Glycoprotein Purification
Glycoprotein Purification - Related Videos
03:59
Isolation and Purification of Recombinant Myelin Oligodendrocyte Glycoproteins
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2025
Source: Jain, R. W., et al. Simple and Efficient Production and Purification of Mouse Myelin Oligodendrocyte Glycoprotein for Experimental Autoimmune Encephalomyelitis Studies. J. Vis. Exp. (2016)This video demonstrates the isolation and purification of MOGtag, a recombinant Myelin Oligodendrocyte Glycoprotein (MOG) used in Experimental Autoimmune Encephalomyelitis (EAE) studies. The protocol involves bacterial lysis, sonication, centrifugation, and nickel affinity chromatography to obtain...
07:08
Efficient Mammalian Cell Expression and Single-step Purification of Extracellular Glycoproteins for Crystallization
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Cited by 5 •
2015
This is a quick, cost-efficient protocol for the production of secreted, glycosylated mammalian proteins and subsequent single-step purification with sufficient yields of homogenous protein for X-ray crystallography and other biophysical studies.
10:47
Simple and Efficient Production and Purification of Mouse Myelin Oligodendrocyte Glycoprotein for Experimental Autoimmune Encephalomyelitis Studies
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Cited by 12 •
2016
We describe a simple protocol using only basic lab equipment to generate and purify large quantities of a fusion protein that contains mouse Myelin Oligodendrocyte Glycoprotein. This protein can be used to induce experimental autoimmune encephalomyelitis driven by both T and B cells.
05:42
Using a Sandwich ELISA to Determine the Immunogenic Glycoprotein Content in a Vaccine
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2025
This video showcases an indirect enzyme-linked immunosorbent assay or ELISA sandwich immunocapture assay designed to assess immunogenic glycoprotein levels in vaccines. The assay plate, containing glycoprotein-specific antibodies, is incubated with serially diluted vaccine samples, including reference and test vaccines, followed by immunoassay to quantify glycoprotein content in the test vaccine.
01:21
Matrix Proteoglycans and Glycoproteins
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2023
Proteoglycans are extensively glycosylated proteins, commonly found in the extracellular matrix, interwoven with collagen fibers. Hyaline cartilage, the most common type of cartilage in the body, consists of short and dispersed collagen fibers associated with large amounts of proteoglycans. These proteoglycans have long negative charges that attract cations, which in turn attract water molecules. This influx of ions and water molecules swells up the proteoglycan like a water-soaked gel that can...
FAQs
Lectin affinity chromatography exploits selective recognition between a lectin and particular carbohydrate structures on glycoproteins. Molecules with compatible glycans bind to the chromatography medium, whereas others pass through or bind less effectively. This selectivity enriches glycoprotein subsets according to glycan composition rather than relying only on protein size or charge.
After glycan-based enrichment, ion-exchange chromatography separates molecules according to charge, while size-exclusion chromatography separates them according to molecular size. These mechanisms provide different forms of selectivity, so a later step can remove contaminants that co-purify during lectin binding. Combining them improves purity and supports more reliable structural and functional analyses.
Glycan composition matters because carbohydrate structure can influence how a glycoprotein is recognized during affinity purification and can also be related to its stability and activity. Examining purified material therefore connects an observed purification pattern with structural information, helping investigators study how glycans contribute to protein behavior.
A typical sequence begins with a complex biological sample, uses lectin affinity chromatography to enrich molecules bearing compatible carbohydrate structures, and then applies ion-exchange or size-exclusion chromatography to improve purity. The sequence moves from glycan-selective capture to broader physicochemical separation, producing material suitable for downstream structural and functional studies.
Purified glycoproteins can be used to characterize biomarkers and assess therapeutic proteins. Isolation provides material in which glycosylation patterns can be examined alongside protein properties, helping researchers evaluate whether carbohydrate features are associated with stability or activity. This makes purification a preparative step for both biological investigation and protein-focused assessment.
In biology, purified glycoproteins enable controlled study of cell recognition, signaling, immune responses, and host-pathogen interactions. Removing the complexity of the original sample helps investigators focus on the target molecule’s structural and functional properties. The resulting information can clarify how carbohydrate-bearing proteins participate in communication, defense, or interactions between organisms.