Description
Key facts
Detection method:Colorimetric,
Sample types:Serum, Plasma, Cell culture supernatant,
Reacts with:Human,
Assay type:Sandwich (quantitative),
Sensitivity:= 0.32 ng/mL,
Range:0.32 - 80 ng/mL,
Assay Platform:Pre-coated microplate (12 x 8 well strips)
Product details:
Human B4GALT1 ELISA Kit is an in vitro enzyme-linked immunosorbent assay for the quantitative measurement of human B4GALT1 in serum, plasma, and cell culture supernatants. This assay employs an antibody specific for human B4GALT1 coated on a 96-well plate
Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage conditions--20°C, Appropriate long-term storage conditions--20°C, Storage information--20°C
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
B4GALT1 also known as beta-14-galactosyltransferase 1 is an enzyme that facilitates the transfer of galactose residues from UDP-galactose to acceptor sugars forming β1-4 galactosidic linkages. This enzyme has an approximate mass of 60 kDa. It is primarily expressed in the Golgi apparatus of many cell types including epithelial cells and fibroblasts. B4GALT1 represents one of seven beta-14-galactosyltransferase enzymes each with varying specificity and function depending on the tissue type.
Biological function summary
B4GALT1 plays an important role in the modification of glycoproteins and glycolipids. It acts as part of a larger complex responsible for the formation and maintenance of glycan structures on cellular proteins which are important for cell-cell communication and protein stability. This modification process is essential for normal cellular functions because it impacts protein folding secretion and cell surface expression. B4GALT1 achieves this by participating in the synthesis of N-linked and O-linked glycans which directly influences various physiological processes.
Pathways
B4GALT1 functions in the glycosylation pathway where it modifies oligosaccharide chains during protein post-translational modification. This pathway is essential for the synthesis of glycoproteins which play a role in cell adhesion and signaling. B4GALT1 also contributes to the protein N-glycosylation metabolic pathway and interacts with proteins like ST3GAL1 which modify glycan structures further. These pathways are indispensable for proper cellular communication and function.
Defects or dysregulation of B4GALT1 can lead to conditions such as congenital disorders of glycosylation. Mutations in this enzyme have been linked to neurological and developmental abnormalities due to impaired glycan synthesis. B4GALT1 has also shown relevance in cancer influencing tumor progression and metastasis. It interacts with MUC1 a protein that when aberrantly glycosylated can promote cancer cell invasiveness and impede immune response therefore affecting cancer prognosis.
