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AB176794

Anti-FUT9 antibody

1

(1 Review)

|

(2 Publications)

Rabbit Polyclonal FUT9 antibody. Suitable for WB, IHC-P and reacts with Human samples. Cited in 2 publications. Immunogen corresponding to Recombinant Fragment Protein within Human FUT9 aa 150 to C-terminus.

View Alternative Names

4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase 9, Fucosyltransferase 9, Fucosyltransferase IX, Galactoside 3-L-fucosyltransferase, Fuc-TIX, FucT-IX, FUT9

2 Images
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-FUT9 antibody (AB176794)
  • IHC-P

Supplier Data

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-FUT9 antibody (AB176794)

Immunohistochemical staining of formalin fixed, paraffin embedded Human fetal stomach tissue labeling FUT9 with ab176794 at 1/100 dilution.

Western blot - Anti-FUT9 antibody (AB176794)
  • WB

Supplier Data

Western blot - Anti-FUT9 antibody (AB176794)

All lanes:

Western blot - Anti-FUT9 antibody (ab176794) at 1/500 dilution

All lanes:

K562 cell lysate

Predicted band size: 100 kDa,118 kDa,120 kDa,153 kDa,17 kDa,29 kDa,42 kDa,43 kDa,48 kDa,52 kDa,54 kDa,57 kDa,70 kDa

Observed band size: 53 kDa,54 kDa

false

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

IHC-P, WB

applications

Immunogen

Recombinant Fragment Protein within Human FUT9 aa 150 to C-terminus. The exact immunogen used to generate this antibody is proprietary information.

Q9Y231

Reactivity data

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Properties and storage information

Form
Lyophilized
Reconstitution
reconstitute with water at 200µL
Purification technique
Affinity purification Protein A
Storage buffer
pH: 7.2 Preservative: 0.02% Sodium azide Constituents: PBS, 1% BSA
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.

The fucosyltransferase 9 (FUT9) is an enzyme that transfers fucose a hexose deoxy sugar to N-acetylglucosamine which is part of the process of glycosylation. Also known as FT9 this enzyme weighs approximately 44 kDa. It is expressed in many tissues but has higher levels in the brain. FUT9 functions to add fucose residues in the synthesis of Lewis X (LeX) antigens which are important for cell-cell interactions.
Biological function summary

The enzyme contributes to the synthesis of glycoproteins and glycolipids impacting cellular adhesion and immune response. FUT9 does not typically join with protein complexes but it plays a significant role in forming the structures essential for developmental processes. The glycan structures generated by FUT9 involve in developmental decisions and the maturation of specific cellular functions particularly in the nervous system.

Pathways

FUT9 participates actively in the N-glycan biosynthesis pathway and specifically influences the creation of the Lewis X antigen. This antigen plays a role in pathways related to leukocyte migration and neural development. In these pathways FUT9 interacts indirectly with adhesion molecules and lectins which recognize and bind to specific sugar structures like LeX affecting downstream signaling and cell movement.

FUT9 relates to certain types of cancer and neurological diseases. Altered fucosylation patterns mediated by FUT9 associate with tumor metastasis and cancer progression. In the context of neurological disorders irregular FUT9 activity correlates with conditions like Alzheimer's where cell adhesion molecules affected by FUT9-mediated fucosylation undergo alterations. This enzyme's interaction with adhesion proteins can influence disease state and severity in these cases.

Product protocols

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

Target data

Catalyzes alpha(1->3) linkage of fucosyl moiety transferred from GDP-beta-L-fucose to N-acetyl glucosamine (GlcNAc) within type 2 lactosamine (LacNAc, beta-D-Gal-(1->4)-beta-D-GlcNAc-) glycan attached to glycolipids and N- or O-linked glycoproteins. Fucosylates distal type 2 LacNAc and its fucosylated (H-type 2 LacNAc) and sialylated (sialyl-type 2 LacNAc) derivatives to form Lewis x (Lex) (CD15) and Lewis y (Ley) antigenic epitopes involved in cell adhesion and differentiation (PubMed : 10386598, PubMed : 10622713, PubMed : 11278338, PubMed : 12107078, PubMed : 16282604, PubMed : 17335083, PubMed : 18395013, PubMed : 23192350, PubMed : 23263199, PubMed : 29593094, PubMed : 37202521). Generates Lex epitopes in the brain, presumably playing a role in the maintenance of neuronal stemness and neurite outgrowth in progenitor neural cells (By similarity) (PubMed : 17335083, PubMed : 23000574). Fucosylates the internal type 2 LacNAc unit of the polylactosamine chain to form VIM-2 antigen that serves as recognition epitope for SELE (PubMed : 23192350). Can also modify milk oligosaccharides, in particular type 2 tetrasaccharide LNnT (PubMed : 37202521).
See full target information FUT9

Publications (2)

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

Acta biochimica et biophysica Sinica 55:1571-1581 PubMed37674364

2023

Fucosyltransferase 9 promotes neuronal differentiation and functional recovery after spinal cord injury by suppressing the activation of Notch signaling.

Applications

Unspecified application

Species

Unspecified reactive species

Jiewen Chen,Xiaolin Zeng,Wenwu Zhang,Gang Li,Haoming Zhong,Chengzhong Xu,Xiang Li,Tao Lin

American journal of human genetics 100:216-227 PubMed28065471

2017

Mutations in ATP6V1E1 or ATP6V1A Cause Autosomal-Recessive Cutis Laxa.

Applications

Unspecified application

Species

Unspecified reactive species

Tim Van Damme,Thatjana Gardeitchik,Miski Mohamed,Sergio Guerrero-Castillo,Peter Freisinger,Brecht Guillemyn,Ariana Kariminejad,Daisy Dalloyaux,Sanne van Kraaij,Dirk J Lefeber,Delfien Syx,Wouter Steyaert,Riet De Rycke,Alexander Hoischen,Erik-Jan Kamsteeg,Sunnie Y Wong,Monique van Scherpenzeel,Payman Jamali,Ulrich Brandt,Leo Nijtmans,G Christoph Korenke,Brian H Y Chung,Christopher C Y Mak,Ingrid Hausser,Uwe Kornak,Björn Fischer-Zirnsak,Tim M Strom,Thomas Meitinger,Yasemin Alanay,Gulen E Utine,Peter K C Leung,Siavash Ghaderi-Sohi,Paul Coucke,Sofie Symoens,Anne De Paepe,Christian Thiel,Tobias B Haack,Fransiska Malfait,Eva Morava,Bert Callewaert,Ron A Wevers
View all publications

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