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Mouse Anti-FUT8 Recombinant Antibody (CBXF-2541) (CBMAB-F1152-CQ)


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Summary

Host Animal
Mouse
Specificity
Human
Clone
CBXF-2541
Antibody Isotype
IgG2a
Application
siRNA, ELISA, IHC, WB

Basic Information

Specificity
Human
Antibody Isotype
IgG2a
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Fucosyltransferase 8
Introduction
This gene encodes an enzyme belonging to the family of fucosyltransferases. The product of this gene catalyzes the transfer of fucose from GDP-fucose to N-linked type complex glycopeptides. This enzyme is distinct from other fucosyltransferases which catalyze alpha1-2, alpha1-3, and alpha1-4 fucose addition. The expression of this gene may contribute to the malignancy of cancer cells and to their invasive and metastatic capabilities. Alternative splicing results in multiple transcript variants.
Entrez Gene ID
2530
UniProt ID
Q9BYC5
Alternative Names
Fucosyltransferase 8; GDP-L-Fuc:N-Acetyl-Beta-D-Glucosaminide Alpha1,6-Fucosyltransferase; Fucosyltransferase 8 (Alpha (1,6) Fucosyltransferase); GDP-Fucose--Glycoprotein Fucosyltransferase; Glycoprotein 6-Alpha-L-Fucosyltransferase; Alpha1-6FucT; EC 2.4.1.68; Alpha (1,6) Fucosyltransferase; Alpha-(1,6)-Fucosyltransferase;
Function
Catalyzes the addition of fucose in alpha 1-6 linkage to the first GlcNAc residue, next to the peptide chains in N-glycans.
Biological Process
Cell migration Source: Ensembl
GDP-L-fucose metabolic process Source: UniProtKB
Integrin-mediated signaling pathway Source: Ensembl
In utero embryonic development Source: UniProtKB
L-fucose catabolic process Source: UniProtKB
N-glycan fucosylation Source: GO_Central
N-glycan processing Source: UniProtKB
Oligosaccharide biosynthetic process Source: ProtInc
Protein glycosylation in Golgi Source: InterPro
Protein N-linked glycosylation Source: GO_Central
Protein N-linked glycosylation via asparagine Source: UniProtKB
Receptor metabolic process Source: Ensembl
Regulation of cellular response to oxidative stress Source: Ensembl
Regulation of gene expression Source: Ensembl
Respiratory gaseous exchange by respiratory system Source: Ensembl
Transforming growth factor beta receptor signaling pathway Source: Ensembl
Viral protein processing Source: Reactome
Cellular Location
Golgi stack membrane. Membrane-bound form in trans cisternae of Golgi.
Involvement in disease
Congenital disorder of glycosylation with defective fucosylation 1 (CDGF1):
A form of congenital disorder of glycosylation, a genetically heterogeneous group of multisystem disorders caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions. CDGF1 is an autosomal recessive disorder, apparent from birth, characterized by poor growth, failure to thrive, hypotonia, skeletal anomalies, and delayed psychomotor development with intellectual disability.
Topology
Cytoplasmic: 1-9
Helical: 10-30
Lumenal: 31-575
PTM
Tyrosine phosphorylated by PKDCC/VLK.
More Infomation

Kyunai, Y. M., Sakamoto, M., Koreishi, M., Tsujino, Y., & Satoh, A. (2023). Fucosyltransferase 8 (FUT8) and core fucose expression in oxidative stress response. Plos one, 18(2), e0281516.

Cuvry, A., Gozalbo-Rovira, R., Strubbe, D., Neyts, J., de Witte, P., Rodríguez-Díaz, J., & Rocha-Pereira, J. (2022). The Role of Histo-Blood Group Antigens and Microbiota in Human Norovirus Replication in Zebrafish Larvae. Microbiology Spectrum, 10(6), e03157-22.

Liang, Y., Wang, T., Gao, R., Jia, X., Ji, T., Shi, P., ... & Han, P. (2022). Fucosyltransferase 8 is Overexpressed and Influences Clinical Outcomes in Lung Adenocarcinoma Patients. Pathology and Oncology Research, 9.

Bastian, K., Scott, E., Elliott, D. J., & Munkley, J. (2021). FUT8 alpha-(1, 6)-fucosyltransferase in cancer. International Journal of Molecular Sciences, 22(1), 455.

Ma, M., Guo, D., Tan, Z., Du, J., Guan, F., & Li, X. (2021). Fucosyltransferase 8 regulation and breast cancer suppression by transcription factor activator protein 2γ. Cancer Science, 112(8), 3190-3204.

Boruah, B. M., Kadirvelraj, R., Liu, L., Ramiah, A., Li, C., Zong, G., ... & Moremen, K. W. (2020). Characterizing human α-1, 6-fucosyltransferase (FUT8) substrate specificity and structural similarities with related fucosyltransferases. Journal of Biological Chemistry, 295(50), 17027-17045.

Tada, K., Ohta, M., Hidano, S., Watanabe, K., Hirashita, T., Oshima, Y., ... & Inomata, M. (2020). Fucosyltransferase 8 plays a crucial role in the invasion and metastasis of pancreatic ductal adenocarcinoma. Surgery Today, 50, 767-777.

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For research use only. Not intended for any clinical use.

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