Recombinant Human LL-37 protein (GST tag)

A DNA sequence encoding the Human LL-37 protein (P49913) (Leu134-Ser170) was expressed with a GST.

Introducing the Recombinant Human LL-37 Protein (GST Tag), a cutting-edge product meticulously engineered to revolutionize the field of protein research. This innovative protein, fused with the Glutathione S-transferase (GST) tag, offers unparalleled versatility and efficiency in various applications.

Crafted with utmost precision, this recombinant protein is derived from human LL-37, a naturally occurring antimicrobial peptide renowned for its potent immunomodulatory properties. The fusion with the GST tag not only facilitates purification but also enhances stability and solubility, ensuring optimal performance in diverse experimental settings.

The Recombinant Human LL-37 Protein (GST Tag) exhibits exceptional purity, surpassing industry standards, thereby guaranteeing reliable and reproducible results. Its high bioactivity enables comprehensive investigations into LL-37's multifaceted functions, including antimicrobial, anti-inflammatory, and wound healing activities.

This product's versatility extends to its compatibility with a wide range of research techniques, such as protein-protein interaction studies, enzyme assays, and cell-based assays. Its seamless integration into existing experimental protocols ensures seamless incorporation into ongoing projects, saving valuable time and resources.

Furthermore, the Recombinant Human LL-37 Protein (GST Tag) is meticulously manufactured under stringent quality control measures, adhering to the highest industry standards. Each batch undergoes rigorous testing to ensure consistency, purity, and functionality, guaranteeing utmost reliability and reproducibility.

In summary, the Recombinant Human LL-37 Protein (GST Tag) represents a breakthrough in protein research, offering an unrivaled combination of purity, stability, and versatility. With its exceptional bioactivity and compatibility with various techniques, this product is poised to revolutionize the understanding of LL-37's intricate mechanisms and pave the way for groundbreaking discoveries in the field of immunology and beyond.