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Mouse Anti-MGAT3 Recombinant Antibody (1C9) (CBMAB-A5448-LY)

The product is antibody recognizes MGAT3. The antibody 1C9 immunoassay techniques such as: WB, ELISA.
See all MGAT3 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
1C9
Antibody Isotype
IgG2a, κ
Application
WB, ELISA

Basic Information

Immunogen
MGAT3 (NP_002400, 430 a.a. ~ 531 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.
Specificity
Human
Antibody Isotype
IgG2a, κ
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 (beta-1,4-)-glycoprotein beta-1,4-N-acetylglucosaminyltransferase
Introduction
There are believed to be over 100 different glycosyltransferases involved in the synthesis of protein-bound and lipid-bound oligosaccharides. The enzyme encoded by this gene transfers a GlcNAc residue to the beta-linked mannose of the trimannosyl core of N-linked oligosaccharides and produces a bisecting GlcNAc. Multiple alternatively spliced variants, encoding the same protein, have been identified. [provided by RefSeq]
Entrez Gene ID
4248
UniProt ID
Q09327
Alternative Names
FLJ43371; GNT-III; GNT3; MGC141943; MGC142278
Function
It is involved in the regulation of the biosynthesis and biological function of glycoprotein oligosaccharides. Catalyzes the addition of N-acetylglucosamine in beta 1-4 linkage to the beta-linked mannose of the trimannosyl core of N-linked sugar chains, called bisecting N-acetylglucosamine (GlcNAc). It is one of the most important enzymes involved in the regulation of the biosynthesis of glycoprotein oligosaccharides. The addition of this bisecting GlcNAc residue alters not only the composition, but also the conformation of the N-glycan. The introduction of the bisecting GlcNAc residue results in the suppression of further processing and elongation of N-glycans, precluding the formation of beta-1,6 GlcNAc branching, catalyzed by MGAT5 since it is unable to use the bisected oligosaccharide as a substrate (PubMed:19403558).

Addition of bisecting N-acetylglucosamine to CDH1/E-cadherin modulates CDH1 cell membrane location (PubMed:19403558).

Inhibits NeuAc-alpha-2,3-Gal-beta-1,4-GlcNAc- formation which modulates sialylation levels and plays a role in cell migration regulation (PubMed:26801611).

In brain, addition of bisecting N-acetylglucosamine to BACE1 blocks its lysosomal targeting in response to oxidative stress and further degradation which increases its location to early endosome and the APP cleavage (By similarity).
Biological Process
Amyloid-beta metabolic process Source: UniProtKB
Cellular response to oxidative stress Source: UniProtKB
Cognition Source: UniProtKB
N-acetylglucosamine metabolic process Source: GO_Central
Negative regulation of lysosomal protein catabolic process Source: UniProtKB
Positive regulation of protein localization to early endosome Source: UniProtKB
Protein localization Source: UniProtKB
Protein N-linked glycosylation Source: UniProtKB
Regulation of cell migration Source: UniProtKB
Cellular Location
Golgi apparatus membrane
Topology
Cytoplasmic: 1-7
Helical: 8-23
Lumenal: 24-533

Nagarajah, S., Saleh, Q. W., Rasmussen, M., & Tepel, M. (2024). Long non-coding RNA MGAT3 in kidney transplant recipients with immunoglobulin A nephropathy. Journal of Nephrology, 1-3.

Zohora, F. T., Batu, T. T., & Mahal, L. K. (2023). Mapping miRNA regulation of MGAT3 reveals upregulation as the dominant mode of action. bioRxiv, 2023-08.

You, X., Wang, Y., Meng, J., Han, S., Liu, L., Sun, Y., ... & Zhang, Y. (2021). Exosomal miR‑663b exposed to TGF‑β1 promotes cervical cancer metastasis and epithelial‑mesenchymal transition by targeting MGAT3. Oncology reports, 45(4), 1-1.

Niu, H., Qu, A., & Guan, C. (2021). Suppression of MGAT3 expression and the epithelial–mesenchymal transition of lung cancer cells by miR-188-5p. biomedical journal, 44(6), 678-685.

Li, J., Xu, J., Li, L., Ianni, A., Kumari, P., Liu, S., ... & Yue, S. (2020). MGAT3-mediated glycosylation of tetraspanin CD82 at asparagine 157 suppresses ovarian cancer metastasis by inhibiting the integrin signaling pathway. Theranostics, 10(14), 6467.

Zhao, L., Liu, H., Luo, S., Moorman, P. G., Walsh, K. M., Li, W., & Wei, Q. (2020). Associations between genetic variants of KIF5B, FMN1, and MGAT3 in the cadherin pathway and pancreatic cancer risk. Cancer medicine, 9(24), 9620-9631.

Nagarajah, S., Rasmussen, M., Hoegh, S. V., & Tepel, M. (2020). Prospective Study of Long Noncoding RNA, MGAT3-AS1, and Viremia of BK Polyomavirus and Cytomegalovirus in Living Donor Renal Transplant Recipients. Kidney International Reports, 5(12), 2218-2227.

Nagarajah, S., Xia, S., Rasmussen, M., & Tepel, M. (2019). Endogenous intronic antisense long non-coding RNA, MGAT3-AS1, and kidney transplantation. Scientific Reports, 9(1), 14743.

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

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