MGAT1, Polyclonal Antibody

Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase; N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I; GNT-I; GlcNAc-T I; MGAT1; GGNT1; GLCT1; GLYT1; MGAT

For Research Use Only. Not for use in diagnostic procedures.

Polyclonal

Rabbit Ig

Rabbit

This MGAT1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide selected from the C-terminal region of human MGAT1.

Purified Rabbit Polyclonal Antibody (Pab)

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.

Vial Concentration: 2 (lot specific)

Maintain refrigerated at 2-8 degree C for up to 6 months. For long term storage store at -20 degree C in small aliquots to prevent freeze-thaw cycles.

Small volumes of anti-MGAT1 antibody vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

There are believed to be over 100 different glycosyltransferases involved in the synthesis of protein-bound and lipid-bound oligosaccharides. MGAT1 (UDP-N-acetylglucosamine:alpha-3-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I) is a medial-Golgi enzyme essential for the synthesis of hybrid and complex N-glycans. The protein, encoded by a single exon, shows typical features of a type II transmembrane protein. The protein is believed to be essential for normal embryogenesis.

Signal Transduction

ELISA (EIA), Immunohistochemistry (IHC), Western Blot (WB)

WB~~1:1000

Western blot analysis of anti-hMGAT1-R426 Pab in Y79 cell line lysate. hMGAT1-R426(arrow) was detected using the purified Pab.

Formalin-fixed and paraffin-embedded human cancer tissue reacted with the primary antibody, which was peroxidase-conjugated to the secondary antibody, followed by AEC staining. This data demonstrates the use of this antibody for immunohistochemistry; clinical relevance has not been evaluated. BC = breast carcinoma; HC = hepatocarcinoma.

50878

mannosyl (alpha-1,3-)-glycoprotein beta-1,2-N-acetylglucosaminyltransferase

alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase

Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase

GGNT1; GLCT1; GLYT1; MGAT; GNT-I; GlcNAc-T I  [Similar Products]

MGAT1_HUMAN

There are believed to be over 100 different glycosyltransferases involved in the synthesis of protein-bound and lipid-bound oligosaccharides. UDP-N-acetylglucosamine:alpha-3-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I is a medial-Golgi enzyme essential for the synthesis of hybrid and complex N-glycans. The protein, encoded by a single exon, shows typical features of a type II transmembrane protein. The protein is believed to be essential for normal embryogenesis. Several variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008]

MGAT1: Initiates complex N-linked carbohydrate formation. Essential for the conversion of high-mannose to hybrid and complex N-glycans. Belongs to the glycosyltransferase 13 family.

Protein type: EC 2.4.1.101; Transferase; Membrane protein, integral; Glycan Metabolism - N-glycan biosynthesis

Chromosomal Location of Human Ortholog: 5q35

Cellular Component: Golgi membrane; membrane; integral to membrane; vesicle

Molecular Function: acetylglucosaminyltransferase activity; metal ion binding; alpha-1,3-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity

Biological Process: cellular protein metabolic process; in utero embryonic development; carbohydrate metabolic process; protein amino acid glycosylation; UDP-N-acetylglucosamine catabolic process; protein amino acid N-linked glycosylation via asparagine; post-translational protein modification

Tan, J., et al., Eur. J. Biochem. 231(2):317-328 (1995).
Kumar, R., et al., Glycobiology 2(4):383-393 (1992).
Hull, E., et al., Biochem. Biophys. Res. Commun. 176(2):608-615 (1991).
Kumar, R., et al., Proc. Natl. Acad. Sci. U.S.A. 87(24):9948-9952 (1990).
Yip, B., et al., Biochem. J. 321 (Pt 2), 465-474 (1997).

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