Mouse Anti-MGAT2 (AA 1-447) Recombinant Antibody (CBFYM-2167) (CBMAB-M2349-FY)

Name: Mouse Anti-MGAT2 (AA 1-447) Recombinant Antibody (CBFYM-2167)
SKU: CBMAB-M2349-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-2167

Application

ELISA

Immunogen

Full length recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.Immunogen sequence: MRFRIYKRKV LILTLVVAAC GFVLWSSNGR QRKNEALAPP LLDAEPARGA GGRGGDHPSV AVGIRRVSNV SAASLVPAVP QPEADNLTLR YRSLVYQLNF DQTLRNVDKA GTWAPRELVL VVQVHNRPEY LRLLLDSLRK A

Specificity

Human

Antibody Isotype

IgG2a, k

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 1-447

More Infomation

Target

Full Name

mannosyl (alpha-1,6-)-glycoprotein beta-1,2-N-acetylglucosaminyltransferase

Introduction

The product of this gene is a Golgi enzyme catalyzing an essential step in the conversion of oligomannose to complex N-glycans. The enzyme has the typical glycosyltransferase domains: a short N-terminal cytoplasmic domain, a hydrophobic non-cleavable signal-anchor domain, and a C-terminal catalytic domain. Mutations in this gene may lead to carbohydrate-deficient glycoprotein syndrome, type II. The coding region of this gene is intronless. Transcript variants with a spliced 5' UTR may exist, but their biological validity has not been determined.

Entrez Gene ID

4247

UniProt ID

Q10469

Alternative Names

Mannosyl (Alpha-1,6-)-Glycoprotein Beta-1,2-N-Acetylglucosaminyltransferase; N-Glycosyl-Oligosaccharide-Glycoprotein N-Acetylglucosaminyltransferase II; Beta-1,2-N-Acetylglucosaminyltransferase II; Mannoside Acetylglucosaminyltransferase 2; EC 2.4.1.143; GlcNAc-T II; GNT-II

Function

Plays an essential role in protein N-glycosylation. Catalyzes the transfer of N-acetylglucosamine (GlcNAc) onto the free terminal mannose moiety in the core structure of the nascent N-linked glycan chain, giving rise to the second branch in complex glycans.

Biological Process

Oligosaccharide biosynthetic process Source: InterPro
Protein N-linked glycosylation Source: GO_Central
Protein N-linked glycosylation via asparagine Source: UniProtKB
Viral protein processing Source: Reactome

Cellular Location

Golgi apparatus membrane

Involvement in disease

Congenital disorder of glycosylation 2A (CDG2A):
A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions.

Topology

Cytoplasmic: 1-9
Helical: 10-29
Lumenal: 30-447

Meng, W., Brigance, R., Mignone, J., Negash, L., Zhao, G., Ahmad, S., ... & Devasthale, P. (2023). Discovery of 12 (BMS-986172) as a Highly Potent MGAT2 Inhibitor that Achieved Targeted Efficacious Exposures at a Low Human Dose for the Treatment of Metabolic Disorders. Journal of Medicinal Chemistry, 66(18), 13135-13147.

Moore, F., Wang, W., Zhao, G., Mignone, J., Meng, W., Chu, C. H., ... & Devasthale, P. (2023). Discovery of Novel Pyridinones as MGAT2 Inhibitors for the Treatment of Metabolic Disorders. Bioorganic & Medicinal Chemistry Letters, 129362.

Cheng, D., Zinker, B. A., Luo, Y., Shipkova, P., De Oliveira, C. H., Krishna, G., ... & Gordon, D. A. (2022). MGAT2 inhibitor decreases liver fibrosis and inflammation in murine NASH models and reduces body weight in human adults with obesity. Cell Metabolism, 34(11), 1732-1748.

Kempson, J., Hou, X., Sun, J. H., Wong, M., Pawluczyk, J., Li, J., ... & Mathur, A. (2022). Synthesis Optimization, Scale-Up, and Catalyst Screening Efforts toward the MGAT2 Clinical Candidate, BMS-963272. Organic Process Research & Development, 26(4), 1327-1335.

Turdi, H., Chao, H., Hangeland, J. J., Ahmad, S., Meng, W., Brigance, R., ... & Devasthale, P. (2021). Screening hit to clinical candidate: discovery of BMS-963272, a potent, selective MGAT2 inhibitor for the treatment of metabolic disorders. Journal of Medicinal Chemistry, 64(19), 14773-14792.

Poskanzer, S. A., Schultz, M. J., Turgeon, C. T., Vidal‐Folch, N., Liedtke, K., Oglesbee, D., ... & Lam, C. (2021). Immune dysfunction in MGAT2‐CDG: a clinical report and review of the literature. American Journal of Medical Genetics Part A, 185(1), 213-218.

Mochida, T., Take, K., Maki, T., Nakakariya, M., Adachi, R., Sato, K., ... & Takekawa, S. (2020). Inhibition of MGAT2 modulates fat‐induced gut peptide release and fat intake in normal mice and ameliorates obesity and diabetes in ob/ob mice fed on a high‐fat diet. FEBS Open bio, 10(3), 316-326.

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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)
Proteogenomic
Other Protocols

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

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