Recombinant Human EPFL9 protein

EPFL9 is a member of the EPIDERMAL PATTERNING FACTOR-LIKE (EPFL) family, a group of small secreted cysteine-rich proteins in plants. These proteins play critical roles in regulating developmental processes and stress responses by modulating cell-to-cell communication. EPFL9. specifically, has been studied in the context of plant growth regulation, particularly in Arabidopsis thaliana. It functions as a signaling peptide that interacts with receptor kinases, such as those in the ERECTA family, to coordinate tissue patterning and organ development.

Structurally, EPFL9 contains conserved cysteine residues that form disulfide bonds, stabilizing its tertiary structure and enabling interaction with target receptors. Its secretion is mediated by an N-terminal signal peptide, a hallmark of extracellular signaling molecules. Studies suggest EPFL9 is involved in fine-tuning stomatal development, vascular differentiation, and inflorescence architecture, though its exact mechanistic role remains under investigation. Unlike some EPFL members with well-defined functions (e.g., EPF1/2 in stomatal patterning), EPFL9 appears to have overlapping or context-dependent roles, potentially acting as a redundant or compensatory signaling component.

Recombinant EPFL9 protein is typically produced in heterologous systems like Escherichia coli or yeast for functional studies. Purified EPFL9 is used to explore ligand-receptor interactions, signaling pathways, and phenotypic effects in planta. Its recombinant form has applications in agricultural biotechnology, such as engineering crops with optimized growth traits or stress resilience. Current research focuses on deciphering its spatiotemporal expression patterns, post-translational modifications, and cross-talk with other signaling networks to harness its potential for improving plant productivity.