Types, Functions and Research Tools of Fucosylation Modification

Fucosylation is an important type of glycosylation modification. It refers to the process by which L-fucose is attached to glycan chains of glycoproteins or glycolipids through specific glycosidic linkages. This modification widely participates in cell recognition, receptor signaling, immune regulation, embryonic development, mucosal barrier function and disease progression, and is an important molecular mechanism connecting glycan structural changes with cellular functional phenotypes.

 

Keywords: fucosylation; core fucose; terminal fucose; FUT; POFUT; lectin; glycan detection; immune regulation

 

1 Conceptual Basis of Fucosylation Modification

1.1 Definition of the Modification

(1) Attachment of fucose residues

Fucosylation refers to the process in which L-fucose residues are attached to N-glycans, O-glycans or glycolipid glycans under the catalysis of fucosyltransferases. Fucose usually participates in linkage in the α configuration and can form different glycosidic linkages, including α1,2, α1,3, α1,4 and α1,6. Different linkage types correspond to different glycan structures and determine functional differences in cell recognition, receptor regulation and immune responses.

(2) Regulation of glycan structure

Fucosylation does not change the amino acid sequence of proteins, but it can significantly affect glycoprotein conformational stability, receptor affinity, cell-surface recognition features and secreted protein function. The biological activities of many receptors, adhesion molecules, immunoglobulins and secreted glycoproteins are related to their fucosylation status.

(3) Dynamic regulatory features

Fucosylation levels are influenced by cell type, developmental stage, metabolic status, inflammatory stimulation, tumor microenvironment and microbiota. GDP-L-fucose donor levels, fucosyltransferase expression, Golgi transport capacity and glycan substrate accessibility jointly determine the final modification pattern.

 

1.2 Main Modification Types

(1) Core fucosylation

Core fucosylation usually refers to the attachment of fucose to the reducing-end GlcNAc of N-glycans through an α1,6 linkage, mainly catalyzed by FUT8. This modification can affect the functions of growth factor receptors, integrins, the Fc region of immunoglobulins and various cell-surface glycoproteins. It is an important direction in receptor signaling and antibody effector function research.

(2) Terminal fucosylation

Terminal fucosylation mainly occurs on the outer arms of glycan chains and can form structures such as H antigen, Lewis antigen and sialyl Lewis X. This type of modification is more involved in cell adhesion, leukocyte recruitment, inflammatory responses, tumor metastasis and mucosal epithelial recognition.

(3) O-fucosylation

O-fucosylation refers to the direct attachment of fucose to serine or threonine residues of proteins. POFUT1 and POFUT2 are key enzymes in this type of modification. O-fucosylation is closely related to Notch signaling, developmental regulation, cell fate determination and the function of extracellular matrix-related proteins.

 

2 Synthesis and Regulation of Fucosylation

2.1 GDP-L-Fucose Supply

(1) De novo synthesis pathway

Intracellular GDP-L-fucose is mainly generated from GDP-mannose and is an important source for maintaining basal fucosylation levels. This pathway depends on sugar nucleotide metabolism and the overall cellular energy state, so abnormal glucose metabolism may indirectly affect fucosylation modification.

(2) Salvage synthesis pathway

Exogenous L-fucose can be converted into GDP-L-fucose through the salvage synthesis pathway. This pathway allows cells to adjust glycan modification levels according to environmental fucose supply and is suitable for studying nutritional supplementation, mucosal glycans, microbial interactions and fucose metabolism regulation.

(3) Donor transport process

GDP-L-fucose needs to enter the Golgi lumen before it can serve as a donor for fucosyltransferases in glycan modification. SLC35C1 is an important GDP-fucose transporter-related molecule. If transport is limited, glycan fucosylation deficiency may occur even when intracellular donor levels are sufficient.

