> 95 % as determined by SDS-PAGE
Please contact us for more information.
Testing in progress
A DNA sequence encoding the human GMFB (Met1-His142) was expressed.
The recombinant human GMFB consists of 142 amino acids and predicts a molecular mass of 16.7 KDa. It migrates as an approximately 17 KDa band in SDS-PAGE under reducing conditions.
Lyophilized from sterile PBS, pH 7.4
1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
2. Please contact us
for any concerns or special requirements.
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Stability & Storage
Samples are stable for up to twelve months from date of receipt at -70℃
Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
GMFB is a nerve growth factor which belongs to the actin-binding proteins ADF family, GMF subfamily. GMFB is involved in nervous system development, angiogenesis and immune function. It is especially crucial for the nervous system. GMFB causes brain cell differentiation, stimulates neural regeneration and inhibits tumor cell proliferation. It contains 1 ADF-H domain and is phosphorylated after phorbol ester stimulation. GMFB overexpression in astrocytes results in the increase of BDNF production. GMFB expression is increased by exercise, thus BDNF is important for exercise-induction of BDNF.
Kim W, et al. (2011) Systematic and quantitative assessment of the ubiquitin-modified proteome. Mol Cell. 44(2):325-40. Zaheer S, et al. (2011) Augmented expression of glia maturation factor in Alzheimer's disease. Neuroscience. 194:227-33. Danielsen JM, et al. (2011) Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level. Mol Cell Proteomics. 10(3):M110.003590.