The recombinant human GMFB protein is typically expressed in Escherichia coli (E. coli) and purified using conventional chromatography techniques . The protein consists of 142 amino acids and is fused to a His-tag at the N-terminus, which facilitates its purification and detection . The molecular weight of the recombinant GMFB is approximately 18.8 kDa .
GMFB is phosphorylated following phorbol ester stimulation and is essential for the nervous system . It stimulates the production of brain-derived neurotrophic factor (BDNF), which is crucial for brain function and plasticity . Overexpression of GMFB in astrocytes has been shown to enhance BDNF production . Additionally, GMFB expression is increased by exercise, highlighting its role in exercise-induced BDNF production .
Research has also indicated that GMFB is related to the production of nitric oxide (NO). It seems to induce the overexpression of inducible nitric oxide synthase (iNOS), leading to increased NO production . This process is p38 and ERK-dependent in endotoxin-stimulated glial cells .
The recombinant GMFB protein is typically stored in a buffer containing 20 mM Tris-HCl (pH 8.0), 0.1 M NaCl, 1 mM DTT, and 10% glycerol . For short-term storage, it can be kept at +4°C for 1-2 weeks. For long-term storage, it should be aliquoted and stored at -20°C or -70°C to avoid repeated freezing and thawing cycles .