 

2.2 Fucosyltransferases

(1) FUT8

FUT8 is the key enzyme for core α1,6 fucosylation. Changes in its activity can affect the functions of glycoproteins such as EGFR, TGF-β receptor, integrins and the IgG Fc region. FUT8-related studies often focus on receptor signaling, tumor progression, antibody effector function and tissue fibrosis.

(2) FUT1 and FUT2

FUT1 and FUT2 mainly participate in α1,2 fucosylation and are associated with H antigen, blood group-related glycans, epithelial surface glycans and mucosal secretory glycans. FUT2 is highly significant in studies of intestinal mucosa, microbial colonization and mucosal immunity.

(3) FUT3, FUT4, FUT6 and FUT7

These enzymes mostly participate in α1,3 or α1,4 fucosylation, forming Lewis antigens and selectin ligand-related structures. They are closely related to leukocyte adhesion, inflammatory cell recruitment, tumor cell migration and vascular endothelial interaction.

(4) POFUT1 and POFUT2

POFUT1 mainly participates in O-fucosylation of EGF-like repeat domains in Notch receptors and affects Notch signal transduction. POFUT2 is associated with O-fucosylation of proteins containing thrombospondin type 1 repeat domains and participates in extracellular matrix regulation, secreted protein maturation and tissue morphogenesis.

 

3 Biological Functions of Fucosylation

3.1 Cell Recognition and Adhesion

(1) Cell-surface glycan recognition

Fucosylated glycans can serve as cell-surface recognition markers and be recognized by lectins, selectins or other glycan-binding proteins. This process participates in immune cell migration, cell-cell contact, vascular endothelial interaction and tissue localization.

(2) Selectin-mediated adhesion

Terminal fucosylated structures are important components of selectin ligands. Leukocyte rolling, adhesion and extravasation at inflammatory sites depend on interactions between glycan structures and vascular endothelial selectins. FUT4-, FUT6- and FUT7-related fucosylation is commonly used to analyze inflammatory recruitment and immune cell migration.

(3) Tumor cell adhesion and metastasis

Increased fucosylation on the surface of tumor cells can enhance their interactions with endothelial cells, platelets or the extracellular matrix, thereby promoting intravascular retention, tissue invasion and distant metastasis. Terminal Lewis-type structures and changes in core fucosylation may both participate in tumor progression.

 

3.2 Regulation of Receptor Signaling

(1) Growth factor receptors

Core fucosylation can affect the conformation, membrane localization and ligand-binding capacity of various receptors. Changes in the fucosylation of glycoprotein receptors such as EGFR, TGF-β receptor and integrins may alter downstream phosphorylation signaling and cellular proliferation, migration and differentiation capacity.

(2) Integrin function

Integrins are important receptors connecting cells with the extracellular matrix. Their fucosylation status can affect focal adhesion formation, cell spreading, migration speed and mechanical responses. Abnormal core fucosylation is often associated with tumor migration, tissue fibrosis and extracellular matrix remodeling.

(3) Immune receptor activity

Immunoglobulins and many immune receptors can carry fucosylation modifications. Core fucose levels in the IgG Fc region affect its binding ability to FcγRIIIa, thereby regulating antibody-dependent cellular cytotoxicity.

 

3.3 Development and Tissue Homeostasis

(1) Embryonic development

Fucosylation participates in cell differentiation, tissue boundary formation and cell migration. During development, glycan structures show temporal and spatial specificity, and fucosylation changes can affect cell fate determination and signaling pathway responses.

(2) Regulation of Notch signaling

O-fucosylation plays an important regulatory role in Notch receptor function. POFUT1-mediated O-fucose modification affects Notch receptor maturation, ligand binding and signal activation, and is therefore closely related to neural development, vascular formation, immune differentiation and tissue regeneration.

(3) Mucosal barrier homeostasis

Fucosylated glycans on mucosal epithelial surfaces such as the intestine and respiratory tract are associated with barrier function, microbial colonization and immune tolerance. FUT2-related secretory fucosylation can affect gut microbiota composition, pathogen adhesion and mucus layer stability.

