GLB1
GLB1 (galactosidase beta 1, also known as EBP and ELNR1) encodes a member of the glycosyl hydrolase 35 family. It gives rise to the lysosomal beta-galactosidase enzyme and is also linked to the elastin-binding protein that contributes to elastic fibre formation. Browse Assay Genie's current range of GLB1 research reagents below, or read on for the biology behind the target.
The GLB1 gene encodes a member of the glycosyl hydrolase 35 family. According to the NCBI Gene summary, at least one transcript variant encodes a preproprotein that is proteolytically processed into the mature lysosomal enzyme. This enzyme catalyses the hydrolysis of a terminal beta-linked galactose residue from ganglioside substrates and other glycoconjugates, which places it in the breakdown of glycoconjugates within the lysosome.
GLB1 also has a second, non-enzymatic identity. UniProt describes a form of the protein that has no beta-galactosidase catalytic activity but plays functional roles in the formation of extracellular elastic fibres (elastogenesis) and in the development of connective tissue. This form appears to be identical to the elastin-binding protein (EBP), a major component of a non-integrin cell surface receptor found on fibroblasts, smooth muscle cells, chondroblasts, leukocytes and certain cancer cell types. In elastin-producing cells it associates with tropoelastin intracellularly and acts as a recycling molecular chaperone, facilitating the secretion of tropoelastin and its assembly into elastic fibres.
The protein is annotated in the lysosome and in the perinuclear region of the cytoplasm, and alternative splicing produces multiple transcript variants. The gene was formerly named elastin receptor 1 (67 kDa), which accounts for the ELNR1 alias, and it belongs to the HGNC group of beta galactosidases. Mutations in GLB1 may result in GM1-gangliosidosis and Morquio B syndrome, making it a common reference point in lysosomal storage disease research. The mouse ortholog is Glb1.
Mutations in GLB1 may result in GM1-gangliosidosis and Morquio B syndrome, so the gene is central to studies of ganglioside and glycoconjugate turnover.
The elastin-binding form acts as a chaperone for tropoelastin and supports elastic fibre assembly and connective tissue development.
The mature lysosomal enzyme removes terminal beta-linked galactose from gangliosides and other glycoconjugates, making it a model glycosyl hydrolase 35 family member.
EBP is a major component of a non-integrin elastin receptor on fibroblasts, smooth muscle cells, chondroblasts, leukocytes and some cancer cells.
GLB1 encodes a lysosomal beta-galactosidase that hydrolyses terminal beta-linked galactose from gangliosides and other glycoconjugates. A form of the protein with no catalytic activity also acts as elastin-binding protein, chaperoning tropoelastin through secretion and into elastic fibres. Check the datasheet of any product for its validated reactivity.
The protein appears to be identical to the elastin-binding protein (EBP), part of a cell surface elastin receptor. The gene was previously named elastin receptor 1, 67kDa, which gives the ELNR1 alias. The current HGNC name is galactosidase beta 1, and UniProt lists the protein as beta-galactosidase.
Mutations in GLB1 may result in GM1-gangliosidosis and Morquio B syndrome, according to the NCBI Gene summary. The mouse ortholog is Glb1, which allows the gene to be studied in murine systems. Check the datasheet of any product for its validated reactivity.
Other lysosomal glycosidases, galactosidase family members and elastin-related targets with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P16278; product specifications from Assay Genie datasheets.