Recombinant Human DEFb1 protein

**Background of Recombinant DEFb1 Protein**

Recombinant DEFb1 (Human Beta-Defensin 1) is a synthetic version of the naturally occurring antimicrobial peptide encoded by the *DEFB1* gene in humans. Defensins are small cationic peptides integral to innate immunity, acting as first-line defenders against pathogens. DEFb1. a member of the β-defensin family, is constitutively expressed in epithelial cells lining mucosal surfaces, skin, and organs like the kidneys and lungs. Its primary role involves disrupting microbial membranes through electrostatic interactions, neutralizing bacteria, fungi, and enveloped viruses. Additionally, DEFb1 exhibits immunomodulatory functions, such as recruiting immune cells (e.g., dendritic cells, T-cells) via chemotaxis, bridging innate and adaptive immunity.

The recombinant form is produced using biotechnological platforms (e.g., *E. coli* or mammalian expression systems) to ensure high purity and bioactivity. This allows scalable production for research and therapeutic applications. Studies highlight DEFb1’s dual role: while it protects against infections, dysregulation is linked to chronic inflammation, autoimmune diseases, and cancer progression. For instance, reduced DEFb1 expression correlates with increased susceptibility to urinary tract infections, while overexpression in tumors may influence microenvironment interactions.

Recent research explores recombinant DEFb1’s therapeutic potential, including antimicrobial coatings, wound healing agents, and adjuvants in vaccines. Its ability to enhance epithelial barrier function and modulate immune responses positions it as a candidate for treating infections, inflammatory disorders, and even as a biomarker for certain cancers. However, challenges like stability in physiological conditions and delivery efficiency require further optimization. Understanding DEFb1’s structure-function relationships and signaling pathways (e.g., CCR6 receptor binding) remains critical for advancing its clinical translation.