This recombinant Human CLDN6 protein is a partial protein produced via in vitro expression in E. coli (cell-free). It boasts a purity exceeding 90%, as determined by SDS-PAGE. Cell-free protein expression is a technique that involves in vitro protein synthesis using translation-compatible extracts derived from whole cells. Essentially, these extracts contain all the necessary macromolecules and components for transcription, translation, and even post-translational modifications. These components include RNA polymerase, regulatory protein factors, transcription factors, ribosomes, and tRNA. When supplemented with cofactors, nucleotides, and the specific gene template, these extracts can synthesize proteins of interest within a few hours.
CLDN6 is a tight junction molecule that plays a crucial role in cell-to-cell adhesion within epithelial or endothelial cell sheets, contributing to the maintenance of cell integrity. CLDN6 is indispensable for the formation of barriers, particularly the lung epithelial barrier and the epidermal permeability barrier (EPB), which effectively prevent the free passage of solutes and water through the extracellular space. CLDN6 exhibits aberrant expression in various malignancies, including ovarian cancer and testicular cancer. It has been implicated in cancer initiation, proliferation, apoptosis, migration, invasion, and progression. Furthermore, its abnormal expression is associated with Hepatitis C infection.