Recombinant Human GlcAT-I protein (His tag N-Terminus)
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Recombinant Human GlcAT-I protein (His tag N-Terminus) is a Human Fragment protein, in the 29 to 335 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, Mass Spec.
대체 명칭 보기
Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3, Glucuronosyltransferase I, GlcAT-I, GlcUAT-I, B3GAT3
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human GlcAT-I protein (His tag N-Terminus) (AB156962)
15% SDS-PAGE analysis of ab156962 (3 µg).
Reactivity 정보
제품 세부 정보
서열 정보
특성 및 보관 정보
제형
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분주 정보
보관 정보
추가 정보
This supplementary information is collated from multiple sources and compiled automatically.
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.
일반 정보
기능
Glycosaminoglycans biosynthesis (PubMed : 25893793). Involved in forming the linkage tetrasaccharide present in heparan sulfate and chondroitin sulfate. Transfers a glucuronic acid moiety from the uridine diphosphate-glucuronic acid (UDP-GlcUA) to the common linkage region trisaccharide Gal-beta-1,3-Gal-beta-1,4-Xyl covalently bound to a Ser residue at the glycosaminylglycan attachment site of proteoglycans. Can also play a role in the biosynthesis of l2/HNK-1 carbohydrate epitope on glycoproteins. Shows strict specificity for Gal-beta-1,3-Gal-beta-1,4-Xyl, exhibiting negligible incorporation into other galactoside substrates including Galbeta1-3Gal beta1-O-benzyl, Galbeta1-4GlcNAc and Galbeta1-4Glc. Stimulates 2-phosphoxylose phosphatase activity of PXYLP1 in presence of uridine diphosphate-glucuronic acid (UDP-GlcUA) during completion of linkage region formation (PubMed : 24425863).
서열 유사성
Belongs to the glycosyltransferase 43 family.
Post-translational modifications
N-glycosylated.
타겟 정보
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