Technical Articles: Reagent Chemistry, Synthesis & Bioscience Guides

Recombinant Human GFUS Protein: Properties & Applications

Recombinant Human GFUS Protein is a key enzyme in the de novo GDP-fucose biosynthesis pathway, enabling researchers to investigate fucosylation mechanisms, glycosylation disorders, and related therapeutic targets in vitro.

Product Name
Recombinant Human GFUS Protein
SKU
rp370814
Gene Name
GFUS (also known as TSTA3, FX)
Protein Function
Catalyzes the final two steps in de novo GDP-fucose biosynthesis (oxidoreductase activity)
Species
Human (Homo sapiens)
Expression System
Recombinant (expression host to be confirmed; see review flags)
Research Areas
Glycobiology, fucosylation, nucleotide sugar metabolism, cancer biology

Background: The GFUS Gene and Protein

GFUS (GDP-fucose synthase), also known as TSTA3 or FX, encodes a bifunctional enzyme that catalyzes the last two steps of the de novo GDP-L-fucose biosynthesis pathway. Specifically, the enzyme converts GDP-4-keto-6-deoxy-D-mannose first to GDP-4-keto-6-deoxy-L-galactose via an epimerase activity, and subsequently to GDP-L-fucose via an NADPH-dependent reductase activity.

Fucosylation — the addition of fucose residues to glycoproteins and glycolipids — is a critical post-translational modification that regulates cell adhesion, immune recognition, selectin-mediated leukocyte trafficking, and oncogenic signaling. GFUS occupies a central regulatory node in this pathway, making it an attractive target for basic research and for studies into cancer, inflammatory diseases, and congenital disorders of glycosylation.

Biochemical Properties of Recombinant Human GFUS Protein

Recombinant Human GFUS Protein (rp370814) is produced using a recombinant expression system and is intended to retain the native bifunctional enzymatic activities of the endogenous human protein. As a member of the short-chain dehydrogenase/reductase (SDR) superfamily, GFUS requires NADPH as a cofactor for its reductase activity.

Key biochemical characteristics include:

  • Dual enzymatic activity: 3,5-epimerase and 4-reductase functions operating sequentially on the same substrate.
  • Cofactor requirement: NADPH dependency for the reductase step.
  • Oligomeric state: GFUS is reported to function as a homotetramer under native conditions; researchers should verify the oligomeric state of the recombinant preparation under their specific assay conditions.

Note: Specific purity grade, formulation buffer, storage conditions, and molecular weight confirmation for rp370814 should be verified against the current product datasheet available from Aladdin Scientific.

Research Applications

Recombinant Human GFUS Protein is suitable for a range of in vitro biochemical and cell biology applications, including but not limited to:

  • Enzyme activity assays: Characterization of GDP-fucose synthase kinetics; substrate and inhibitor screening for drug discovery targeting the fucosylation pathway.
  • Glycobiology research: Investigating the regulation of cellular fucosylation levels and their downstream effects on glycoprotein function.
  • Cancer biology: GFUS expression is altered in certain cancers; recombinant protein supports mechanistic studies on tumor-associated glycan remodeling.
  • Structural studies: As a well-characterized SDR family member, GFUS protein can be used in crystallography or cryo-EM studies to support structure-based drug design.
  • Antibody production and validation: As an antigen for generating or validating anti-GFUS antibodies.

Researchers working in immunology may also find GFUS relevant, as fucosylation of selectin ligands is critical for leukocyte rolling and extravasation during inflammation.

Handling, Storage, and Quality Considerations

Recombinant proteins require careful handling to maintain activity. General best-practice guidelines applicable to Recombinant Human GFUS Protein include:

  • Storage: Store at –80 °C for long-term preservation. Avoid repeated freeze-thaw cycles, which can denature the protein and reduce enzymatic activity. Aliquot upon receipt.
  • Reconstitution: If supplied lyophilized, reconstitute in the buffer specified in the product datasheet. Centrifuge the vial briefly before opening to collect contents.
  • Working conditions: Maintain protein on ice during experimental setup. Include appropriate positive and negative controls in all activity assays.
  • Quality assurance: Aladdin Scientific recombinant proteins are subject to quality control testing; consult the Certificate of Analysis (CoA) for lot-specific purity, activity, and endotoxin data.

Always refer to the current product datasheet for rp370814 for authoritative storage, formulation, and handling instructions specific to this product.

Frequently asked questions

What is the biological function of the GFUS protein?

GFUS encodes a bifunctional enzyme — GDP-fucose synthase — that catalyzes the final two steps of the de novo GDP-L-fucose biosynthesis pathway via sequential 3,5-epimerase and NADPH-dependent 4-reductase activities. GDP-fucose is the essential donor substrate for all fucosyltransferases, making GFUS a master regulator of cellular fucosylation.

What expression system is used to produce Recombinant Human GFUS Protein (rp370814)?

The specific expression host used for rp370814 should be confirmed in the current product datasheet or Certificate of Analysis from Aladdin Scientific, as expression systems may include E. coli, insect cells, or mammalian cells depending on the production batch. Please contact Aladdin Scientific technical support for the most up-to-date specifications.

What research applications is Recombinant Human GFUS Protein suitable for?

Recombinant Human GFUS Protein is suitable for in vitro enzyme activity assays, inhibitor and substrate screening, structural biology studies, glycobiology research, cancer biology investigations, and use as an antigen for antibody generation or validation. It is particularly relevant for researchers studying fucosylation, nucleotide sugar metabolism, and glycan-mediated cell signaling.

How should Recombinant Human GFUS Protein be stored to maintain activity?

For long-term storage, keep the protein at –80 °C and avoid repeated freeze-thaw cycles by aliquoting upon receipt. During experiments, maintain the protein on ice. Always refer to the product-specific datasheet for rp370814 for authoritative storage and handling instructions.

Is Recombinant Human GFUS Protein suitable for use as an antigen?

Yes, recombinant proteins are commonly used as antigens for immunization to generate polyclonal or monoclonal antibodies, as well as for antibody validation assays such as ELISA and Western blot. Researchers should verify the antigenicity and purity specifications of rp370814 in the product datasheet before use.

References

  1. Tonetti M, Sturla L, Bisso A, Benatti U, De Flora A. Synthesis of GDP-L-fucose by the human FX protein. J Biol Chem. 1996;271(44):27274-27279.
  2. Becker DJ, Lowe JB. Fucose: biosynthesis and biological function in mammals. Glycobiology. 2003;13(7):41R-53R.
  3. Lütteke T, et al. GLYCOSCIENCES.de: an Internet portal to support glycomics and glycobiology research. Glycobiology. 2006;16(5):71R-81R.

Products are supplied for research and development use only. Not for use in humans, animals, diagnosis, or therapy.

Categories: Technical Articles: Reagent Chemistry, Synthesis & Bioscience Guides

Da — when not otherwise indicated, molecular weight units are daltons.   Mw — weight-average molecular weight.   Mn — number-average molecular weight.

Products are supplied for research and development use only. Not for use in humans, animals, diagnosis, or therapy.

Cite this article

Aladdin Scientific. "Recombinant Human GFUS Protein: Properties & Applications" Aladdin Knowledge Base, updated 31 ott 2026. https://www.aladdinsci.com/eu_it/faqs/recombinant-human-gfus-protein-properties-applications-en.html
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