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N-Acetylglucosamine (GlcNAc)-type Glycoprotein Conjugation Service

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Why Is N-Acetylglucosamine (GlcNAc)-Type Glycoprotein Conjugation Services Necessary?

GlcNAc-type glycoproteins encompass a vast array of proteins modified with N-acetylglucosamine residues. This includes proteins with N-linked glycans, O-linked GlcNAc, and glycosylphosphatidylinositol (GPI) anchors. This type of glycoprotein is widely present in humans and other organisms and is mainly involved in cell-to-cell interactions and interactions between cells and the external environment. In medical research, conjugation glycoproteins are often used in cancer research, vaccine development, and the design of therapeutic antibodies. The necessity of providing conjugation services for GlcNAc-type glycoproteins is mainly reflected in:

  • Elucidating biological roles: Understanding how GlcNAc modifications regulate protein functions and cellular pathways.
  • Biomarker discovery: Identifying GlcNAc-modified proteins as potential diagnostic or prognostic markers for various diseases.
  • Therapeutic development: Designing and synthesizing targeted glycoconjugates for drug delivery, vaccine development, or therapeutic intervention.
  • Diagnostic tool development: Creating highly specific reagents for detecting GlcNAc-modified proteins in clinical samples.

Our Glycoprotein Conjugation service enables clients to accelerate drug discovery, obtain high-quality glycoconjugates, and streamline biomarker identification through advanced metabolic engineering and bioorthogonal chemistry techniques.

How to Conjugate GlcNAc-type Glycoprotein?

The core coupling principle of our GlcNAc-type glycoprotein conjugation service relies primarily on bioorthogonal click chemistry, such as Aldehyde Reaction-based and Azide Reaction-based Glycoprotein Conjugation services. This principle is rooted in the strategic incorporation of a bioorthogonal handle onto the GlcNAc residue, which can then react selectively and efficiently with a functionalized probe or molecule without interfering with native biological processes. We generally perform glycoprotein conjugation by the following method.

Metabolic Precursor Engineering

We introduce synthetic GlcNAc precursors (e.g., N-azidoacetylgalactosamine (GalNAz) or N-azidoacetylglucosamine (GlcNAz)) into cellular systems. These precursors contain an azide functional group, which is chemically inert in biological systems but highly reactive with alkynes.

Enzymatic Incorporation

Cellular enzymes, such as O-GlcNAc transferase (OGT), recognize these modified sugars and metabolically incorporate them into newly synthesized or existing GlcNAc-modified proteins.

Bioorthogonal Click Reaction

Once the proteins are labeled with azide-GlcNAc, an alkyne-containing probe (e.g., a fluorescent dye, biotin) is introduced. The azide and alkyne groups react rapidly and specifically via click chemistry (either copper-catalyzed or strain-promoted), forming a stable triazole linkage. This reaction occurs under mild, physiological conditions, preserving protein integrity and functions.

This approach offers superior specificity and efficiency compared to traditional chemical modification methods, which often rely on less selective reactions with native amino acid residues.

Fig. 1. Azide-based metabolic engineering strategies. (OA Literature)Fig.1 Application of azide-based click chemistry in glycans.1,

Unlocking Glycoprotein Insights: Creative Biolabs' GlcNAc-type Glycoprotein Conjugation Service

Creative Biolabs' GlcNAc-type glycoprotein conjugation service provides a robust platform for the selective and efficient attachment of various molecules (e.g., fluorescent dyes, biotin, therapeutic agents, nanoparticles) to GlcNAc residues on target proteins. Our service provision involves a meticulous, multi-stage process to ensure high-quality and reliable conjugates.

Project Consultation & Design

We begin with an in-depth discussion to understand your specific research objectives. Our experts will help design the optimal GlcNAc-type glycoprotein conjugation strategy, considering your target molecule, desired label, and downstream applications. This step ensures a tailored approach for maximum efficiency and success.

