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Recombinant Human Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase (MGAT2), partial

Recombinant Human Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase (MGAT2), partial — Plays an essential role in protein N-glycosylation. Purity >90%.

SKU: BCRECP-001159 Categories: ,

Product Specifications

Product SkuBCRECP-001159
Product DescriptionRecombinant Human Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase (MGAT2) Protein is expressed from E.coli with N-terminal 10xHis-tagged and C-terminal Myc-tagged. It contains 30-447aa. [Accession | Q10469].
Uniprot No.Q10469
Gene NamesMGAT2
PurityGreater than 90% as determined by SDS-PAGE.
Expression SystemE.coli
Expression Region30-447aa
SpeciesHomo sapiens (Human)
Tag InfoN-terminal 10xHis-tagged and C-terminal Myc-tagged
Molecular weight55.7kDa
ActivityPlease contact us to obtain bioactivity data.
BufferIf the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose.
StorageStore at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Research AreasSignal Transduction

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 Context

Subcellular Location: Golgi apparatus membrane (Single-pass type II membrane protein)
Disease Association: 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. [The disease is caused by variants affecting the gene represented in this entry]
Pathway: Protein modification; protein glycosylation

Product Specifications

Recombinant Human Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase (MGAT2), partial is a recombinant protein from Homo sapiens (Human), expressed in E.coli, covering amino acids 30-447aa, with N-terminal 10xHis-tagged and C-terminal Myc-tagged tag, molecular weight 55.7kDa, purity Greater than 90% as determined by SDS-PAGE.. Suitable for ELISA and Western Blot applications.

SDS-PAGE: Single band at expected molecular weight confirming purity.

ELISA: Suitable as coating antigen or detection standard.

Western Blot: Compatible with standard Western Blot protocols.

Protein Interaction: Validated for SPR (Surface Plasmon Resonance) and BLI (Bio-Layer Interferometry) studies.

Shipping: Shipped at ambient temperature. Lyophilized protein is stable during transit.

Storage: Store lyophilized protein at -20°C to -80°C. Reconstituted protein should be aliquoted and stored at -80°C. Avoid repeated freeze-thaw cycles.

Shelf Life: 12 months from date of receipt when stored as recommended.

Shipping Time: Orders placed before 2 PM EST ship same day. International orders typically deliver within 5-10 business days.

Protein Biology

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

Subcellular Location

Golgi apparatus membrane (Single-pass type II membrane protein)

Disease Association

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. [The disease is caused by variants affecting the gene represented in this entry]

Subunit

Homodimer

Pathway

Protein modification; protein glycosylation

Gene: MGAT2  |  Organism: Homo sapiens  |  Synonyms: Beta-1,2-N-acetylglucosaminyltransferase II; GlcNAc-T II; Mannoside acetylglucosaminyltransferase 2; N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II
Key Publications

Frequently Asked Questions

How do I order or inquire about this product?

Fill out the Online Inquiry form with your required quantity and specifications. You can also email sales@biocrestsci.com. Our team typically responds within 4 business hours with a quote and availability confirmation.

What is the shipping and delivery time?

Orders placed before 2 PM EST ship the same day. Domestic (US) delivery typically takes 2-3 business days. International orders deliver within 5-10 business days. All products are shipped at ambient temperature with appropriate packaging to ensure stability.

How should I store this recombinant protein?

Lyophilized proteins should be stored at -20°C to -80°C upon receipt. After reconstitution, aliquot and store at -80°C. Avoid repeated freeze-thaw cycles. Shelf life is 12 months from date of receipt when stored as recommended.

What quality controls are performed on your products?

Each product undergoes SDS-PAGE purity analysis (typically >85-95%), endotoxin testing, and bioactivity validation. Products are validated for ELISA, Western Blot, and SPR/BLI applications as specified on this product page. A Certificate of Analysis (CoA) is available upon request.

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