Recombinant Human KLK11 protein

Kallikrein-related peptidase 11 (KLK11) is a serine protease encoded by the KLK11 gene, part of the human tissue kallikrein gene family located on chromosome 19q13.4. This family comprises 15 conserved serine proteases involved in diverse physiological processes, including hormone processing, skin desquamation, and inflammation. KLK11 is primarily expressed in hormone-regulated tissues (e.g., prostate, breast, ovary) and bodily fluids like seminal plasma and cerebrospinal fluid. It functions through proteolytic cleavage of substrates such as kininogens, extracellular matrix components, and other kallikreins, playing roles in tissue remodeling, cell signaling, and carcinogenesis.

Recombinant KLK11 refers to the engineered form of this protein produced in heterologous expression systems (e.g., Escherichia coli, mammalian cells) for research and therapeutic applications. Its production enables controlled study of KLK11's biochemical properties, substrate specificity, and regulatory mechanisms. Notably, KLK11 shows clinical relevance in cancer, with altered expression observed in prostate, ovarian, and breast cancers. Downregulation of KLK11 is linked to tumor progression and poor prognosis, suggesting potential as a diagnostic biomarker or therapeutic target.

Recombinant KLK11 is utilized to investigate its tumor-suppressive roles, including induction of apoptosis and inhibition of angiogenesis. Structural studies of the recombinant protein have identified critical residues for enzymatic activity and glycosylation patterns influencing stability. Challenges in production include maintaining proper post-translational modifications, often addressed using mammalian expression systems. Current research focuses on understanding its interaction networks and developing KLK11-based assays for early cancer detection. Its recombinant form remains vital for deciphering pathophysiological roles and translational applications in precision medicine.