 

4 Fucosylation and Immune Regulation

4.1 Innate Immunity

(1) Pathogen recognition

Some pathogens can recognize host fucosylated glycans and use them as adhesion and invasion sites. Changes in host cell-surface glycan patterns may affect pathogen colonization efficiency and may also alter mucosal microbial ecology.

(2) Inflammatory cell recruitment

Fucosylated selectin ligands participate in the recruitment of neutrophils, monocytes and lymphocytes to inflammatory sites. If these glycan structures are abnormal, the efficiency of inflammatory cell entry into tissues and the intensity of inflammatory responses may both change.

(3) Glycan-recognition receptors

C-type lectins, mannose-binding lectin and some immune-related glycan-binding proteins can recognize glycan structures on cell surfaces or pathogen surfaces. Although not all lectins directly recognize fucose structures, they are commonly used in glycan recognition, immune response and glycosylation microenvironment evaluation.

 

4.2 Adaptive Immunity

(1) Antibody effector function

Core fucose content in the IgG Fc region is an important factor affecting antibody effector function. Low-fucosylated IgG usually has stronger binding ability to FcγRIIIa and can enhance ADCC effects. This mechanism has important value in therapeutic antibody engineering and immunotherapy.

(2) T cell regulation

Glycan modifications on the T cell surface can affect cell activation, migration and immune synapse formation. Fucosylation changes may alter interactions between T cells and antigen-presenting cells or vascular endothelium.

(3) Immune tolerance and autoimmunity

Abnormal fucosylation can change immune recognition thresholds and inflammatory response intensity, and has potential research value in autoimmune diseases, chronic inflammation and immune imbalance-related diseases.

 

5 Association Between Fucosylation and Disease

5.1 Tumorigenesis and Tumor Progression

(1) Abnormal expression

Abnormal expression of FUT family enzymes is observed in many tumors, leading to changes in core fucosylation or terminal fucosylation levels. These changes can affect tumor cell proliferation, invasion, metastasis, angiogenesis and immune escape.

(2) Tumor markers

Some fucosylated glycoproteins can serve as tumor-associated markers. In studies of liver cancer, pancreatic cancer and gastrointestinal tumors, changes in specific fucosylated glycoprotein levels are often used for diagnosis, prognostic evaluation or therapeutic response monitoring.

(3) Therapeutic response

Fucosylation can affect receptor signaling, antibody drug efficacy and the tumor immune microenvironment. Regulation of core or terminal fucosylation helps explore antibody drug optimization, targeted therapy sensitization and immunotherapy response mechanisms.

 

5.2 Inflammation and Infection

(1) Chronic inflammation

Inflammatory states can induce changes in glycosyltransferase expression, remodeling cell-surface fucosylation levels. These changes may further affect leukocyte adhesion, tissue infiltration and inflammatory amplification.

(2) Infection susceptibility

Pathogens often use host glycans as binding sites. Differences in fucosylation patterns can affect interactions between bacteria, viruses or parasites and host epithelial cells.

(3) Mucosal barrier injury

Fucosylated glycans in the intestinal and respiratory mucosa can affect microbial ecology, mucus layer stability and local immune responses. FUT2-related glycan changes are often associated with intestinal barrier function and infection susceptibility research.

 

5.3 Genetic and Metabolic Abnormalities

(1) Congenital disorders of glycosylation

Abnormalities in fucose donor synthesis, donor transport or transferase function may cause glycosylation defects, affecting multi-organ development, immune function and neurological manifestations.

(2) Influence of metabolic status

Cellular metabolic status can affect sugar nucleotide donor levels and thereby alter fucosylation capacity. Glucose metabolism, energy metabolism and inflammatory metabolic reprogramming may all indirectly affect glycan modification.

(3) Tissue fibrosis

Receptor glycan modifications can affect fibrosis-related signaling such as TGF-β. Increased core fucosylation may enhance some profibrotic pathway activities and participate in tissue remodeling and fibrosis progression.

