Glycophorin A
Glycophorin A - Related Videos
04:33
Real-Time Imaging of Macrophage Phagocytosis of IgG-Opsonized Red Blood Cells
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2025
This video demonstrates an assay to monitor independent macrophage-mediated red blood cell (RBC) phagocytosis events. Mouse immunoglobulin G (IgG)-opsonized human RBCs are incubated with mouse macrophages and observed under a confocal microscope. The RBCs are engulfed by macrophages via a phagocytic cup formation and targeted for lysosomal degradation.
09:28
A Microfluidic Device for Quantifying Bacterial Chemotaxis in Stable Concentration Gradients
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Cited by 7 •
2010
This protocol describes the development of a microfluidic device for investigating bacterial chemotaxis in stable concentration gradients of chemoeffectors.
07:34
Manipulation of Rhythmic Food Intake in Mice Using a Custom-Made Feeding System
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2022
Restricting the timing of food intake has emerged as a promising intervention to attenuate diet-induced metabolic diseases. This manuscript details the construction and use of an efficient system built in-house for measuring and manipulating rhythmic food intake in mice.
11:52
Enrichment of NK Cells from Human Blood with the RosetteSep Kit from StemCell Technologies
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Cited by 8 •
2007
Natural killer cells are a small population of lymphocytes. Here we show how to isolate these cells from human blood by negative selection, using a kit from StemCell Technologies. The cells obtained are viable and untouched by antibodies, and therefore ready to be used for a number of procedures.
15:06
Synthesis of an Intein-mediated Artificial Protein Hydrogel
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Cited by 2 •
2014
We present the synthesis of a split-intein-mediated protein hydrogel. The building blocks of this hydrogel are two protein copolymers each containing a subunit of a trimeric protein that serves as a crosslinker and one half of a split intein. Mixing of the two protein copolymers triggers an intein trans-splicing reaction, yielding a polypeptide unit that self-assembles into a hydrogel. This hydrogel is highly pH- and temperature-stable, compatible with organic solvents, and easily incorporates...
FAQs
The abundant sialic acid residues on its extracellular domain contribute a strong negative surface charge to erythrocytes. This charge is an important biophysical feature of the cell surface and can influence how the membrane participates in interactions with surrounding components. Studying this property helps researchers connect glycophorin A structure with the physical organization and behavior of red blood cells.
The membrane-spanning region anchors glycophorin A within the lipid bilayer and supports its organization with other membrane components. This positioning allows investigators to examine how an abundant transmembrane protein contributes to red blood cell membrane structure. Rather than acting only as a surface marker, the protein also provides a model for studying relationships between membrane proteins and the surrounding bilayer.
Molecular variants of Glycophorin A contribute to differences in MNS blood group antigens. Those differences are relevant when researchers study transfusion compatibility because antigen variation can affect how red blood cells are distinguished immunologically. The same molecular diversity also provides a system for investigating how changes in a host-cell surface protein influence recognition by other biological agents.
Because Glycophorin A is abundant and erythroid-specific, researchers can use its presence to distinguish red blood cells from other cell types in a sample. Detection of this marker supports identification and isolation workflows without relying only on general membrane properties. The resulting cell population can then be examined for membrane structure, antigen variation, or developmental state.
Changes in the presence of this erythroid-specific membrane protein provide a way to follow the development of cells along the erythroid lineage. Researchers can use Glycophorin A as an indicator when assessing whether a population contains erythroid cells during differentiation studies. This application links a defined membrane component to changes in cellular identity and developmental progression.
Malaria parasites must recognize and invade host cells, making red blood cell surface molecules relevant to studies of host-pathogen interaction. Glycophorin A offers a well-defined erythrocyte component for examining that recognition process. Investigators can also consider its molecular variants when asking whether differences in the host-cell surface affect parasite binding or invasion-related behavior.