Rabbit Polyclonal MGAT3 antibody. Suitable for WB and reacts with Human samples. Immunogen corresponding to Recombinant Fragment Protein within Human MGAT3 aa 250-500.
pH: 7
Preservative: 0.01% Thimerosal (merthiolate)
Constituents: 10% Glycerol (glycerin, glycerine), 1.21% Tris, 0.75% Glycine
| WB | |
|---|---|
| Human | Expected |
| Mouse | Predicted |
| Rat | Predicted |
| Species | Dilution info | Notes |
|---|---|---|
Species Human | Dilution info Use at an assay dependent concentration. | Notes - |
| Species | Dilution info | Notes |
|---|---|---|
Species Mouse, Rat | Dilution info - | Notes - |
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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).
GGNT3, MGAT3, N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase III, GNT-III, GlcNAc-T III, N-acetylglucosaminyltransferase III
Rabbit Polyclonal MGAT3 antibody. Suitable for WB and reacts with Human samples. Immunogen corresponding to Recombinant Fragment Protein within Human MGAT3 aa 250-500.
pH: 7
Preservative: 0.01% Thimerosal (merthiolate)
Constituents: 10% Glycerol (glycerin, glycerine), 1.21% Tris, 0.75% Glycine
MGAT3 also known as GlcNAc-TIII is an enzyme involved in the modification of N-glycans. It catalyzes the addition of N-acetylglucosamine in a beta-14 linkage to core mannose residues on asparagine-linked carbohydrate chains. MGAT3 is approximately 60 kDa in mass and finds expression across various tissues but shows higher levels in the liver pancreas and certain immune cells. By adding a bisecting GlcNAc MGAT3 influences the branching pattern of N-glycans which impacts protein stability and cell signaling.
The bisecting GlcNAc addition by MGAT3 plays an important role in cellular communication and immune responses. It often works as part of a larger enzymatic system that modifies proteins and lipids on the cell surface. The activity of MGAT3 affects cell-cell interactions and receptor activity. This modification can hinder the action of galectins a family of proteins that bind specific carbohydrate structures affecting processes like cell-cell adhesion and immune cell function.
MGAT3 integrates into the glycosylation pathway modifying glycoproteins that play roles in both intracellular and intercellular processes. It forms connections with the TGF-beta signaling pathway by altering receptor glycosylation influencing signal strength and cell fate decisions. MGAT3-related modifications can affect how ligands bind to receptors like EGFR affecting the downstream signaling cascade and cellular outcomes.
MGAT3 modifications have implications for cancer progression and immune system disorders. Altered N-glycan branching patterns can lead to abnormal cell proliferation and immune evasion common in cancers such as liver cancer and pancreatic cancer. MGAT3 links to the activity of other glycosyltransferases and its deregulation may impact proteins like PD-L1 which plays a role in immune checkpoint pathways potentially leading to immune escape and tumor progression.
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