NGB Human

Neuroglobin is a heme protein, meaning it contains a heme group that can bind oxygen. This property allows neuroglobin to augment oxygen supply to neurons, promoting their survival under hypoxic conditions (low oxygen levels) . The protein’s ability to bind oxygen is crucial for its role in protecting neurons from damage during events such as ischemic strokes or traumatic brain injuries .

Neuroglobin expression is upregulated in response to hypoxic conditions. This means that when neurons are deprived of oxygen, the production of neuroglobin increases, helping to mitigate the damage caused by the lack of oxygen . Studies have shown that inhibiting neuroglobin expression can reduce neuronal survival after hypoxia, while overexpression of neuroglobin can enhance neuronal survival .

Recombinant neuroglobin is produced using various expression systems, such as Escherichia coli (E. coli) or wheat germ . The recombinant protein is typically purified using techniques like size exclusion chromatography to ensure high purity and proper folding . The amino acid sequence of recombinant neuroglobin is identical to that of the native human protein, ensuring that it retains its biological functionality .

Recombinant neuroglobin is primarily used for research purposes. It is employed in studies investigating the protein’s role in neuroprotection, its potential therapeutic applications, and its involvement in various neurological conditions . The protein’s ability to protect neurons from hypoxic damage makes it a promising candidate for developing treatments for conditions such as stroke, traumatic brain injury, and neurodegenerative diseases .

Recombinant neuroglobin is typically lyophilized and stored at -20°C to maintain its stability . After reconstitution, it can be stored at 4°C for a limited period without significant loss of activity . It is important to avoid repeated freeze-thaw cycles to preserve the protein’s integrity .