Recombinant Human GALNT11 Protein: Function & Applications

Recombinant Human GALNT11 Protein is a recombinantly expressed form of polypeptide N-acetylgalactosaminyltransferase 11, a key enzyme mediating the initiation of mucin-type O-linked glycosylation in human cells.

Protein Name

Recombinant Human GALNT11 (Polypeptide N-Acetylgalactosaminyltransferase 11)

SKU

rp369233

Gene Name

GALNT11

Protein Family

GalNAc-transferase (GALNT) family

Biological Function

Catalyzes the initial transfer of GalNAc to serine or threonine residues, initiating mucin-type O-glycosylation

Expression System

Recombinant (specific host system to be confirmed; see product datasheet)

Research Applications

Glycobiology, O-glycosylation pathway studies, enzyme activity assays, protein interaction studies

What Is GALNT11 and Why Does It Matter?

GALNT11, also known as polypeptide N-acetylgalactosaminyltransferase 11, is a member of the large GalNAc-transferase enzyme family. These enzymes are responsible for catalyzing the first committed step in mucin-type O-linked glycosylation: the transfer of N-acetylgalactosamine (GalNAc) from the donor substrate UDP-GalNAc to serine or threonine residues on target proteins.

O-glycosylation is one of the most abundant and functionally diverse post-translational modifications (PTMs) found in eukaryotic cells. It plays critical roles in protein folding, stability, cell–cell communication, immune recognition, and the regulation of signaling pathways. The GALNT family comprises at least 20 members in humans, each displaying distinct, though sometimes overlapping, substrate specificities and tissue expression patterns.

GALNT11 has been identified as a relevant enzyme in developmental signaling contexts, with studies suggesting involvement in Notch and other receptor-mediated pathways through site-specific glycosylation of key substrates. Its expression profile and substrate selectivity make it a subject of active research in developmental biology, cancer biology, and congenital disease research.

Protein Structure and Biochemical Properties

Like other members of the GALNT family, GALNT11 is a type II transmembrane protein that localizes primarily to the Golgi apparatus, the principal subcellular site of O-glycosylation. The protein contains a short N-terminal cytoplasmic tail, a single transmembrane domain, a stem region, and a large luminal catalytic domain.

The catalytic domain harbors two key structural motifs characteristic of GalNAc-transferases: the catalytic GT-A fold responsible for sugar nucleotide binding and transfer, and a lectin domain that recognizes already-glycosylated substrates, thereby enabling dense, ordered glycosylation patterns on mucin-type proteins.

Recombinant Human GALNT11 Protein (SKU: rp369233) is produced using recombinant expression technology, enabling researchers to obtain a defined, consistent preparation of this enzyme outside its native cellular environment. Precise purity, formulation buffer, molecular weight, and activity specifications are detailed in the product datasheet; researchers are advised to consult the datasheet for lot-specific quality control data.

Research Applications

Recombinant Human GALNT11 Protein is suitable for a range of in vitro research applications where a defined, soluble or recombinant enzyme preparation is required:

• Enzyme Activity Assays: Characterizing the substrate specificity of GALNT11 using peptide or glycopeptide substrates in radiometric, fluorescent, or mass spectrometry-based activity assays.
• O-Glycosylation Pathway Research: Investigating the role of GALNT11 in initiating mucin-type O-glycosylation on specific protein substrates, including signaling receptors and extracellular matrix components.
• Protein–Protein Interaction Studies: Using the recombinant protein as a tool to study interactions with partner proteins, regulatory factors, or inhibitors.
• Drug Discovery and Inhibitor Screening: Employing the purified enzyme in high-throughput or focused screens for small-molecule inhibitors of GALNT11 activity, relevant to cancer and congenital disease therapeutic programs.
• Structural Studies: Providing homogeneous protein for crystallography or biophysical characterization of the GALNT11 catalytic and lectin domains.

Researchers working on Notch signaling, left-right body axis determination, cystic kidney disease models, or mucin glycoprotein biology will find this recombinant protein particularly relevant to their experimental programs.

Handling, Storage, and Quality Considerations

Proper handling and storage of recombinant proteins are essential to maintaining activity and ensuring reproducible experimental results. General best-practice recommendations for recombinant enzyme preparations include:

• Storage: Store at –80 °C for long-term preservation. Avoid repeated freeze–thaw cycles, which can denature the protein and reduce enzymatic activity. Aliquot upon receipt if multiple uses are anticipated.
• Working Conditions: Keep protein on ice during experimental setup. Use appropriate buffer conditions as specified in the product datasheet to maintain enzyme stability and activity.
• Quality Control: Each lot of Recombinant Human GALNT11 Protein is subject to quality control testing. Consult the certificate of analysis (CoA) provided with the product for lot-specific data on purity (typically assessed by SDS-PAGE), identity, and biological activity where applicable.
• Carrier Proteins: If the formulation includes BSA or other stabilizers, account for these when designing downstream assays, particularly those sensitive to exogenous protein.

For specific storage temperature, buffer composition, recommended concentration ranges, and expiry, always refer to the product datasheet and CoA for SKU rp369233 available from Aladdin Scientific.

Frequently asked questions

What is the biological function of GALNT11?

GALNT11 (polypeptide N-acetylgalactosaminyltransferase 11) catalyzes the transfer of N-acetylgalactosamine (GalNAc) from UDP-GalNAc to serine or threonine residues on target proteins, initiating mucin-type O-linked glycosylation. This modification plays essential roles in protein stability, cell signaling, and intercellular communication. GALNT11 has been implicated in developmental pathways including Notch signaling.

What research applications is Recombinant Human GALNT11 Protein suitable for?

Recombinant Human GALNT11 Protein (rp369233) is suitable for enzyme activity assays, O-glycosylation pathway studies, protein–protein interaction analyses, inhibitor screening, and structural biology studies. It is particularly useful for researchers investigating mucin-type glycosylation, Notch signaling, developmental biology, and related disease models.

How should Recombinant Human GALNT11 Protein be stored to maintain activity?

The protein should be stored at –80 °C for long-term stability. Repeated freeze–thaw cycles should be avoided by aliquoting the protein upon receipt. Always refer to the product-specific datasheet and certificate of analysis for SKU rp369233 for the precise storage buffer, recommended concentration, and shelf-life information.

What distinguishes GALNT11 from other members of the GALNT family?

While all GALNT family members initiate mucin-type O-glycosylation, individual members differ in their substrate peptide specificity, tissue expression patterns, and regulatory roles. GALNT11 has a distinct substrate preference and has been specifically linked to developmental signaling contexts such as Notch pathway regulation and left-right body axis determination. The precise substrate scope of GALNT11 relative to other family members remains an active area of research.

References

1. Bennett EP, Mandel U, Clausen H, Gerken TA, Fritz TA, Tabak LA. Control of mucin-type O-glycosylation: a classification of the polypeptide GalNAc-transferase gene family. Glycobiology. 2012;22(6):736-756. doi:10.1093/glycob/cwr182
2. Schjoldager KT, Clausen H. Site-specific protein O-glycosylation modulates proprotein processing - deciphering specific functions of the large polypeptide GalNAc-transferase gene family. Biochimica et Biophysica Acta. 2012;1820(12):2079-2094.
3. Boskovski MT, Yuan S, Pedersen NB, et al. The heterotaxy gene GALNT11 glycosylates Notch to orchestrate cilia type and laterality. Nature. 2013;504(7480):456-459. doi:10.1038/nature12723

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