Metabolic Labeling

Cells or organisms are cultured in the presence of engineered azido-sugar precursors (e.g., GalNAz), which are metabolically incorporated into GlcNAc residues via cellular enzymatic pathways. This results in the de novo biosynthesis of azido-tagged glycoproteins within the biological system.

Protein Isolation & Purification

Following metabolic labeling, target proteins are isolated from the cellular matrix. We employ robust purification protocols, including affinity chromatography and size-exclusion chromatography, to obtain highly pure protein samples enriched with the azido-tagged GlcNAc modifications, ensuring optimal subsequent conjugation efficiency.

Bioorthogonal Conjugation

The purified azido-tagged glycoproteins are then subjected to highly specific bioorthogonal conjugation reactions. Utilizing click chemistry (e.g., copper-catalyzed azide-alkyne cycloaddition or strain-promoted azide-alkyne cycloaddition), we covalently attach various probes, tags, or therapeutic molecules to the azido-GlcNAc residues. This step ensures precise and efficient labeling without interfering with native protein functions.

Quality Control & Characterization

Post-conjugation, rigorous quality control measures are implemented. This includes mass spectrometry (MS) for verification of conjugation, SDS-PAGE for purity and size assessment, and functional assays to confirm the integrity and activity of the conjugated glycoprotein. This ensures the final product meets the standards for your research.

Unlock the full potential of your glycoprotein research with Creative Biolabs' GlcNAc-type glycoprotein conjugation service. Our commitment to scientific excellence and client satisfaction ensures superior results for your most challenging projects. Our expert team is ready to discuss your specific project requirements and provide tailored solutions. Please contact us to obtain more content.

FAQs

Q1: What types of proteins can be modified using Creative Biolabs' GlcNAc-type conjugation service?

A1: Our service is highly versatile and can be applied to a wide range of proteins that are naturally or can be engineered to be GlcNAc-modified. This includes recombinant proteins, native proteins from cell lysates, and even proteins within live cells through metabolic labeling. If you have a specific protein in mind, please reach out for a detailed consultation to discuss its suitability.

Q2: How does this service compare to general protein labeling methods?

A2: Unlike general protein labeling methods that react non-specifically with various amino acid residues (e.g., lysines), our GlcNAc-type glycoprotein conjugation service utilizes highly specific bioorthogonal chemistry. This ensures precise, site-specific labeling on GlcNAc residues and preserves the protein's native functions and structure. This specificity is crucial for accurate biological studies.

Q3: What kind of data will I receive with my conjugated protein?

A3: Upon completion, you will receive a comprehensive project report detailing the experimental procedures, quality control data (e.g., mass spectrometry results verifying conjugation, SDS-PAGE images confirming purity), and characterization results. We ensure you have all the necessary information to confidently proceed with your downstream applications.

Customer Review

Providing Critical Insights
"The precision and efficiency of Creative Biolabs' GlcNAc conjugation service are unmatched. Using Creative Biolabs's N-acetylglucosamine (GlcNAc)-type glycoprotein conjugation service in our research has significantly improved our ability to track protein glycosylation dynamics in live cells, providing critical insights into signaling pathways." - Dr. R. N. Fa***r.

Facilitated the Development of Vaccine Candidates
"Creative Biolabs' team provided exceptional support throughout our project. Using Creative Biolabs's N-acetylglucosamine (GlcNAc)-type glycoprotein conjugation service in our research has significantly facilitated the development of novel glyco-vaccine candidates, offering a clear advantage over traditional methods due to its high specificity and yield." - Prof. K. L. An***e.

Reference

  1. Zhang, Xiu, and Yan Zhang. "Applications of azide-based bioorthogonal click chemistry in glycobiology." Molecules 18.6 (2013): 7145-7159. DOI: 10.3390/molecules18067145. Distributed under an Open Access license CC BY 3.0, without modification.

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