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AB283994

Human B3GAT3 ELISA Kit

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Human B3GAT3 ELISA Kit is a Sandwich (quantitative) ELISA for the measurement of Human B3GAT3 in Human in Biofluids, Cell Culture Media, Cell/Tissue Extracts samples.

View Alternative Names

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

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Sandwich ELISA - Human B3GAT3 ELISA Kit (AB283994)
  • sELISA

Supplier Data

Sandwich ELISA - Human B3GAT3 ELISA Kit (AB283994)

Example of Human B3GAT3 standard curve. Background-subtracted data values (mean +/- SD) are graphed.

Key facts

Detection method

Colorimetric

Sample types

Plasma, Cell culture supernatant, Serum, Cell Lysate

Reacts with

Human

Assay type

Sandwich (quantitative)

Sensitivity

= 1.8 ng/mL

Range

3.75 - 240 ng/mL

Assay time

5h

Assay Platform

Pre-coated microplate (12 x 8 well strips)

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "sELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Product details

The Human B3GAT3 ELISA (Enzyme-Linked Immunosorbent Assay) Kit is designed for detection of B3GAT3 in human plasma, serum, cell culture, and cell lysate samples.

This assay employs a quantitative sandwich enzyme immunoassay technique that measures human B3GAT3 in approximately 5 hours. A polyclonal antibody specific for human B3GAT3 has been pre-coated onto a 96-well microplate with removable strips. B3GAT3 in standards and samples is sandwiched by the immobilized antibody and a biotinylated polyclonal antibody specific for human B3GAT3, which is recognized by a streptavidin-peroxidase (SP) conjugate. All unbound material is washed away and a peroxidase enzyme substrate is added. The color development is stopped and the intensity of the color is measured.

Precision

[ { "reproducibilityType": "Inter", "sample": "Overall", "replicates": 60, "mean": null, "standardDeviation": null, "coefficientOfVariability": "10.2" }, { "reproducibilityType": "Intra", "sample": "Overall", "replicates": 60, "mean": null, "standardDeviation": null, "coefficientOfVariability": "5.3" } ]

What's included?

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Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
Multi
Storage information
Please refer to protocols

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.

Product protocols

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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