CRAMP, rat

Product Name: CRAMP, rat

Sequence One Letter Code: GLVRKGGEKFGEKLRKIGQKIKEFFQKLALEIEQ

Sequence Three Letter Code: H-Gly-Leu-Val-Arg-Lys-Gly-Gly-Glu-Lys-Phe-Gly-Glu-Lys-Leu-Arg-Lys-Ile-Gly-Gln-Lys-Ile-Lys-Glu-Phe-Phe-Gln-Lys-Leu-Ala-Leu-Glu-Ile-Glu-Gln-OH

Chemical Formula:C181H302N50O48

Molecular Weight: 3946.9

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C

Research Area: Bacterial

Source / Species: rat

Conjugation: Unconjugated

Code Nacres: NA.26

Application: CRAMP (rat) is the rodent homolog of the human antimicrobial peptide LL-37 and is expressed in immune tissues, mucosal surfaces, and select regions of the central nervous system. It plays a central role in innate immune defense by exerting antimicrobial and immunomodulatory activities. In addition to pathogen defense, rCRAMP has been implicated in modulation of inflammatory responses and promotion of gastric mucosal healing. This peptide is widely used in research on host–pathogen interactions, mucosal immunity, neuroimmune communication, and tissue repair processes. It provides a relevant model for studying cathelicidin function in rodent systems and comparative antimicrobial peptide biology.

Current Research: CRAMP (rat), commonly referred to as rCRAMP, is the rat homolog of the human cathelicidin antimicrobial peptide LL-37. Like LL-37, it is derived from a larger precursor protein that undergoes proteolytic cleavage to release the active cationic peptide. rCRAMP is expressed in immune-related tissues, epithelial surfaces, and certain regions of the central nervous system, reflecting its broad role in host defense and immune regulation. Structurally, rCRAMP is an amphipathic, α-helical peptide with cationic properties that enable selective interaction with negatively charged microbial membranes. This interaction promotes membrane destabilization and permeabilization, leading to antimicrobial activity against a wide spectrum of pathogens, including Gram-positive and Gram-negative bacteria, as well as certain fungi. Its membrane-targeting mechanism contributes to rapid microbial killing and reduces susceptibility to classical resistance mechanisms. Beyond direct antimicrobial activity, rCRAMP functions as an immunomodulatory mediator. It influences cytokine production, chemotactic signaling, and immune cell recruitment. rCRAMP can modulate macrophage and neutrophil responses, regulate inflammatory mediator release, and participate in shaping early innate immune reactions. These activities position it as both an effector molecule and a signaling regulator within the innate immune network. In mucosal immunity, rCRAMP plays a protective role at epithelial barriers, including the gastrointestinal tract. Experimental models suggest involvement in gastric mucosal defense and healing processes, where it contributes to epithelial restitution and modulation of local inflammation. Its capacity to influence epithelial cell proliferation, migration, and wound repair parallels similar functions described for human LL-37, supporting its utility in tissue repair studies. rCRAMP is also relevant in studies of neuroimmune communication. Expression in select brain regions and glial populations indicates a potential role in central nervous system immune surveillance and inflammatory signaling. Investigations into cathelicidin peptides in the CNS explore their involvement in neuroinflammation, barrier integrity, and responses to infection or injury. rCRAMP provides a species-appropriate tool for examining these processes in rodent models. In host–pathogen interaction research, rCRAMP is used to evaluate bacterial susceptibility, immune signaling pathways, and inflammatory outcomes in vivo. Rodent infection models frequently assess how modulation of cathelicidin expression influences pathogen clearance, inflammatory burden, and survival. Additionally, rCRAMP contributes to studies examining interactions between antimicrobial peptides and microbial virulence factors. Because rCRAMP is the endogenous cathelicidin in rats, it serves as an important comparative model for understanding conserved and divergent features of cathelicidin biology across species. Comparative analyses between rCRAMP and LL-37 provide insight into structure–function relationships, receptor interactions, and context-dependent immunomodulatory effects. Such studies are valuable for translational research aiming to develop peptide-based therapeutics or immunomodulators. Methodologically, rCRAMP is applied in antimicrobial assays, cytokine profiling studies, chemotaxis experiments, epithelial barrier models, and wound-healing assays. It is also used in mechanistic investigations of membrane–peptide interactions and innate immune signaling pathways. Overall, CRAMP (rat) is a multifunctional antimicrobial and immunoregulatory peptide central to innate immune defense in rodent systems. Its roles in pathogen defense, inflammation modulation, mucosal protection, and tissue repair make it a versatile research tool for studying host–pathogen interactions, epithelial immunity, neuroimmune signaling, and comparative antimicrobial peptide biology.