 

6 Research Methods for Fucosylation

6.1 Glycan Structure Detection

(1) Lectin detection

Lectins such as AAL, AOL, UEA-I, LCA and PSA can recognize different fucosylated structures and are commonly used in Western blot, ELISA, flow cytometry, immunofluorescence or tissue section detection. Lectin detection is relatively simple and suitable for preliminary screening of fucosylation levels, but its structural resolution is limited.

(2) Enzymatic digestion validation

α-fucosidases can remove fucose residues with specific linkage types and are used to verify whether lectin signals depend on fucose structures. α1,2, α1,3/4 and α1,6 fucosidases can be used for terminal or core fucose structure validation.

(3) Mass spectrometry analysis

Glycomics and glycoproteomics mass spectrometry can analyze fucosylated glycan composition, linkage types and modification sites. This method is suitable for in-depth analysis of glycan changes in disease samples, cell models and secreted proteins.

 

6.2 Functional Validation Strategies

(1) FUT gene intervention

siRNA, knockout or overexpression of FUT family genes can be used to determine the effects of specific fucosyltransferases on cellular phenotypes. FUT8 is commonly used for core fucosylation functional studies, while FUT3/4/6/7 are often used for terminal fucosylation and selectin ligand research.

(2) Donor metabolism intervention

Supplementation with L-fucose, L-fucose-1-phosphate or GDP-L-fucose, or regulation of donor synthesis and transport-related factors such as FKP and SLC35C1, can be used to analyze the effect of donor levels on fucosylation modification.

(3) Receptor and signaling detection

If receptor function is studied, glycan changes, receptor expression, ligand binding, downstream phosphorylation signaling and cellular phenotype should be detected simultaneously. Observing changes in fucosylation levels alone is not sufficient to prove functional causality.

 

6.3 Evaluation Indicators

 

Research Direction	Key Detection Content	Recommended Evaluation Indicators	Key Points in Result Interpretation
Core fucosylation	N-glycan core α1,6 fucose	FUT8 expression, LCA/PSA binding, glycopeptide mass spectrometry	Focus on receptor signaling, IgG Fc function and cell migration
Terminal fucosylation	α1,2/α1,3/α1,4 fucose structures	UEA-I/AAL binding, Lewis antigen and sLeX expression	Focus on adhesion, inflammatory recruitment and tumor metastasis
O-fucosylation	Protein O-fucose modification	POFUT1/POFUT2 expression, Notch signaling output	Focus on developmental signaling and cell fate determination
Donor metabolism	GDP-L-fucose synthesis and transport	FKP, SLC35C1 and response to L-fucose supplementation	Determine whether fucosylation changes are caused by donor limitation
Glycan recognition	Lectins or glycan-binding receptors	AAL, AOL, UEA-I, LCA and CLEC/MBL-related detection	Distinguish glycan structural changes from glycan recognition responses
Disease function	Tumor, inflammation, infection or fibrosis phenotypes	Migration and invasion, adhesion, inflammatory factors and receptor signaling	Establish the causal chain between glycan modification and pathological phenotype

 

7 Reagent and Detection Tool Selection for Fucosylation Modification

7.1 Reagents, Enzymes and Detection Tools for Fucosylation Research

 

