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AB198741

Anti-FUT8 antibody

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(2 Publications)

Rabbit Polyclonal FUT8 antibody. Suitable for WB and reacts with Human samples. Cited in 2 publications. Immunogen corresponding to Synthetic Peptide within Human FUT8.

View Alternative Names

Alpha1-6FucT, Fucosyltransferase 8, GDP-fucose--glycoprotein fucosyltransferase, Glycoprotein 6-alpha-L-fucosyltransferase, FUT8

1 Images
Western blot - Anti-FUT8 antibody (AB198741)
  • WB

Supplier Data

Western blot - Anti-FUT8 antibody (AB198741)

All lanes:

Western blot - Anti-FUT8 antibody (ab198741) at 1/200 dilution

Lane 1:

LoVo cell lysates at 40 µg

Lane 2:

PC3 cell lysates at 40 µg

Predicted band size: 66 kDa

false

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

WB

applications

Immunogen

Synthetic Peptide within Human FUT8. The exact immunogen used to generate this antibody is proprietary information.

Q9BYC5

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7.4 Preservative: 0.05% Sodium azide Constituents: PBS, 50% Glycerol (glycerin, glycerine)
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

Supplementary information

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

FUT8 also known as alpha-(16)-fucosyltransferase represents an important enzyme responsible for transferring fucose from GDP-fucose to the innermost N-acetylglucosamine of N-glycans producing core fucosylation. The molecular mass of FUT8 is approximately 60 kDa. It expresses ubiquitously across various tissues with elevated levels seen in the liver lung and placenta. Researchers frequently study FUT8 due to its significance in glycosylation processes.
Biological function summary

FUT8 impacts numerous cellular activities by modulating glycan branching on glycoproteins. It functions independently and is not directly part of a larger protein complex. FUT8's activity influences cell-cell interactions signaling pathways and receptor functions. It plays an important part in maintaining cellular homeostasis and influences immune responses and cell growth as affected by glycosylation patterns on the cell surface and extracellular matrix.

Pathways

FUT8 is a critical component of the N-glycan biosynthesis pathway where it regulates the addition of fucose to glycans. This process affects protein folding and stability. The enzyme interacts with important glycoproteins like EGFR and integrins impacting signaling pathways such as the Wnt and TGF-beta pathways. Altered FUT8 activity can modify pathways and relationships with other proteins changing cellular responses.

FUT8 has connections to cancers and liver fibrosis due to its role in modifying glycans and subsequently influencing cellular communication and adhesion. Abnormal core fucosylation affects proteins like alpha-fetoprotein in liver cancer which might serve as a biomarker. Furthermore changes in FUT8 activity and expression could relate to epidermal growth factor receptor (EGFR) signaling disruptions promoting tumor proliferation. Scientists consider FUT8 a potential therapeutic target in these diseases.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Catalyzes the addition of fucose in alpha 1-6 linkage to the first GlcNAc residue, next to the peptide chains in N-glycans (PubMed : 17172260, PubMed : 29304374, PubMed : 36280670, PubMed : 9133635). Fucosylates the reducing GlcNAc residue in complex-type N-glycans attached on the fragment crystallizable (Fc) of IgGs. Fully converts Fc glycoforms containing one or two terminal GlcNAc moieties (G0-GlcNAc and G0) (PubMed : 36280670).
See full target information FUT8

Publications (2)

Recent publications for all applications. Explore the full list and refine your search

Nature communications 15:652 PubMed38253527

2024

EGFR core fucosylation, induced by hepatitis C virus, promotes TRIM40-mediated-RIG-I ubiquitination and suppresses interferon-I antiviral defenses.

Applications

Unspecified application

Species

Unspecified reactive species

Qiu Pan,Yan Xie,Ying Zhang,Xinqi Guo,Jing Wang,Min Liu,Xiao-Lian Zhang

PeerJ 11:e14850 PubMed36793891

2023

Abnormal expression of induces intravillous vascularization dysplasia in ectopic pregnancy.

Applications

Unspecified application

Species

Unspecified reactive species

Qian Zhu,Xiaoya Zhao,Duo Zhang,Wei Xia,Jian Zhang
View all publications

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