Recombinant Human GALNT10 Protein: Function & Applications

Recombinant Human GALNT10 Protein is a key enzyme in the initiation of mucin-type O-glycosylation, catalyzing the transfer of N-acetylgalactosamine to serine and threonine residues on target peptides and proteins.

Gene Name

GALNT10

Protein Family

Polypeptide GalNAc transferase (ppGalNAcT) family

Biological Function

Initiates mucin-type O-glycosylation by transferring GalNAc from UDP-GalNAc to Ser/Thr residues of target proteins

Expression System

Recombinant expression system (refer to product datasheet for details)

SKU

rp365117

Research Areas

Glycobiology, cancer biology, enzyme biochemistry

Supplier Reference

absea#PP-657

Background: GALNT10 and O-Glycosylation

GALNT10 (UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 10) is a member of the large GalNAc transferase family, which collectively catalyze the first and committed step in mucin-type O-glycosylation. This post-translational modification is among the most abundant and structurally diverse forms of protein glycosylation in metazoans.

The enzyme transfers N-acetylgalactosamine (GalNAc) from the activated sugar donor UDP-GalNAc onto specific serine (Ser) and threonine (Thr) residues of acceptor proteins, generating the Tn antigen (GalNAc-α-O-Ser/Thr). This initial modification subsequently serves as the scaffold for further elongation by other glycosyltransferases, ultimately producing the complex and diverse O-glycan structures found on mucins and other glycoproteins.

Different members of the GALNT family display distinct, though sometimes overlapping, peptide substrate specificities, expression patterns, and subcellular localizations, allowing for precise spatiotemporal control of O-glycosylation in human tissues.

Biochemical Properties of Recombinant Human GALNT10

Recombinant Human GALNT10 Protein (SKU: rp365117) is produced using a recombinant expression system to ensure consistency and reproducibility across experiments. As a member of the ppGalNAcT family, GALNT10 contains characteristic structural domains including a catalytic domain and a ricin-type lectin domain at the C-terminus, the latter of which is believed to contribute to substrate recognition and binding.

The catalytic mechanism of GALNT10, like other family members, is dependent on divalent metal ions (typically Mn²⁺) and utilizes UDP-GalNAc as the sugar nucleotide donor. Researchers should ensure appropriate cofactor conditions are met in enzymatic assays to achieve optimal activity.

For detailed information on purity, molecular weight, formulation, storage conditions, and activity specifications, users should consult the official product datasheet provided by Aladdin Scientific at the time of purchase, as lot-specific data may vary.

Research Applications

Recombinant Human GALNT10 Protein is suitable for a range of in vitro research applications in the fields of glycobiology, cancer biology, and biochemistry:

• Enzyme Activity Assays: GALNT10 can be used as a positive control or active enzyme in radiometric, fluorometric, or HPLC-based GalNAc transferase activity assays to evaluate substrate preferences or inhibitor compounds.
• Substrate Mapping and Glycoproteomics: The protein is valuable for in vitro glycosylation reactions aimed at identifying and validating GALNT10 substrates, informing glycoproteomic and structural biology studies.
• Cancer Biology Research: Aberrant O-glycosylation patterns, including altered GALNT expression, are well-documented in various cancers. Recombinant GALNT10 supports mechanistic studies into tumor-associated glycan changes and their functional consequences.
• Drug Discovery and Inhibitor Screening: As a validated target in disease-relevant pathways, GALNT10 is useful in high-throughput screening campaigns designed to identify small-molecule inhibitors of O-glycosylation initiation.
• Structural Biology: Purified recombinant protein may support crystallographic or biophysical studies of GalNAc transferase structure–function relationships.

Handling, Storage, and Quality Considerations

To ensure optimal performance of Recombinant Human GALNT10 Protein, researchers should adhere to the following general best practices for recombinant enzyme handling:

• Storage: Store the protein according to the conditions specified on the product datasheet. Recombinant proteins are typically stored at −80 °C to prevent degradation. Avoid repeated freeze-thaw cycles, which can compromise activity and integrity.
• Aliquoting: Upon first thaw, it is recommended to prepare single-use aliquots to minimize freeze-thaw cycling.
• Buffer Compatibility: Ensure the assay buffer is compatible with the protein formulation. Consult the datasheet for recommended buffer conditions.
• Quality Control: Aladdin Scientific's recombinant proteins are subject to quality control testing. Lot-specific purity and activity data are provided with each shipment. Researchers should verify these parameters upon receipt.
• Biosafety: Handle as per standard laboratory biosafety guidelines for recombinant proteins. Refer to the Safety Data Sheet (SDS) for specific hazard information.

Frequently asked questions

What is the biological function of GALNT10?

GALNT10 encodes a polypeptide N-acetylgalactosaminyltransferase that initiates mucin-type O-glycosylation by transferring GalNAc from UDP-GalNAc to serine or threonine residues on target proteins. This modification is critical for the biosynthesis of mucins and many other glycoproteins involved in cell signaling, adhesion, and cancer biology.

What are the recommended applications for Recombinant Human GALNT10 Protein (rp365117)?

Recombinant Human GALNT10 Protein is recommended for in vitro enzyme activity assays, substrate specificity studies, glycoproteomic investigations, cancer biology research involving aberrant O-glycosylation, and small-molecule inhibitor screening. It may also be suitable for structural biology applications. Please consult the product datasheet for verified application-specific conditions.

What cofactors are required for GALNT10 enzymatic activity?

Like other members of the GalNAc transferase family, GALNT10 requires divalent metal ions—most commonly Mn²⁺—for catalytic activity, along with the sugar nucleotide donor UDP-GalNAc. Researchers should ensure these components are present at appropriate concentrations in their assay systems. Refer to the product datasheet and relevant literature for optimized assay conditions.

How should Recombinant Human GALNT10 Protein be stored?

Recombinant Human GALNT10 Protein should be stored according to the conditions specified on the product datasheet, typically at −80 °C. Avoid repeated freeze-thaw cycles to preserve enzyme activity and protein integrity. Single-use aliquots are strongly recommended upon first thaw.

Is GALNT10 relevant to cancer research?

Yes, aberrant expression and activity of GALNT family members, including GALNT10, have been associated with altered O-glycosylation patterns observed in multiple cancer types. These changes can affect tumor cell adhesion, invasion, immune evasion, and response to therapy, making GALNT10 a relevant target for mechanistic and translational cancer research.

References

1. Bennett, E. P. et al. Control of mucin-type O-glycosylation: A classification of the polypeptide GalNAc-transferase gene family. Glycobiology, 2012.
2. Gill, D. J. et al. Initiation of GalNAc-type O-glycosylation in the endoplasmic reticulum promotes cancer cell invasiveness. Proceedings of the National Academy of Sciences, 2013.
3. Tran, D. T. & Ten Hagen, K. G. Mucin-type O-glycosylation during development. Journal of Biological Chemistry, 2013.

Products are supplied for research and development use only. Not for use in humans, animals, diagnosis, or therapy.