Product Module	Cat. No.	Product Name	Grade/Purity	System Role	Recommended Application Scenario
Fucose donor/metabolic substrate	F110930	L-(-)-Fucose	Moligand™, ≥98%	Exogenous fucose supplementation to support salvage synthesis pathway research	Studying the effects of exogenous fucose on cellular fucosylation levels, mucosal glycans and receptor glycosylation
Fucose donor/metabolic substrate	L422823	L-(-)-Fucose	Moligand™, 10mM in DMSO	Exogenous fucose supplementation	Suitable for dose treatment and metabolic supplementation studies in cell experiments
Fucose metabolic intermediate	L354522	L-Fucose-1-phosphate disodium salt	≥95%	Intermediate in the GDP-fucose salvage synthesis pathway	Suitable for fucose metabolism, donor synthesis and sugar nucleotide precursor research
Fucose metabolic derivative	L350656	L-Fucitol	≥98%	Material for fucose-related metabolism research	Suitable for glycometabolism controls and fucose derivative research
Sugar nucleotide donor	G407394	GDP-L-fucose disodium salt	≥96%	Direct donor for fucosyltransferase reactions	Suitable for in vitro FUT enzyme reactions, glycan synthesis and fucosylation donor supplementation experiments
Sugar nucleotide donor	G409416	GDP-L-fucose disodium salt	≥95%	Donor for fucosyltransferase reactions	Suitable for glycosyltransferase activity analysis and in vitro glycan modification reactions
Salvage synthesis enzyme	L1520615	L-fucokinase/GDP-fucose pyrophos-phorylase (FKP)	Bioactive,Recombinant,ActiBioPure™,High Performance,EnzymoPure™,≥95%(SDS-PAGE),Protein concentration: See COA; ≥5 U/mg protein	Catalyzes conversion of L-fucose to GDP-L-fucose	Suitable for GDP-fucose preparation, salvage synthesis pathway and sugar nucleotide donor research
Fucosyltransferase	A1446095	alpha-1,2-Fucosyltransferase (α1,2FucT)		Catalyzes α1,2 fucosylation	Suitable for H antigen, FUT1/FUT2-related glycans and mucosal fucosylation research
Fucosyltransferase	F1431907	Fucosyltransferase 6		Participates in terminal fucosylation and formation of Lewis-related structures	Suitable for Lewis antigen, selectin ligand and inflammation-related adhesion research
Fucosyltransferase	F1446101	Fucosyltransferase 8		Key enzyme for core α1,6 fucosylation	Suitable for FUT8-mediated core fucosylation, receptor signaling and antibody Fc glycosylation research
Fucosyltransferase	F1455524	Fucosyltransferase 9		Participates in specific glycan fucosylation modification	Suitable for neural development, cell recognition and FUT family functional comparison
O-fucosyltransferase	P1428983	Protein O-Fucosyltransferase 1		Catalyzes protein O-fucosylation	Suitable for Notch-related O-fucosylation, developmental signaling and cell fate regulation
Recombinant FUT protein	rp330157	Recombinant Human FUT3 Protein	≥90%(SDS-PAGE)	Catalyzes FUT3-related terminal fucosylation	Suitable for Lewis antigen, tumor glycans and cell adhesion mechanism research
FUT inhibitor	F1446105	FUT8-IN-1		Inhibits FUT8-related core fucosylation	Suitable for functional blockade of core fucosylation, receptor signaling and tumor cell phenotype research
Fucosidase	F477365	α-1,2-Fucosidase solution	buffered aqueous solution	Hydrolyzes α1,2-linked fucose residues	Suitable for validating α1,2 fucosylated structures, UEA-I signal specificity and glycan digestion controls
Fucosidase	F755029	α-1→(2,3,4)-Fucosidase solution from Xanthomonas sp.	buffered aqueous solution	Hydrolyzes α1,2/1,3/1,4-linked terminal fucose	Suitable for terminal fucosylation structure validation and confirmation of lectin detection signals
