Mouse Anti-MGAT3 (AA 430-531) Recombinant Antibody (CBFYM-2169) (CBMAB-M2351-FY)

Name: Mouse Anti-MGAT3 (AA 430-531) Recombinant Antibody (CBFYM-2169)
SKU: CBMAB-M2351-FY
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

CBFYM-2169

Application

ELISA, WB

Immunogen

Recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.Immunogen sequence: LVSAQNGDFP RWGDYEDKRD LNYIRGLIRT GGWFDGTQQE YPPADPSEHM YAPKYLLKNY DRFHYLLDNP YQEPRSTAAG GWRHRGPEGR PPARGKLDEA EV

Specificity

Human

Antibody Isotype

IgG1, k

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

Storage

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

Epitope

AA 430-531

More Infomation

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.

Entrez Gene ID

4248

UniProt ID

Q09327

Alternative Names

Mannosyl (Beta-1,4-)-Glycoprotein Beta-1,4-N-Acetylglucosaminyltransferase; N-Glycosyl-Oligosaccharide-Glycoprotein N-Acetylglucosaminyltransferase III; N-Acetylglucosaminyltransferase III; GlcNAc-T III; GNT-III; Beta-1,4-Mannosyl-Glycoprotein 4-Beta-N-Acetylglucosaminyltransferase; EC 2.4.1.144; GGNT3; GNT3

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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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)
Proteogenomics
Other Protocols

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

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