these challenges and exploring new applications for LL-37 in various fields of medicine.

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