Mouse Anti-FUT9 Recombinant Antibody (CF177) (CBMAB-FT311LY)

Name: Mouse Anti-FUT9 Recombinant Antibody (CF177)
SKU: CBMAB-FT311LY
Rating: 5 (1 reviews)

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Datasheet

SDS

Request for COA

Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Host Animal

Mouse

Clone

CF177

Application

ELISA, WB, IHC

Immunogen

fucosyltransferase 9 (alpha (1, 3) fucosyltransferase)

Specificity

Human

Antibody Isotype

IgG1

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!]

Format

Liquid

Buffer

50% glycerol

Preservative

0.02% sodium azide

Storage

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

More Infomation

Target

Full Name

Fucosyltransferase 9

Introduction

The protein encoded by this gene belongs to the glycosyltransferase family. It is localized to the golgi, and catalyzes the last step in the biosynthesis of Lewis X (LeX) antigen, the addition of a fucose to precursor polysaccharides. This protein is one of the few fucosyltransferases that synthesizes the LeX oligosaccharide (CD15) expressed in the organ buds progressing in mesenchyma during embryogenesis. It is also responsible for the expression of CD15 in mature granulocytes. A common haplotype of this gene has also been associated with susceptibility to placental malaria infection. [provided by RefSeq, Nov 2011]

Entrez Gene ID

10690

UniProt ID

Q9Y231

Function

Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the N-acetyl glucosamine (GlcNAc) of a distal lactosamine unit of a glycoprotein or a glycolipid-linked polylactosamine chains through an alpha-1,3 glycosidic linkage and participates in particular to the Lewis x (Lex)/CD15 epitope biosynthesis in neurons which allows cell differentiation, cell adhesion, and initiation of neurite outgrowth (PubMed:23263199, PubMed:23192350, PubMed:10386598, PubMed:17335083, PubMed:23000574, PubMed:11278338, PubMed:10622713, PubMed:18395013, PubMed:12107078, PubMed:16282604).

Also fucosylates di-, tri- and tetraantennary N-glycans linked to glycoproteins and the inner lactosamine unit of the alpha2,3-sialylated polylactosamine resulting in sLex (CD15s) epitope synthesis (PubMed:11278338, PubMed:12107078, PubMed:18395013).

Furthermore, it is capable of synthesizing Lewis a (Lea), although to a lesser extent than Lex and Lewis y (Ley) and to confer SELE-dependent, but not SELL- and SELP-selectin-dependent, cell rolling and adhesion by enhancing Lex and sLex synthesis (PubMed:18395013, PubMed:23192350).

Biological Process

Carbohydrate metabolic process Source: ProtInc
Cellular polysaccharide biosynthetic process Source: UniProtKB
Fucosylation Source: UniProtKB
L-fucose catabolic process Source: UniProtKB
Neuron differentiation Source: UniProtKB
Oligosaccharide biosynthetic process Source: Reactome
Positive regulation of neuron projection development Source: UniProtKB
Protein glycosylation Source: UniProtKB
Regulation of leukocyte cell-cell adhesion Source: UniProtKB
Regulation of leukocyte tethering or rolling Source: UniProtKB

Cellular Location

Trans-Golgi network membrane; Golgi apparatus membrane

Topology

Cytoplasmic: 1-11
Helical: 12-32
Lumenal: 33-359

PTM

N-glycosylated with complex-type N-glycans.

Chaubey, S., Nader, Y. M., Shah, D., Kumova, O. K., Prahaladan, V., Carey, A. J., ... & Bhandari, V. (2021). α1, 3-Fucosyltransferase-IX, an enzyme of pulmonary endogenous lung stem cell marker SSEA-1, alleviates experimental bronchopulmonary dysplasia. Pediatric Research, 89(5), 1126-1135.

Fan, R., Han, X., Gong, Y., He, L., Xue, Z., Yang, Y., ... & Zhang, J. (2021). Alterations of fucosyltransferase genes and fucosylated glycans in gastric epithelial cells infected with Helicobacter pylori. Pathogens, 10(2), 168.

Blanas, A., Cornelissen, L. A., Kotsias, M., van der Horst, J. C., van de Vrugt, H. J., Kalay, H., ... & van Vliet, S. J. (2019). Transcriptional activation of fucosyltransferase (FUT) genes using the CRISPR-dCas9-VPR technology reveals potent N-glycome alterations in colorectal cancer cells. Glycobiology, 29(2), 137-150.

Shan, M., Yang, D., Dou, H., & Zhang, L. (2019). Fucosylation in cancer biology and its clinical applications. Progress in molecular biology and translational science, 162, 93-119.

Cho, E. H., Soliman, M., Alfajaro, M. M., Kim, J. Y., Seo, J. Y., Park, J. G., ... & Cho, K. O. (2018). Bovine nebovirus interacts with a wide spectrum of histo-blood group antigens. Journal of Virology, 92(9), e02160-17.

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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme Linked Immunospot (ELISpot)
Proteogenomic
Other Protocols

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Isotype control

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

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