Annexin A2
Annexin A2 - Related Videos
09:09
Annexin V and Propidium Iodide Labeling
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2023
Staining with annexin V and propidium iodide (PI) provides researchers with a way to identify different types of cell death—either necrosis or apoptosis. This technique relies on two components. The first, annexin V, is a protein that binds certain phospholipids called phosphatidylserines, which normally occur only in the inner, cytoplasm-facing leaflet of a cell’s membrane, but become “flipped” to the outer leaflet during the early stages of apoptosis. The second component is the DNA-binding...
07:11
Dissipative Microgravimetry to Study the Binding Dynamics of the Phospholipid Binding Protein Annexin A2 to Solid-supported Lipid Bilayers Using a Quartz Resonator
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Cited by 5 •
2018
Here, we present an experimental protocol that can be employed to determine the binding affinities and mode of interaction of label-free phospholipid-binding protein annexin A2 with immobilized solid-supported bilayers (SLB) by simultaneously measuring the mass uptake and the viscoelastic properties of the protein annexin A2.
04:21
Annexin V Binding Assay: A Fluorescence-Based Technique to Identify Apoptotic Erythrocytes via Phosphatidylserine Labeling
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2025
In this video, we demonstrate the Annexin V binding assay to measure the degree of eryptosis, erythrocyte programmed cell death, using fluorescent Annexin V staining. Apoptotic erythrocytes demonstrate phosphatidylserine translocation from the inner to the outer leaflet of the cell membrane, causing the fluorophore-tagged Annexin V to bind to the translocated phosphatidylserine, thereby emitting a fluorescent signal.
07:34
Modified Annexin V/Propidium Iodide Apoptosis Assay For Accurate Assessment of Cell Death
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Cited by 543 •
2011
An accurate method for the assessment of cell death is described. The protocol improves upon conventional Annexin V/ propidium iodide (PI) protocols, which display up to 40% false- positive events in cell lines and primary cells from a broad range of animal models.
07:00
A Method to Study the C924T Polymorphism of the Thromboxane A2 Receptor Gene
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2019
In the present study, we describe a methodology to analyze the C924T genotype. The protocol consists of three phases: DNA extraction, amplification by polymerase chain reaction (PCR), and analysis of the restriction fragment length polymorphism (RFLP) on agarose gel.
FAQs
Calcium provides the condition required for Annexin A2’s annexin core to bind negatively charged phospholipids. This makes membrane association dependent on both the presence of calcium and the lipid character of the membrane. In experimental studies, these features help explain why Annexin A2 can organize membrane-associated processes rather than remaining uniformly distributed in the cell.
The N-terminal region provides a partner-binding interface that can associate with S100A10 and other proteins. Through these interactions, Annexin A2 connects membrane-associated activity with the actin cytoskeleton. Examining this region therefore adds information beyond protein abundance, helping researchers investigate how molecular partnerships support cell-surface organization and membrane-related processes.
Phospholipid binding identifies when Annexin A2 can associate with a membrane, whereas partner interactions indicate how that association may be organized or regulated within the cell. Considering both properties gives a broader view of its molecular behavior. This combined perspective is relevant to studies of membrane trafficking, cell-surface organization, and fibrinolytic activity.
Localization should be interpreted in relation to calcium-dependent membrane binding, the availability of negatively charged phospholipids, and interactions involving the N-terminal region. A detected signal can therefore reflect both membrane association and recruitment through binding partners. Comparing localization with protein abundance and interaction data helps distinguish where Annexin A2 is found from how it may function there.
Immunoblotting measures Annexin A2 protein abundance, while gene-expression analysis evaluates its expression at the gene level. These readouts address related but distinct questions and should not be treated as interchangeable. Using them together can show whether an observed change concerns expression, the amount of protein present, or both, strengthening interpretation in biological studies.
Immunofluorescence microscopy shows where Annexin A2 is localized within cells or at cell-associated structures. This spatial information complements abundance measurements from immunoblotting and can indicate whether the protein is associated with membranes or particular cellular regions. Researchers use the resulting localization patterns to examine cell-surface organization and membrane-associated processes.
Co-immunoprecipitation is useful when the research question concerns proteins associated with Annexin A2. It supports investigation of interactions involving S100A10 and other partners, complementing methods that measure abundance or localization. In broader studies of disease mechanisms and therapeutic targets, interaction data can help connect Annexin A2’s molecular associations with membrane organization or fibrinolytic activity.