Uses
Anti-GLG1 antibody produced in rabbit, a Prestige Antibody, is developed and validated by the Human Protein Atlas (HPA) project
(www.proteinatlas.org). Each antibody is tested by immunohistochemistry against hundreds of normal and disease tissues. These images can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. The antibodies are also tested using immunofluorescence and western blotting. To view these
protocols and other useful information about Prestige Antibodies and the HPA, visit .
General Description
GLG1 (golgi glycoprotein 1) is a type I transmembrane sialoglycoprotein, which is rich in cysteine residues. It is localized to the Golgi bodies, in the medial cisternae. This gene is located on human chromosome 16q22-q23. It is an FGF (fibroblast growth factor)-binding protein, independent of tyrosine kinase. It has a unique CFR (cysteine-rich fibroblast growth factor receptor) motif, of which 16 repeats are present in the extracellular domain. Its transmembrane domain consists of 21 amino acids, and its cytoplasmic domain has only 13 amino acids. Due to alternative splicing, a different isoform of GLG1 has an additional 24 amino acids in the cytoplasmic domain. This isoform is located in the Golgi apparatus, whereas the isoform with the shorter cytoplasmic tail is localized to the cell surface. It is ubiquitously expressed from an early embryonic stage to adulthood.
Biochem/physiol Actions
GLG1 (golgi glycoprotein 1) binds to FGF (fibroblast growth factor), as well as to E-selectin and TGFβ (transforming growth factor β). It regulates the function of TGFβ, by modulating its maturation and secretion. This protein interacts with FGF18 at the cell surface, and positively regulates the FGF18 signaling cascade. GLG1 might act as a chaperone protein by regulating the processing and targeting of basic fibroblast growth factor (bFGF), in the cell. This protein is also associated with malignant astrocytomas in humans, and might have a role in the malignancy of these tumors. It is suggested that GLG1 aids in binding of E-selectin to myeloid cells. It might also play a role in the initiation of leukocyte endothelial contact formation, as it is expressed in microvilli of leukocytes.
