FUT10 Antibody

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Description

Introduction to FUT10 Antibody

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.

Key FeaturesDetails
TargetFUT10 protein (61 kDa)
HostPrimarily rabbit polyclonal; some mouse monoclonal variants exist
ApplicationsWestern blot (WB), immunohistochemistry (IHC), immunofluorescence (IF), ELISA
Species ReactivityHuman, mouse, rat

Western Blot (WB)

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 .

Immunohistochemistry (IHC)

Critical for spatial analysis of FUT10 in tissues. Antigen retrieval with TE (pH 9.0) or citrate buffer (pH 6.0) is recommended .

Immunofluorescence (IF) and ELISA

Validated for subcellular localization studies and quantitative assays .

Western Blot Validation

  • 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 .

Immunohistochemistry Validation

  • Human testis: Proteintech’s 18660-1-AP (1:100) stains spermatogonia and spermatocytes, indicating FUT10’s role in germ cell development .

Role in ER Quality Control

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 .

Cancer and Immune Modulation

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 .

Stem Cell Regulation

FUT10 promotes neural stem cell self-renewal by synthesizing Lewis X (LeX) structures on N-glycans, maintaining an undifferentiated state during brain development .

Future Directions and Challenges

  • 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 .

Product Specs

Buffer
**Preservative:** 0.03% Proclin 300
**Constituents:** 50% Glycerol, 0.01M PBS, pH 7.4
Form
Liquid
Lead Time
Made-to-order (14-16 weeks)
Synonyms
FUT10 antibody; At2g15350 antibody; F26H6.13Putative fucosyltransferase 10 antibody; AtFUT10 antibody; EC 2.4.1.- antibody
Target Names
FUT10
Uniprot No.

Target Background

Function
FUT10 Antibody may be involved in cell wall biosynthesis. It may act as a fucosyltransferase.
Database Links
Protein Families
Glycosyltransferase 37 family
Subcellular Location
Golgi apparatus.
Tissue Specificity
Expressed in root, leaves, stems and seedlings.

Q&A

Here’s a structured FAQ for FUT10 antibody research, incorporating methodological guidance and empirical data from peer-reviewed studies and technical specifications:

Advanced Research Questions

Q3: How does FUT10-mediated core fucosylation impact antibody-dependent cellular cytotoxicity (ADCC)?

Mechanistic insights:

  • FUT10 catalyzes α(1,3)-fucosylation of N-glycans on IgG Fc regions, altering FcγRIIIa binding affinity .

  • Experimental design:

    • Compare ADCC activity of FUT10-knockout vs. wild-type IgG using NK cell activation assays .

    • Quantify fucose epitopes via LC-MS/MS glycomics .

Data contradiction example:

ConditionADCC Activity (EC50)Fucosylation LevelSource
Wild-type IgG12 nMHigh
FUT10−/− IgG48 nMUndetectable

Q4: What strategies resolve discrepancies in FUT10 localization across studies?

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 .

Q5: How to model FUT10’s role in neural development using in vivo systems?

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:

  • Include Fut9/Fut11 double knockouts to exclude redundant fucosyltransferase activity .

Technical Reference Tables

Table 1: FUT10 Antibody Specifications

ParameterDetailSource
Host speciesRabbit
ReactivityHuman, Mouse, Rat
ImmunogenSynthetic peptide (aa 400–C-term)
Glycan specificityCore α(1,3)-fucose

Table 2: Functional Impact of FUT10 Knockout

AssayWild-type ResultFUT10−/− ResultImplication
ADCC (PR8 challenge)100% survival0% survivalFcγR binding critical
N-glycan fucosylation92% ± 4%<5%Core fucose essential

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