Fucosidase	F755030	α1-3,4-Fucosidase, Xanthomonas sp.	Native α1-3,4-fucosidase from Xanthomonas species. Catalyzes the hydrolysis of α1,3- and α1,4-linked branched, non-reducing terminal fucose from complex carbohydrates. Note: 1 mU = 1 milliunit.	Removes α1,3- and α1,4-linked non-reducing terminal fucose	Suitable for Lewis antigen, selectin ligand and terminal fucosylation structure validation
Fucosidase	F755038	Recombinant α-1,6-Fucosidase (LpAlfC)	Bioactive,ActiBioPure™,High Performance,EnzymoPure™,His Tag,≥90%(SDS-PAGE),≥500 U/mg protein	Hydrolyzes core α1,6 fucose	Suitable for FUT8 core fucosylation validation and N-glycan core modification analysis
Fucosidase	rp223165	Recombinant α1-3,4 Fucosidase (BbAfcB)	Bioactive,Recombinant,ActiBioPure™,High Performance,EnzymoPure™,His Tag,≥90%(SDS-PAGE),≥2U/mg protein; protein concentration: 5-10mg/ml	Hydrolyzes α1,3/1,4-linked fucose	Suitable for Lewis-related glycans, tumor glycans and inflammation-related adhesion structure validation
Glycan release enzyme	P755140	PNGase F from Elizabethkingia meningoseptica	Recombinant, ready-to-use solution, expressed in <I>E. coli</I>	Releases N-glycans	Suitable for N-glycan core fucosylation analysis and glycoproteomics sample preparation
Glycan release enzyme	P755104	PNGase Fast	Recombinant, expressed in <I>E. coli</I>	Rapidly releases N-glycans	Suitable for glycoprotein deglycosylation, N-glycan detection and mass spectrometry sample processing
Glycan release enzyme	R488845	Recombinant PNGase F	Specific Activity ＞25 U/mg;Activity 5 U/ml	Releases N-glycans	Suitable for glycoprotein N-glycan analysis and core fucosylation site research
Endoglycosidase	E755036	Endoglycosidase F1, Elizabethkingia meningosepticum, Recombinant, E. coli	Endoglycosidase F1, <i>Elizabethkingia meningosepticum</i>, Recombinant, <i>E. coli</i> cleaves asparagine-linked or free oligomannose and hybrid. Suitable for deglycosylation of native proteins.	Cleaves oligomannose-type and hybrid-type N-glycans	Suitable for N-glycan structural typing and deglycosylation validation
O-glycan release enzyme	O489836	O-Glycosidase	Specific Activity ≥ 12 U/mg;Activity ≥ 1.25 U/ml	Releases certain O-glycans	Suitable for O-glycan fucosylation and mucin-related glycan research
Fucose-specific lectin	A419041	Aleuria aurantia lectin (AAL)		Recognizes multiple fucosylated glycans	Suitable for total fucosylation detection, lectin blotting, flow cytometry and tissue staining
Fucose-specific lectin	A1452065	Aleuria Aurantia Lectin (Fluorescein)		AAL-type lectin recognizing fucosylated structures	Suitable for flow cytometric detection of cell-surface fucosylation and immunofluorescence localization
Fucose-specific lectin	A1452258	Aleuria Aurantia Lectin (Agarose)		Affinity enrichment of fucosylated glycoproteins	Suitable for AAL affinity enrichment, glycoproteomics and mass spectrometry sample preparation
Fucose-specific lectin	A1451322	Aleuria Aurantia Lectin (Biotinylated)		Biotinylated fucose-recognition probe	Suitable for lectin ELISA, Western blot and streptavidin-based detection systems
Fucose-specific lectin	L405821	Lectin, Fucose specific (= AOL) from Aspergillus oryzae (5mg/mL, PBS pH6.5)		Recognizes fucosylated glycans	Suitable for fucosylated glycoprotein detection, cell-surface glycan analysis and glycomics validation
α1,2 fucose-recognizing lectin	U1452859	Ulex Europaeus Agglutinin I		Recognizes α1,2 fucosylated structures	Suitable for FUT1/FUT2-related H antigen, mucosal epithelial glycans and blood group-related glycan detection
α1,2 fucose-recognizing lectin	U1452257	Ulex Europaeus Agglutinin I (Fluorescein)		Fluorescent detection of α1,2 fucosylated structures	Suitable for flow cytometry, immunofluorescence and tissue localization analysis
