Enolase-1 is a multifunctional enzyme with a molecular mass of approximately 49.3 kDa . It catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate, a critical step in glycolysis. Beyond its glycolytic function, Enolase-1 also acts as a plasminogen receptor on the cell surface, particularly in tumors, where it contributes to cancer cell proliferation, migration, invasion, and metastasis .
Enolase-1 is involved in various physiological and pathological processes. It is predominantly expressed during the early stages of embryonic development . In cancer biology, Enolase-1 overexpression and post-translational modifications are of diagnostic and prognostic value in many cancer types . The enzyme’s role in anaerobic metabolism under hypoxic conditions makes it a critical player in tumor progression and survival .
Recombinant human Enolase-1 is produced using DNA sequences encoding the human ENO1 gene, typically expressed in Escherichia coli . The recombinant protein is often tagged with polyhistidine for purification purposes and is verified for purity using techniques like SDS-PAGE and HPLC . It is commonly used in research to study its biochemical properties, interactions, and potential as a therapeutic target.
Recombinant Enolase-1 is valuable in various research applications, including:
Recombinant Enolase-1 is typically lyophilized and stored at -20°C to -80°C to maintain its stability and activity. It is recommended to avoid repeated freeze-thaw cycles to preserve its integrity .
Enolase-1’s multifunctional nature and involvement in critical biological processes make it a significant focus of research, particularly in understanding cancer biology and developing potential therapeutic interventions.