ERO1L Human

ERO1L is an FAD-dependent protein disulfide oxidase. It works in conjunction with Protein Disulfide Isomerase (PDI) to catalyze the formation of disulfide bonds in nascent proteins. Disulfide bonds are critical for the structural integrity and function of many proteins. The activity of ERO1L is tightly regulated to ensure that the oxidative environment within the ER is maintained without causing excessive oxidative stress .

The primary function of ERO1L is to reoxidize PDI, which in turn catalyzes the formation of disulfide bonds in substrate proteins. ERO1L transfers electrons from PDI to molecular oxygen, producing hydrogen peroxide (H₂O₂) as a byproduct. This process is vital for the proper folding of secretory and membrane proteins .

Recombinant human ERO1L is produced using baculovirus expression systems in insect cells. The recombinant protein is typically tagged with a His-tag to facilitate purification. It is supplied as a carrier-free formulation, meaning it does not contain Bovine Serum Albumin (BSA), which can interfere with certain applications .

Recombinant ERO1L is used in various research applications, including:

• Protein Folding Studies: Understanding the mechanisms of protein folding and the role of disulfide bond formation.
• Oxidative Stress Research: Investigating the effects of oxidative stress and the role of ERO1L in maintaining ER homeostasis.
• Drug Development: Screening for compounds that can modulate the activity of ERO1L and PDI, which may have therapeutic potential for diseases related to protein misfolding .

Recombinant ERO1L is typically stored at -20 to -70°C to maintain its stability. It is important to avoid repeated freeze-thaw cycles to prevent degradation. The protein is supplied in a solution containing Tris, NaCl, and TCEP, which helps maintain its stability during storage .