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AB276585

Recombinant Human GALNT2 protein (His tag)

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(1 Publication)

Recombinant Human GALNT2 protein (His tag) is a Human Fragment protein, in the 52 to 571 aa range, expressed in HEK 293 cells, with >95%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE.

View Alternative Names

Polypeptide N-acetylgalactosaminyltransferase 2, Polypeptide GalNAc transferase 2, Protein-UDP acetylgalactosaminyltransferase 2, UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2, GalNAc-T2, pp-GaNTase 2, GALNT2

1 Images
SDS-PAGE - Recombinant Human GALNT2 protein (His tag) (AB276585)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human GALNT2 protein (His tag) (AB276585)

SDS-PAGE analysis of ab276585

Key facts

Purity

>95% SDS-PAGE

Endotoxin level

< 1 EU/µg

Expression system

HEK 293 cells

Tags

His tag N-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

Q10471

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.5 Constituents: 0.87% Sodium chloride, 0.3% Tris, 0.05% Polyoxyethylene lauryl ether

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"KKKDLHHSNGEEKAQSMETLPPGKVRWPDFNQEAYVGGTMVRSGQDPYARNKFNQVESDKLRMDRAIPDTRHDQCQRKQWRVDLPATSVVITFHNEARSALLRTVVSVLKKSPPHLIKEIILVDDYSNDPEDGALLGKIEKVRVLRNDRREGLMRSRVRGADAAQAKVLTFLDSHCECNEHWLEPLLERVAEDRTRVVSPIIDVINMDNFQYVGASADLKGGFDWNLVFKWDYMTPEQRRSRQGNPVAPIKTPMIAGGLFVMDKFYFEELGKYDMMMDVWGGENLEISFRVWQCGGSLEIIPCSRVGHVFRKQHPYTFPGGSGTVFARNTRRAAEVWMDEYKNFYYAAVPSARNVPYGNIQSRLELRKKLSCKPFKWYLENVYPELRVPDHQDIAFGALQQGTNCLDTLGHFADGVVGVYECHNAGGNQEWALTKEKSVKHMDLCLTVVDRAPGSLIKLQGCRENDSRQKWEQIEGNSKLRHVGSNLCLDSRTAKSGGLSVEVCGPALSQQWKFTLNLQQ","proteinLength":"Fragment","predictedMolecularWeight":"61.6 kDa","actualMolecularWeight":null,"aminoAcidEnd":571,"aminoAcidStart":52,"nature":"Recombinant","expressionSystem":"HEK 293 cells","accessionNumber":"Q10471","tags":[{"tag":"His","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Ambient - Can Ship with Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The GALNT2 protein also known as polypeptide N-acetylgalactosaminyltransferase 2 facilitates the initial step of mucin-type O-glycosylation by transferring N-acetylgalactosamine to serine or threonine residues on proteins. This enzyme has a molecular mass of approximately 69 kDa. GALNT2 expression occurs across various tissues with higher levels observed in the liver and small intestine. It plays a role in the modification of secreted and membrane-bound mucin glycoproteins.
Biological function summary

The function of GALNT2 extends beyond simple glycosylation. It contributes to protein sorting and stability within the Golgi apparatus. GALNT2 functions as a solitary entity and not within a larger protein complex. Its enzymatic activity has regulatory implications in lipid metabolism and signal transduction influencing the bioavailability of certain hormones and receptors by modifying glycans on their surface.

Pathways

GALNT2 plays roles in both the O-glycan biosynthesis pathway and the Wnt signaling pathway. In the O-glycan biosynthesis pathway GALNT2 interacts with other glycosyltransferases to ensure the proper glycosylation of proteins. Within the Wnt signaling pathway it indirectly influences the stability of certain proteins like frizzled receptors which are necessary for effective signaling. These pathways highlight GALNT2's integrative role in cellular processes such as development and homeostasis.

GALNT2 has an association with cardiovascular diseases and metabolic syndrome. Research shows that altered glycosylation patterns mediated by GALNT2 can affect the functionality of apolipoproteins like APOC3 thereby influencing lipid levels in the blood. Dysregulation of GALNT2 activity can lead to imbalances in these metabolic processes contributing to the pathogenesis of these conditions. Understanding GALNT2’s role presents potential therapeutic angles for managing such diseases.

Specifications

Form

Lyophilized

General info

Function

Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b. Probably involved in O-linked glycosylation of the immunoglobulin A1 (IgA1) hinge region. Involved in O-linked glycosylation of APOC-III, ANGPTL3 and PLTP. It participates in the regulation of HDL-C metabolism (PubMed : 27508872, PubMed : 32293671).

Sequence similarities

Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily.

Product protocols

Target data

Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b. Probably involved in O-linked glycosylation of the immunoglobulin A1 (IgA1) hinge region. Involved in O-linked glycosylation of APOC-III, ANGPTL3 and PLTP. It participates in the regulation of HDL-C metabolism (PubMed : 27508872, PubMed : 32293671).
See full target information Polypeptide N-acetylgalactosaminyltransferase 2

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Nutrients 16: PubMed38999895

2024

Gastroprotective Effect of Isoferulic Acid Derived from Foxtail Millet Bran against Ethanol-Induced Gastric Mucosal Injury by Enhancing GALNT2 Enzyme Activity.

Applications

Unspecified application

Species

Unspecified reactive species

Xiaoqin La,Xiaoting He,Jingyi Liang,Zhaoyan Zhang,Hanqing Li,Yizhi Liu,Ting Liu,Zhuoyu Li,Changxin Wu
View all publications

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