MGAT3 Antibody (N-term) 精选
Purified Rabbit Polyclonal Antibody (Pab)
- 产品详情
- 实验流程
- 背景知识
Application
| WB, IHC-P, E |
|---|---|
| Primary Accession | Q09327 |
| Other Accession | NP_002400 |
| Reactivity | Human, Mouse |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 61313 Da |
| Antigen Region | 72-102 aa |
| Gene ID | 4248 |
|---|---|
| Other Names | Beta-1, 4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase, N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase III, GNT-III, GlcNAc-T III, N-acetylglucosaminyltransferase III, MGAT3, GGNT3 |
| Target/Specificity | This MGAT3 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 72-102 amino acids from the N-terminal region of human MGAT3. |
| Dilution | WB~~1:1000 IHC-P~~1:100 E~~Use at an assay dependent concentration. |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | MGAT3 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
For Research Use Only. Not For Use In Diagnostic Procedures.
| Name | MGAT3 (HGNC:7046) |
|---|---|
| Synonyms | GGNT3 |
| 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). Adds bisecting GlcNAc residue to complex-type N-linked-glycans attached on fragment crystallizable (Fc) of IgGs. Readily converts fucosylated and non-fucosylated core glycoforms with terminal GlcNAcs on both antennae. Prior galactosylation of GlcNAc on the alpha(1->3) Man branch prevents N-glycan bisection, whereas galactosylation of GlcNAc on the alpha(1->6) Man branch is permissive. |
| Cellular Location | Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. Note=Colocalizes with ST6GAL1 and B4GALT1 in the Golgi stacks of cisternae, including the cis-part of the Golgi stacks |
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
There are believed to be over 100 different glycosyltransferases involved in the synthesis of protein-bound and lipid-bound oligosaccharides. MGAT3 (N-acetylglucosaminyltransferase III) transfers a GlcNAc residue to the beta-linked mannose of the trimannosyl core of N-linked oligosaccharides and produces a bisecting GlcNAc. Expression of this gene may be controlled by a multiple-promoter system.
REFERENCES
Shibukawa, Y., et al., J. Biol. Chem. 278(5):3197-3203 (2003).
Koyama, N., et al., Eur. J. Biochem. 238(3):853-861 (1996).
Kim, Y.J., et al., Gene 170(2):281-283 (1996).
Ihara, Y., et al., J. Biochem. 113(6):692-698 (1993).
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