FUT10 (Fucosyltransferase 10) is a glycosyltransferase enzyme involved in α1,3-fucosylation of glycoproteins and glycolipids. The FUT10 antibody is a polyclonal or monoclonal immunoglobulin designed to detect and study FUT10 expression in cells, tissues, or biological samples. It is critical for researching FUT10’s role in glycosylation, ER quality control, and its implications in diseases such as cancer.
Used to detect FUT10 protein levels in lysates. For example:
HeLa cells: FUT10 antibody (ab217197, Abcam) at 1:300 dilution detects a ~41–48 kDa band consistent with FUT10’s observed molecular weight .
IHC: FUT10 antibody (18660-1-AP, Proteintech) at 1:100 dilution in human testis sections highlights FUT10 localization in germ cells .
Critical for spatial analysis of FUT10 in tissues. Antigen retrieval with TE (pH 9.0) or citrate buffer (pH 6.0) is recommended .
Validated for subcellular localization studies and quantitative assays .
HeLa cells: Proteintech’s 18660-1-AP detects a prominent band at ~41–48 kDa, confirming specificity .
Testis tissue: Abcam’s ab217197 shows strong reactivity in germ cells, with no cross-reactivity reported .
Human testis: Proteintech’s 18660-1-AP (1:100) stains spermatogonia and spermatocytes, indicating FUT10’s role in germ cell development .
FUT10 and FUT11 function as protein O-fucosyltransferases in the ER, modifying EMI domain-containing proteins (e.g., MMRN1). This process regulates protein secretion and cellular stress responses .
In clear cell renal cell carcinoma (ccRCC):
Prognostic Biomarker: Low FUT10 expression correlates with poor survival and advanced clinical stages .
Immune Infiltration: Higher FUT10 levels associate with increased central memory T cells (Tcm) and reduced NK CD56bright cells, suggesting FUT10 modulates tumor immunity .
FUT10 promotes neural stem cell self-renewal by synthesizing Lewis X (LeX) structures on N-glycans, maintaining an undifferentiated state during brain development .
Therapeutic Targeting: FUT10’s role in immune evasion and cancer progression warrants exploration as a therapeutic target .
Mechanistic Studies: Limited understanding of FUT10’s substrate specificity and interactions (e.g., with EMI domains) requires further investigation .
Clinical Validation: Current findings rely on bioinformatics and in vitro models; in vivo studies are critical for translating insights to clinical applications .
KEGG: ath:AT2G15350
STRING: 3702.AT2G15350.1
Here’s a structured FAQ for FUT10 antibody research, incorporating methodological guidance and empirical data from peer-reviewed studies and technical specifications:
Mechanistic insights:
FUT10 catalyzes α(1,3)-fucosylation of N-glycans on IgG Fc regions, altering FcγRIIIa binding affinity .
Experimental design:
Data contradiction example:
| Condition | ADCC Activity (EC50) | Fucosylation Level | Source |
|---|---|---|---|
| Wild-type IgG | 12 nM | High | |
| FUT10−/− IgG | 48 nM | Undetectable |
Troubleshooting framework:
Antibody validation: Confirm cross-reactivity with species-specific isoforms (human vs. murine FUT10) .
Fixation artifacts: Compare fresh-frozen vs. formalin-fixed samples to assess epitope masking .
Subcellular fractionation: Isolate Golgi/ER membranes to distinguish biosynthetic vs. functional pools .
Advanced methodology:
Generate conditional FUT10 knockout mice (Nestin-Cre/FUT10flox) to study stem cell self-renewal defects .
Profile Lewis X-glycans via lectin microarray in embryonic vs. adult brain sections .
Critical controls:
| Parameter | Detail | Source |
|---|---|---|
| Host species | Rabbit | |
| Reactivity | Human, Mouse, Rat | |
| Immunogen | Synthetic peptide (aa 400–C-term) | |
| Glycan specificity | Core α(1,3)-fucose |
| Assay | Wild-type Result | FUT10−/− Result | Implication |
|---|---|---|---|
| ADCC (PR8 challenge) | 100% survival | 0% survival | FcγR binding critical |
| N-glycan fucosylation | 92% ± 4% | <5% | Core fucose essential |