Recombinant Human MGAT4A comes from a mammalian cell system and covers amino acid region 93-535. The protein features dual tags—an N-terminal 10xHis-tag and a C-terminal Myc-tag—which help with purification and detection. SDS-PAGE analysis shows the protein maintains a purity level above 85%, making it suitable for research applications. This recombinant protein is intended for research use only and doesn't include the complete sequence.
MGAT4A appears to play an important role in N-glycan branching, a process that seems crucial for proper protein folding and function. The protein acts as a glycosyltransferase, adding N-acetylglucosamine to specific mannose residues on glycoproteins. This modification is likely vital for cellular processes like cell-cell communication and protein stability. That's why MGAT4A has become a protein of interest in studies examining glycosylation pathways and related disorders.
Potential Applications
Note: The applications listed below are based on what we know about this protein's biological functions, published research, and experience from experts in the field. However, we haven't fully tested all of these applications ourselves yet. We'd recommend running some preliminary tests first to make sure they work for your specific research goals.
1. Glycosyltransferase Enzyme Characterization Studies
Researchers can use this recombinant MGAT4A protein to investigate the enzymatic properties and substrate specificity of this N-acetylglucosaminyltransferase under controlled in vitro conditions. The dual His and Myc tags make protein purification and detection more straightforward, allowing scientists to study enzyme kinetics, optimal reaction conditions, and cofactor requirements. Since the protein comes from a mammalian expression system, it's more likely to have proper protein folding and post-translational modifications that may be critical for enzymatic function. Studies like these could help us understand the biochemical mechanisms behind N-glycan biosynthesis pathways.
2. Protein-Protein Interaction Studies
Both the N-terminal His tag and C-terminal Myc tag make this protein well-suited for pull-down assays and co-immunoprecipitation experiments. These approaches might help identify potential binding partners or regulatory proteins that interact with MGAT4A. The tags allow for immobilization on appropriate matrices and detection using tag-specific antibodies, which could lead to discovering protein complexes involved in glycosylation processes. Interaction studies like these may reveal regulatory mechanisms and pathway components that influence how MGAT4A functions in cellular glycan processing.
3. Antibody Development and Validation
This purified recombinant protein works well as an antigen for generating specific antibodies against human MGAT4A or for validating existing antibodies. The high purity level (>85%) and defined protein region (aa 93-535) offer a standardized target for immunization protocols or ELISA-based antibody screening. The dual tags also provide alternative detection methods to confirm antibody specificity and test for cross-reactivity.
4. Structural and Biophysical Analysis
Scientists can apply this recombinant MGAT4A protein in structural biology approaches like X-ray crystallography, NMR spectroscopy, or cryo-electron microscopy to understand the three-dimensional structure of this glycosyltransferase domain. The mammalian expression system should provide properly folded protein that's suitable for biophysical characterization techniques, including dynamic light scattering, thermal stability assays, and circular dichroism spectroscopy. Analysis like this might provide insights into the molecular architecture and conformational properties of this important glycan-processing enzyme.
