Phospho-ser129 Antibody
Phospho-ser129 Antibody - Related Videos
10:52
Radiolabeling and Quantification of Cellular Levels of Phosphoinositides by High Performance Liquid Chromatography-coupled Flow Scintillation
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Cited by 21 •
2016
Phosphoinositides are signaling lipids whose relative abundance rapidly changes in response to various stimuli. This article describes a method to measure the abundance of phosphoinositides by metabolically labeling cells with 3H-myo-inositol, followed by extraction and deacylation. Extracted glycero-inositides are then separated by high-performance liquid chromatography and quantified by flow scintillation.
01:42
Phosphoinositides and PIPs
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2023
Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs. Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
10:58
PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions
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Cited by 7 •
2017
Here we present a supported lipid bilayer in the context of a microfluidic platform to study protein-phosphoinositide interactions using a label-free method based on pH modulation.
13:21
Antibody Generation: Producing Monoclonal Antibodies Using Hybridomas
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2023
Source: Frances V. Sjaastad1,2, Whitney Swanson2,3, and Thomas S. Griffith1,2,3,4 1 Microbiology, Immunology, and Cancer Biology Graduate Program, University of Minnesota, Minneapolis, MN 55455 2 Center for Immunology, University of Minnesota, Minneapolis, MN 55455 3 Department of Urology, University of Minnesota, Minneapolis, MN 55455 4 Masonic Cancer Center, University of Minnesota, Minneapolis, MN 55455 Polyclonal antibodies are defined as a collection of antibodies directed against...
01:10
Antibody Structure
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2019
Overview Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding. The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains Antibodies consist of four polypeptide chains: two identical heavy...
FAQs
Recognition depends on the antibody binding an epitope that contains serine 129 in its phosphorylated state. This phosphoserine-containing region gives the reagent selectivity for a modified form of α-synuclein rather than treating all α-synuclein species as equivalent. Assay conditions and antibody characteristics still influence how clearly that selective signal can be detected.
Phosphorylation at serine 129 identifies an α-synuclein form associated with pathological protein accumulation. Detecting this modification helps researchers examine where disease-associated protein deposits occur and how their presence changes across experimental settings. In medicine-focused research, that information connects molecular protein changes with Lewy body pathology and related synucleinopathies.
The observed signal depends on the biological material, assay format, antibody, and experimental conditions. Tissue sections, cultured cells, and protein assays present the target in different contexts, so detection may emphasize localization or protein-level measurement. Comparing results therefore requires attention to both the sample type and the method used to generate the signal.
The same target-specific reagent can support different experimental readouts. In immunohistochemistry, it helps examine modified α-synuclein in tissue sections; in immunofluorescence, it supports detection in cultured cells; and in immunoblotting, it is applied to protein assays. Selecting among these formats depends on whether the study emphasizes tissue distribution, cellular localization, or protein detection.
Researchers first choose a suitable sample and assay format, such as a tissue section, cultured-cell preparation, or protein assay. They then apply the antibody under conditions appropriate for that method and examine the resulting detection or localization signal. The workflow should remain aligned with the intended question, whether it concerns pathological distribution, cellular changes, or protein-level comparison.
Comparisons are useful when investigators want to evaluate differences in α-synuclein pathology among experimental disease models. Detection of the phosphorylated form can reveal variation in protein accumulation or clearance, helping researchers assess how models reproduce aspects of Lewy body or related synuclein pathology. Such comparisons also support evaluation of disease mechanisms and potential therapeutic effects.
Phospho-ser129 detection provides a way to track a disease-associated α-synuclein modification in research samples. In Parkinson’s disease and other synucleinopathies, these measurements can support studies of pathological accumulation, biomarker development, and therapeutic research. The resulting evidence is experimental and helps characterize disease-related protein changes rather than serving as a standalone clinical diagnosis.