Abcam, ab156962, Recombinant Human GlcAT-I protein

Size: 100µg
Recombinant Human GlcAT-I protein is a Human Fragment protein, in the 29 to 335 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, Mass Spec.
Key facts
Purity:>90% SDS-PAGE,
Expression system:Escherichia coli,
Tags:His tag N-Terminus,
Applications:Mass Spec, SDS-PAGESee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:No,
Accession:O94766,
Animal free:No,
Carrier free:No,
Species:Human,
Storage buffer:pH: 8Constituents: 10% Glycerol (glycerin, glycerine), 0.88% Sodium chloride, 0.32% Tris HCl, 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

Product details:
Previously labelled as B3GAT3.

Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage duration-1-2 weeks, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--20°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
GlcAT-I also known as glucuronyltransferase-I is an enzyme responsible for the transfer of glucuronic acid to various substrates. It catalyzes the formation of glycosaminoglycans by adding glucuronic acid to non-reducing ends. This protein has a molecular mass of approximately 38 kDa and expresses predominantly in tissues associated with the synthesis of glycosaminoglycans such as the liver and cartilage. GlcAT-I is an important component in glycoprotein and proteoglycan production playing an important role in cellular communication and structural integrity.
Biological function summary
The enzyme GlcAT-I has a central role in the biosynthesis of chondroitin sulfate dermatan sulfate and heparan sulfate. These glycosaminoglycans are part of proteoglycan complexes which are important for maintaining the biomechanical properties of tissues. Through its activity GlcAT-I contributes to the structural functionality of the extracellular matrix (ECM) serving essential functions in cellular adhesion and tissue repair. GlcAT-I modulates interactions that are integral to maintaining health and development of connective tissues.
Pathways
This enzyme operates significantly within the glycosaminoglycan biosynthesis pathway. GlcAT-I collaborates closely with other glycosyltransferases in the synthesis of proteoglycans influencing ECM organization and cell signaling pathways. It shares interactions with proteins such as decorin and biglycan which are essential components in the formation of the ECM. Through its function in these pathways GlcAT-I plays roles in cellular proliferation and differentiation processes.
Malfunctions in GlcAT-I activity connect to skeletal disorders such as osteoarthritis and Ehlers-Danlos syndrome. These conditions involve defects in ECM composition and its mechanical strength. Altered GlcAT-I function can influence the structural arrangement of proteins like aggrecan within the ECM leading to compromised tissue integrity and joint function. By understanding its involvement researchers can target GlcAT-I in therapeutic strategies for treating these disorders.