Rab5 Rab9 Lamp1

Rab5, Rab9, and LAMP1 are molecular markers used to identify distinct compartments in the endosomal and lysosomal system, making them important for studying intracellular membrane trafficking. Rab5 is associated with early endosomes, Rab9 regulates transport from late endosomes toward the trans-Golgi network, and LAMP1 is a major lysosomal membrane glycoprotein; together, their localization reflects the progression and organization of cargo-processing pathways. In biology, researchers use these proteins in fluorescence microscopy, immunostaining, and colocalization analyses to characterize organelle identity, endosome maturation, lysosome formation, and defects in vesicular transport linked to cellular disease.

Rab5 Rab9 Lamp1 - Related Videos

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JoVE Journal - Biology
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Assessing Autophagic Flux by Measuring LC3, p62, and LAMP1 Co-localization Using Multispectral Imaging Flow Cytometry

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Cited by 94 •

2017

Here, multispectral imaging flow cytometry with an analytical feature that compares bright detail images of 3 autophagy markers and quantifies their co-localization, along with LC3 spot counting, was used to measure autophagy in an objective, quantitative, and statistically robust manner.

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JoVE EoE - Immunodiagnostics

Assessment of Intracellular Growth of Coxiella Mutants within Eukaryotic Cells

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2025

This video demonstrates a method for assessing the intracellular growth of GFP-tagged Coxiella mutants within cultured epithelial cells. The mutant phenotype is visualized using immunostaining and epifluorescence microscopy, allowing the study of the effect of the mutation on intracellular growth.

Nitrogen Cavitation and Differential Centrifugation Allows for Monitoring the Distribution of Peripheral Membrane Proteins in Cultured Cells

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Cited by 15 •

2017

Here we present protocols for detergent-free homogenization of cultured mammalian cells based on nitrogen cavitation and subsequent separation of cytosolic and membrane-bound proteins by ultracentrifugation. This method is ideal for monitoring the partitioning of peripheral membrane proteins between soluble and membrane fractions.

In Vitro Polymerization of F-actin on Early Endosomes

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Cited by 3 •

2017

Early endosome functions depend on F-actin polymerization. Here, we describe a microscopy-based in vitro assay that reconstitutes the nucleation and polymerization of F-actin on early endosomal membranes in test tubes, thus rendering this complex series of reactions amenable to biochemical and genetic manipulations.

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