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Mouse Anti-MGAT5 Recombinant Antibody (3E9) (CBMAB-G6382-LY)

This product is antibody recognizes MGAT5. The antibody 3E9 immunoassay techniques such as: WB.
See all MGAT5 antibodies
Published Data
Fig. 1 Representative western blot images of assayed proteins in a comparison (Comp) and schizophrenia (Scz) subject.
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Summary

Host Animal
Mouse
Specificity
Human
Clone
3E9
Antibody Isotype
IgG
Application
WB

Basic Information

Specificity
Human
Antibody Isotype
IgG
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
Purity
> 95% Purity determined by SDS-PAGE.
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
mannosyl (alpha-1,6-)-glycoprotein beta-1,6-N-acetyl-glucosaminyltransferase
Introduction
The protein encoded by this gene belongs to the glycosyltransferase family. It catalyzes the addition of beta-1,6-N-acetylglucosamine to the alpha-linked mannose of biantennary N-linked oligosaccharides present on the newly synthesized glycoproteins. It is one of the most important enzymes involved in the regulation of the biosynthesis of glycoprotein oligosaccharides. Alterations of the oligosaccharides on cell surface glycoproteins cause significant changes in the adhesive or migratory behavior of a cell. Increase in the activity of this enzyme has been correlated with the progression of invasive malignancies. [provided by RefSeq, Oct 2011]
Entrez Gene ID
4249
UniProt ID
Q09328
Alternative Names
Mannosyl (Alpha-1;6-)-Glycoprotein Beta-1;6-N-Acetyl-Glucosaminyltransferase; Alpha-Mannoside Beta-1;6-N-Acetylglucosaminyltransferase; Mannoside Acetylglucosaminyltransferase 5; N-Acetylglucosaminyl-Transferase V; EC 2.4.1.155; GlcNAc-T V;
Function
Catalyzes the addition of N-acetylglucosamine (GlcNAc) in beta 1-6 linkage to the alpha-linked mannose of biantennary N-linked oligosaccharides (PubMed:10395745, PubMed:30140003).

Catalyzes an important step in the biosynthesis of branched, complex-type N-glycans, such as those found on EGFR, TGFR (TGF-beta receptor) and CDH2 (PubMed:10395745, PubMed:22614033, PubMed:30140003).

Via its role in the biosynthesis of complex N-glycans, plays an important role in the activation of cellular signaling pathways, reorganization of the actin cytoskeleton, cell-cell adhesion and cell migration. MGAT5-dependent EGFR N-glycosylation enhances the interaction between EGFR and LGALS3 and thereby prevents rapid EGFR endocytosis and prolongs EGFR signaling. Required for efficient interaction between TGFB1 and its receptor. Enhances activation of intracellular signaling pathways by several types of growth factors, including FGF2, PDGF, IGF, TGFB1 and EGF. MGAT5-dependent CDH2 N-glycosylation inhibits CDH2-mediated homotypic cell-cell adhesion and contributes to the regulation of downstream signaling pathways. Promotes cell migration. Contributes to the regulation of the inflammatory response. MGAT5-dependent TCR N-glycosylation enhances the interaction between TCR and LGALS3, limits agonist-induced TCR clustering, and thereby dampens TCR-mediated responses to antigens. Required for normal leukocyte evasation and accumulation at sites of inflammation (By similarity).

Inhibits attachment of monocytes to the vascular endothelium and subsequent monocyte diapedesis (PubMed:22614033).

Secreted alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A:
Promotes proliferation of umbilical vein endothelial cells and angiogenesis, at least in part by promoting the release of the growth factor FGF2 from the extracellular matrix.
Biological Process
Negative regulation of protein tyrosine phosphatase activity Source: ARUK-UCL
Positive regulation of cell migration Source: ARUK-UCL
Positive regulation of receptor signaling pathway via STAT Source: ARUK-UCL
Protein N-linked glycosylation Source: ARUK-UCL
Protein N-linked glycosylation via asparagine Source: UniProtKB
Viral protein processing Source: Reactome
Cellular Location
Golgi apparatus
Golgi apparatus membrane
Secreted alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A:
Secreted
Topology
Cytoplasmic: 1-13
Helical: 14-30
Lumenal: 31-741
PTM
N-glycosylated.
A secreted form is released from the membrane after cleavage by gamma-secretase.

Yale, A. R., Kim, E., Gutierrez, B., Hanamoto, J. N., Lav, N. S., Nourse, J. L., ... & Flanagan, L. A. (2023). Regulation of neural stem cell differentiation and brain development by MGAT5-mediated N-glycosylation. Stem Cell Reports.

de-Souza-Ferreira, M., Ferreira, É. E., & de-Freitas-Junior, J. C. M. (2023). Aberrant N-glycosylation in cancer: MGAT5 and β1, 6-GlcNAc branched N-glycans as critical regulators of tumor development and progression. Cellular Oncology, 1-21.

Li, X., Zhou, G., Tian, X., Chen, F., Li, G., & Ding, Y. (2021). The polymorphisms of FGFR2 and MGAT5 affect the susceptibility to COPD in the Chinese people. BMC Pulmonary Medicine, 21(1), 1-13.

Yang, Y., Wu, J., Liu, F., He, J., Wu, F., Chen, J., & Jiang, Z. (2021). IGF2BP1 promotes the liver cancer stem cell phenotype by regulating MGAT5 mRNA stability by m6A RNA methylation. Stem Cells and Development, 30(22), 1115-1125.

Marhuenda, E., Fabre, C., Zhang, C., Martin-Fernandez, M., Iskratsch, T., Saleh, A., ... & Bakalara, N. (2021). Glioma stem cells invasive phenotype at optimal stiffness is driven by MGAT5 dependent mechanosensing. Journal of experimental & clinical cancer research, 40(1), 1-14.

Pereira, M. S., Durães, C., Catarino, T. A., Costa, J. L., Cleynen, I., Novokmet, M., ... & Pinho, S. S. (2020). Genetic variants of the MGAT5 gene are functionally implicated in the modulation of T cells glycosylation and plasma IgG glycome composition in ulcerative colitis. Clinical and Translational Gastroenterology, 11(4).

Cai, J., Huang, J., Wang, W., Zeng, J., & Wang, P. (2020). miR-124-3p Regulates FGF2–EGFR Pathway to Overcome Pemetrexed Resistance in Lung Adenocarcinoma Cells by Targeting MGAT5. Cancer Management and Research, 11597-11609.

Yan, G., Li, Y., Zhan, L., Sun, S., Yuan, J., Wang, T., ... & Hu, W. (2019). Decreased miR-124-3p promoted breast cancer proliferation and metastasis by targeting MGAT5. American journal of cancer research, 9(3), 585.

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

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