Human/Mouse/Rat Golgi Glycoprotein 1/GLG1 Alexa Fluor™ Plus 594-conjugated Antibody

GLG1 (Golgi complex-Localized Glycoprotein 1; also CFR1, E-Selectin ligand-1/ESL-1, MG-160 and Cys-rich FGF receptor) is a 150-160 kDa (reducing; 130 kDa nonreducing) glycoprotein. It is expressed in both Golgi and/or the cell membrane of multiple cell types, including neutrophils (from rodents; not humans), liver stellate cells, neurons, cardiac myocytes, monocytes and bronchial epithelial cells. In the blood, GLG1/ESL-1 collaborates with PSGL-1 to mediate leukocyte binding to endothelial cell surfaces. PSGL-1 initiates leukocyte tethering while GLG1 promotes slow rolling. GLG1 also serves as an intra-Golgi receptor for multiple FGFs, including FGF-1, -2, -4, -18 and possibly -3, and as a component of an unusual latent TGF-beta complex. Mature human GLG1 is an 1150 amino acid (aa) type I transmembrane protein. It contains a 1116 aa extracellular/luminal region (aa 30-1145) plus a short 13 aa cytoplasmic segment. The extracellular region possesses a 16 aa poly-Gln segment followed by 16 Cys-rich repeats (aa 116-1101). There are three potential isoform variants, one of which possess a 24 aa extension at the C‑terminus, a second that couples the aforementioned C‑terminal extension to a deletion of aa 147-157, and a third that contains a 14 aa substitution for aa 685-1179. It is suggested that the longer C‑terminus retains GLG1 in the Golgi, while shorter cytoplasmic segments allow for presentation at the cell membrane. Over aa 1048‑1145, human and mouse are identical in aa sequence.