α1,2 fucose-recognizing lectin	U1451227	Ulex Europaeus Agglutinin I (Biotinylated)		Biotinylated UEA-I probe	Suitable for lectin blotting, lectin ELISA and tissue section detection
α1,2 fucose-recognizing lectin	U1453574	Ulex Europaeus Agglutinin I (Agarose)		Enrichment of α1,2 fucosylated glycoproteins	Suitable for FUT1/FUT2-related glycoprotein separation and downstream mass spectrometry analysis
α1,2 fucose-recognizing lectin	L755063	Lectin from Ulex europaeus (gorse, furze)	lyophilized powder	Recognizes α1,2 fucosylated structures	Suitable for basic lectin staining and cell-surface glycan analysis
α1,2 fucose-recognizing lectin	L755071	Lectin from Ulex europaeus (gorse, furze)	peroxidase conjugate, lyophilized powder	HRP-labeled α1,2 fucose-recognition probe	Suitable for lectin blotting and chromogenic detection
α1,2 fucose-recognizing lectin	L755025	Lectin from Ulex europaeus (gorse, furze)	biotin conjugate, lyophilized powder	Biotinylated α1,2 fucose-recognition probe	Suitable for tissue staining, ELISA and glycoprotein detection
α1,2 fucose-recognizing lectin	L755096	Lectin from Ulex europaeus (gorse, furze)	FITC conjugate, lyophilized powder	Fluorescent detection of α1,2 fucosylation	Suitable for flow cytometry and immunofluorescence
Core fucose-related lectin	L140096	Lens culinaris lectin (LCA/LcH)		Preferentially recognizes core fucosylated N-glycan-related structures	Suitable for FUT8-related core fucosylation, IgG Fc glycans and receptor N-glycan detection
Core fucose-related lectin	L1453519	Lens Culinaris Agglutinin (Fluorescein)		LCA-type probe	Suitable for cell-surface N-glycan and core fucosylation-related detection
Core fucose-related lectin	L1454625	Lens Culinaris Agglutinin (Biotinylated)		Biotinylated LCA-type probe	Suitable for lectin blotting, ELISA and tissue section detection
Core fucose-related lectin	L755046	Lectin from Lens culinaris (lentil)	Isoelectric focusing marker, pI (1) 8.2, (2) 8.6, (3) 8.8	Recognizes complex N-glycan-related structures	Suitable for N-glycan structure detection and lectin experiment controls
Core fucose-related lectin	L755037	Lectin from Lens culinaris (lentil)	Sepharose™ conjugate, saline suspension	Enriches LCA-binding glycoproteins	Suitable for enrichment of core fucosylation-related glycoproteins
Core fucose-related lectin	P140103	Pisum sativum lectin (PSA)		Recognizes core fucosylation-related N-glycan structures	Suitable for complementary analysis of core-fucosylated glycoproteins with LCA
Core fucose-related lectin	P1451232	Pisum Sativum Agglutinin (Biotinylated)		Biotinylated PSA probe	Suitable for lectin ELISA, Western blot and tissue detection
Vascular/fucose-related lectin	L1442702	Lotus tetragonolobus lectin		Recognizes fucose-related glycan structures	Suitable for vascular endothelial, epithelial glycan and cell-surface fucosylation research
Vascular/fucose-related lectin	L1452577	Lotus Tetragonolobus Lectin (Fluorescein)		Fluorescent detection of fucose-related glycans	Suitable for immunofluorescence, flow cytometry and tissue localization
FUT gene intervention	F1490166	FUT1 Human Pre-designed siRNA Set A		Downregulates FUT1	Suitable for functional validation of α1,2 fucosylation, H antigen and epithelial surface glycans
FUT gene intervention	F1478442	FUT2 Human Pre-designed siRNA Set A		Downregulates FUT2	Suitable for research on secretory fucosylation, intestinal mucosa and microbial adhesion
FUT gene intervention	F1473007	FUT3 Human Pre-designed siRNA Set A		Downregulates FUT3	Suitable for Lewis antigen formation, tumor glycans and cell adhesion research
