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AB171721

Recombinant Human FUT3 protein (denatured)

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Recombinant Human FUT3 protein (denatured) is a Human Fragment protein, in the 35 to 361 aa range, expressed in Escherichia coli, with >80%, suitable for SDS-PAGE.

View Alternative Names

FT3B, LE, FUT3, 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase FUT3, 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase, Alpha-3-fucosyltransferase FUT3, Blood group Lewis alpha-4-fucosyltransferase, Fucosyltransferase 3, Fucosyltransferase III, Lewis FT, FucT-III

1 Images
SDS-PAGE - Recombinant Human FUT3 protein (denatured) (AB171721)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human FUT3 protein (denatured) (AB171721)

15% SDS-PAGE analysis of ab171721 (3 μg).

Key facts

Purity

>80% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

P21217

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 10% Glycerol (glycerin, glycerine), 2.4% Urea, 0.32% Tris HCl

storage-buffer

Reactivity data

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

Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMGSRVSRDDATGSPRAPSGSSRQDTTPTRPTLLILLWTWPFHIPVALSRCSEMVPGTADCHITADRKVYPQADTVIVHHWDIMSNPKSRLPPSPRPQGQRWIWFNLEPPPNCQHLEALDRYFNLTMSYRSDSDIFTPYGWLEPWSGQPAHPPLNLSAKTELVAWAVSNWKPDSARVRYYQSLQAHLKVDVYGRSHKPLPKGTMMETLSRYKFYLAFENSLHPDYITEKLWRNALEAWAVPVVLGPSRSNYERFLPPDAFIHVDDFQSPKDLARYLQELDKDHARYLSYFRWRETLRPRSFSWALDFCKACWKLQQESRYQTVRSIAAWFT","proteinLength":"Fragment","predictedMolecularWeight":"40.6 kDa","actualMolecularWeight":null,"aminoAcidEnd":361,"aminoAcidStart":35,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P21217","tags":[{"tag":"His","terminus":"N-Terminus"}]}]

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

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The FUT3 protein also known as fucosyltransferase 3 plays an important role in catalyzing the addition of fucose a type of sugar to precursor carbohydrates. This process is essential for the synthesis of Lewis blood group antigens. The molecular mass of FUT3 is approximately 43 kDa. It is mainly expressed in the gastrointestinal tract and liver though its presence is also noted in other tissues to a lesser extent.
Biological function summary

FUT3 contributes to the formation of fucosylated oligosaccharide structures on glycoproteins and glycolipids. It is not strictly part of a multi-protein complex but works closely intertwined with other glycosyltransferases for effective oligosaccharide biosynthesis. FUT3's activity influences cell-cell recognition and signaling processes by modifying cell surface carbohydrate structures.

Pathways

FUT3 is heavily involved in glycosphingolipid biosynthesis and the metabolic pathway of glycan structures. FUT3 works together with other fucosyltransferases such as FUT1 and FUT2 in these pathways dictating the structural diversity and functionality of various glycoconjugates. These pathways are important for cellular interactions and communication impacting blood group antigen expression.

Mutations or altered expression of FUT3 have connections with certain cancers and leukocyte adhesion deficiencies. In specific colorectal and gastric cancers changes in FUT3 expression levels correlate with tumor progression and metastasis. FUT3 also interacts with proteins like E-selectin in immune-related disorders affecting leukocyte extravasation and inflammation processes.

Specifications

Form

Liquid

Additional notes

ab17121 was purified by anion-exchange and gel-filtration chromatography techniques.

