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AB168400

Anti-GALNT10 antibody

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(1 Publication)

Mouse Polyclonal GALNT10 antibody. Suitable for WB and reacts with Human samples. Cited in 1 publication. Immunogen corresponding to Recombinant Full Length Protein corresponding to Human Polypeptide N-acetylgalactosaminyltransferase 10.

View Alternative Names

Polypeptide N-acetylgalactosaminyltransferase 10, Polypeptide GalNAc transferase 10, Protein-UDP acetylgalactosaminyltransferase 10, UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10, GalNAc-T10, pp-GaNTase 10, GALNT10

Key facts

Host species

Mouse

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

WB

applications

Immunogen

Recombinant Full Length Protein corresponding to Human Polypeptide N-acetylgalactosaminyltransferase 10.

Q86SR1

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein A
Storage buffer
pH: 7.4 Constituents: PBS
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot

Supplementary information

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

GALNT10 also known as polypeptide N-acetylgalactosaminyltransferase 10 is a member of the GalNAc-T family of enzymes. The enzyme plays an important mechanical role by catalyzing the transfer of N-acetylgalactosamine (GalNAc) to serine and threonine residues on proteins a process called O-glycosylation. This enzymatic activity is critical for proper protein modification and function. GALNT10 has a molecular mass of approximately 68 kDa. It is expressed in a variety of tissues notably in the liver which indicates its extensive role in protein processing within this organ.
Biological function summary

Polypeptide N-acetylgalactosaminyltransferase 10 influences the initial steps of mucin-type O-glycosylation which significantly affects protein stability and cell signaling. It is not part of a large enzyme complex but its function is integral to the regulation of substrate-specific modifications. This protein aids in the modulation of various glycoproteins impacting diverse physiological processes. Alterations in its activity potentially lead to changes in cell-cell interactions and mucosal protection.

Pathways

GALNT10 is involved in O-glycan biosynthetic pathways where its role is pivotal in glycan structure formation and diversity. This pathway enables the proper glycosylation of proteins that are essential for cell-cell communication and adhesion. GALNT10's activity relates closely to other glycosyltransferases within this pathway including GALNT1 reflecting its cooperative nature within glycosylation networks. Moreover it supports the broader glycosylation landscape by influencing the availability of glycosylation sites on various protein substrates.

GALNT10 has associations with specific conditions such as cancers and metabolic syndromes. Abnormal function or expression of this enzyme can contribute to tumorigenesis due to its influence on glycosylation patterns that affect cell adhesion and signaling. The enzyme is also linked to liver disorders arising from its high expression in liver tissue and its impact on protein processing. In the context of cancer GALNT10’s interactions with similar glycosylation enzymes like GALNT3 illustrate its role in modifying glycan structures which are critical for cellular transformation and cancer progression.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

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 activity toward Muc5Ac and EA2 peptide substrates.
See full target information Polypeptide N-acetylgalactosaminyltransferase 10

Publications (1)

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

Nature communications 14:870 PubMed36797266

2023

Spatial proteomics reveals secretory pathway disturbances caused by neuropathy-associated TECPR2.

Applications

Unspecified application

Species

Unspecified reactive species

Karsten Nalbach,Martina Schifferer,Debjani Bhattacharya,Hung Ho-Xuan,Wei Chou Tseng,Luis A Williams,Alexandra Stolz,Stefan F Lichtenthaler,Zvulun Elazar,Christian Behrends
View all publications

Product promise

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