FUT gene intervention	F1489655	FUT4 Human Pre-designed siRNA Set A		Downregulates FUT4	Suitable for terminal fucosylation, selectin ligands and inflammatory cell adhesion research
FUT gene intervention	F1460681	FUT6 Human Pre-designed siRNA Set A		Downregulates FUT6	Suitable for Lewis-related glycans, tumor metastasis and inflammation-related adhesion mechanisms
FUT gene intervention	F1475634	FUT7 Human Pre-designed siRNA Set A		Downregulates FUT7	Suitable for sLeX/selectin ligands, leukocyte recruitment and immune cell migration research
FUT gene intervention	F1487079	FUT8 Human Pre-designed siRNA Set A		Downregulates FUT8	Suitable for core fucosylation, receptor signaling and antibody Fc fucosylation research
FUT gene intervention	F1471443	FUT9 Human Pre-designed siRNA Set A		Downregulates FUT9	Suitable for neural development, cell recognition and FUT family functional comparison
POFUT gene intervention	P1467088	POFUT1 Human Pre-designed siRNA Set A		Downregulates POFUT1	Suitable for Notch O-fucosylation, developmental signaling and cell fate research
POFUT gene intervention	P1470035	POFUT2 Human Pre-designed siRNA Set A		Downregulates POFUT2	Suitable for O-fucosylation of TSR domain proteins and extracellular matrix-related research
GDP-fucose transport intervention	S1469821	SLC35C1 Human Pre-designed siRNA Set A		Downregulates GDP-fucose transporter	Suitable for Golgi donor transport, global fucosylation deficiency and glycosylation abnormality models
POFUT detection antibody	Ab122526	Pofut1 Antibody	Carrier Free, ExactAb™, Azide Free, Validated, High Performance, See COA	Detects POFUT1	Suitable for protein expression detection related to Notch O-fucosylation
FUT detection ELISA	EJ1514066	Human Galactoside 2-alpha-L-fucosyltransferase 2 (FUT2) ELISA Kit	BioReagent	Quantitatively detects FUT2	Suitable for mucosal fucosylation, secretory glycans and intestinal barrier research
FUT detection ELISA	EJ1512763	Mouse Alpha- (1,6) -fucosyltransferase (FUT8) ELISA Kit	BioReagent	Quantitatively detects FUT8	Suitable for core fucosylation, receptor signaling and disease tissue analysis in mouse models
C-type lectin detection	EJ1513484	Human C-Type Lectin Domain Family 4 Member A (DCIR) ELISA Kit	BioReagent	Detects DCIR	Can be used for glycan-recognition receptors, immune cell glycan recognition and inflammation model research
C-type lectin detection	EJ1513485	Human c-type Lectin Domain Family 4 Member G(CLEC4G) ELISA Kit	BioReagent	Detects CLEC4G	Suitable for liver sinusoidal endothelium, glycan recognition and immune clearance-related research
Mannose-binding lectin detection	EJ1514289	Human Mannose Binding Lectin (MBP/MBL) ELISA Kit	BioReagent	Detects MBL	Suitable for innate immunity, glycan recognition and complement pathway research
Mannose-binding lectin detection	EJ1512120	Rat Mannose Binding Lectin (MBP/MBL) ELISA Kit	BioReagent	Detects rat MBL	Suitable for glycan recognition and immune response analysis in animal models
Galectin detection	EJ1513891	Human Galectin 3 (Galectin-3) ELISA Kit	BioReagent	Detects Galectin-3	Can be used for auxiliary evaluation of glycan recognition, inflammation, tumor microenvironment and fibrosis models
Galectin detection	EJ1513895	Human Galectin 9 (GAL-9) ELISA Kit	BioReagent	Detects Galectin-9	Suitable for immune regulation, T cell function and tumor immune microenvironment research

 

The research value of fucosylation lies not only in identifying glycan structural changes, but also in clarifying how specific glycan modifications are translated into detectable cellular functions and pathological phenotypes.

 

For more related articles, please see below:

[1] Glycosylation in Biopharmaceuticals