Recombinant Human B4GALT6 Protein, N-His from ProteoGenix; catalogue ARO-P11173; research use only.
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Recombinant human B4GALT6 protein, also known as beta-1,4-galactosyltransferase 6, is a glycosyltransferase enzyme that plays a crucial role in the biosynthesis of complex glycoproteins. This protein is encoded by the B4GALT6 gene and is involved in the transfer of galactose residues from UDP-galactose to N-acetylglucosamine (GlcNAc) residues on glycoproteins. The recombinant form of this protein is produced through genetic engineering techniques and has numerous applications in the field of biotechnology and medicine.
The recombinant human B4GALT6 protein is a 413 amino acid long polypeptide with a molecular weight of approximately 47 kDa. It contains a conserved catalytic domain and a C-terminal transmembrane domain. The catalytic domain consists of a GT-A fold, which is a common structural motif found in glycosyltransferases. This domain is responsible for the transfer of galactose from UDP-galactose to the acceptor substrate. The transmembrane domain anchors the protein to the endoplasmic reticulum, where it carries out its function in glycosylation.
The primary function of recombinant human B4GALT6 protein is to catalyze the addition of galactose residues to glycoproteins, a process known as galactosylation. This enzymatic activity is essential for the proper folding and function of glycoproteins, as well as for their recognition by other molecules in the body. B4GALT6 is highly specific for N-acetylglucosamine (GlcNAc) residues, which are found on the core structure of many glycoproteins. By adding galactose to these residues, B4GALT6 contributes to the diversity and complexity of glycoproteins, which are involved in various biological processes such as cell signaling, immune response, and cell adhesion.
In addition to its role in galactosylation, recombinant human B4GALT6 protein has also been shown to have sialyltransferase activity. This means that it can also transfer sialic acid residues to glycoproteins, further increasing the diversity of glycoprotein structures. Sialylation is important for the stability and function of glycoproteins, and deficiencies in this process have been linked to various diseases.
The recombinant form of B4GALT6 has a wide range of applications in both research and medicine. One of the main uses of this protein is in the study of glycosylation and its role in various biological processes. By manipulating the expression or activity of B4GALT6, researchers can investigate the effects of glycosylation on different cellular functions and disease states. In addition, recombinant B4GALT6 can be used to produce glycoproteins with specific glycan structures, which can be used as tools for studying protein-protein interactions and as potential therapeutic agents.
Recombinant human B4GALT6 protein also has potential clinical applications. Mutations in the B4GALT6 gene have been associated with a rare genetic disorder called Ehlers-Danlos syndrome progeroid type 2 (EDS-P2). This syndrome is characterized by a range of symptoms including joint hypermobility, skin hyperextensibility, and premature aging. Studies have shown that recombinant B4GALT6 protein can correct the abnormal glycosylation patterns observed in EDS-P2 patients, providing a potential therapeutic approach for this disease.
Furthermore, recombinant B4GALT6
ProteoGenix catalogue number ARO-P11173. For research use only.
Host: Escherichia coli (E.coli); Expression system: Prokaryotic expression; Molecular weight: 32.93 kDa; Fragment: Glu125-Tyr382; Buffer: Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol..
Available configurations: 50ug, 100ug, 1mg.
This product is manufactured by ProteoGenix and sold through ABMIUM without relabelling.
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