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AB156962

Recombinant Human GlcAT-I protein

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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.

View Alternative Names

Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3, Glucuronosyltransferase I, GlcAT-I, GlcUAT-I, B3GAT3

1 Images
SDS-PAGE - Recombinant Human GlcAT-I protein (AB156962)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human GlcAT-I protein (AB156962)

15% SDS-PAGE analysis of ab156962 (3 µg).

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE, Mass Spec

applications

Biologically active

No

Accession

O94766

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 10% Glycerol (glycerin, glycerine), 0.88% Sodium chloride, 0.32% Tris HCl, 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "Mass Spec": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Product details

Previously labelled as B3GAT3.
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Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMGSQPCDCLPPLRAAAEQLRQKDLRISQLQAELRRPPPAPAQPPEPEALPTIYVVTPTYARLVQKAELVRLSQTLSLVPRLHWLLVEDAEGPTPLVSGLLAASGLLFTHLVVLTPKAQRLREGEPGWVHPRGVEQRNKALDWLRGRGGAVGGEKDPPPPGTQGVVYFADDDNTYSRELFEEMRWTRGVSVWPVGLVGGLRFEGPQVQDGRVVGFHTAWEPSRPFPVDMAGFAVALPLLLDKPNAQFDSTAPRGHLESSLLSHLVDPKDLEPRAANCTRVLVWHTRTEKPKMKQEEQLQRQGRGSDPAIEV","proteinLength":"Fragment","predictedMolecularWeight":"36.4 kDa","actualMolecularWeight":null,"aminoAcidEnd":335,"aminoAcidStart":29,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"O94766","tags":[{"tag":"His","terminus":"N-Terminus"}]}]
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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
False
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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.
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Specifications

Form

Liquid

Additional notes

ab156962 was purified using conventional chromatography techniques.

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General info

Function

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).

Sequence similarities

Belongs to the glycosyltransferase 43 family.

Post-translational modifications

N-glycosylated.

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Product protocols

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Target data

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).
See full target information B3GAT3
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