Brefeldin A is a fungal antibiotic that interferes with protein transport from the endoplasmic reticulum to the Golgi complex. Golgi brefeldin A-resistant guanine nucleotide exchange factor 1 (GBF1) regulates the recruitment of proteins to membranes by mediating the GDP to GTP exchange pathway. It is a member of the Sec7 domain family, and confers resistance to the action of brefeldin A It activates ADP ribosylation factor 1 (ARF1), thus blocking the first step in brefeldin A-mediated inhibition of GDP-GTP exchange. Phosphorylation of GBF1 at Thr(1337) by AMP-activated protein kinase has been shown to attenuate GBF1 activity. GBF1 is also known as BFA-resistant GEF 1, Golgi-specific brefeldin A resistance factor 1, ARF1GEF, and KIAA0248.
These products are affinity-purified IgG antibodies that recognize human GBF1 protein. The antibodies were raised in rabbit using synthetic peptides, and can be used for Western blot (WB) detection or immunoprecipitation (IP) of human GBF1 protein.