General info

Function

Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to both the subterminal N-acetyl glucosamine (GlcNAc) of type 1 chain (beta-D-Gal-(1->3)-beta-D-GlcNAc) glycolipids and oligosaccharides via an alpha(1,4) linkage, and the subterminal glucose (Glc) or GlcNAc of type 2 chain (beta-D-Gal-(1->4)-beta-D-GlcNAc) oligosaccharides via an alpha(1,3) linkage, independently of the presence of terminal alpha-L-fucosyl-(1,2) moieties on the terminal galactose of these acceptors (PubMed : 11058871, PubMed : 12668675, PubMed : 1977660). Through its catalytic activity, participates in the synthesis of antigens of the Lewis blood group system, i.e. Lewis a (Le(a)), lewis b (Le(b)), Lewis x/SSEA-1 (Le(x)) and lewis y (Le(y)) antigens (PubMed : 11058871, PubMed : 12668675, PubMed : 1977660). Also catalyzes the transfer of L-fucose to subterminal GlcNAc of sialyl- and disialyl-lactotetraosylceramide to produce sialyl Lewis a (sLe(a)) and disialyl Lewis a via an alpha(1,4) linkage and therefore may regulate cell surface sLe(a) expression and consequently regulates adhesive properties to E-selectin, cell proliferation and migration (PubMed : 11058871, PubMed : 12668675, PubMed : 27453266). Catalyzes the transfer of an L-fucose to 3'-sialyl-N-acetyllactosamine by an alpha(1,3) linkage, which allows the formation of sialyl-Lewis x structure and therefore may regulate the sialyl-Lewis x surface antigen expression and consequently adhesive properties to E-selectin (PubMed : 11058871, PubMed : 29593094). Prefers type 1 chain over type 2 acceptors (PubMed : 7721776). Type 1 tetrasaccharide is a better acceptor than type 1 disaccharide suggesting that a beta anomeric configuration of GlcNAc in the substrate is preferred (PubMed : 7721776). Lewis-positive (Le(+)) individuals have an active enzyme while Lewis-negative (Le(-)) individuals have an inactive enzyme (PubMed : 1977660).

Sequence similarities

Belongs to the glycosyltransferase 10 family.

Post-translational modifications

Glycosylated.

Product protocols

Target data

Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to both the subterminal N-acetyl glucosamine (GlcNAc) of type 1 chain (beta-D-Gal-(1->3)-beta-D-GlcNAc) glycolipids and oligosaccharides via an alpha(1,4) linkage, and the subterminal glucose (Glc) or GlcNAc of type 2 chain (beta-D-Gal-(1->4)-beta-D-GlcNAc) oligosaccharides via an alpha(1,3) linkage, independently of the presence of terminal alpha-L-fucosyl-(1,2) moieties on the terminal galactose of these acceptors (PubMed : 11058871, PubMed : 12668675, PubMed : 1977660). Through its catalytic activity, participates in the synthesis of antigens of the Lewis blood group system, i.e. Lewis a (Le(a)), lewis b (Le(b)), Lewis x/SSEA-1 (Le(x)) and lewis y (Le(y)) antigens (PubMed : 11058871, PubMed : 12668675, PubMed : 1977660). Also catalyzes the transfer of L-fucose to subterminal GlcNAc of sialyl- and disialyl-lactotetraosylceramide to produce sialyl Lewis a (sLe(a)) and disialyl Lewis a via an alpha(1,4) linkage and therefore may regulate cell surface sLe(a) expression and consequently regulates adhesive properties to E-selectin, cell proliferation and migration (PubMed : 11058871, PubMed : 12668675, PubMed : 27453266). Catalyzes the transfer of an L-fucose to 3'-sialyl-N-acetyllactosamine by an alpha(1,3) linkage, which allows the formation of sialyl-Lewis x structure and therefore may regulate the sialyl-Lewis x surface antigen expression and consequently adhesive properties to E-selectin (PubMed : 11058871, PubMed : 29593094). Prefers type 1 chain over type 2 acceptors (PubMed : 7721776). Type 1 tetrasaccharide is a better acceptor than type 1 disaccharide suggesting that a beta anomeric configuration of GlcNAc in the substrate is preferred (PubMed : 7721776). Lewis-positive (Le(+)) individuals have an active enzyme while Lewis-negative (Le(-)) individuals have an inactive enzyme (PubMed : 1977660).
See full target information FUT3

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