flotillin (Novus Biologicals)
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92
Structured Review
Novus Biologicals
flotillin
Flotillin, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 92/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/flotillin+1/Flotillin-1+Antibody/pmc13088877-126-21-28
Average 92 stars, based on 8 article reviews
Flotillin, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 92/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/flotillin+1/Flotillin-1+Antibody/pmc13088877-126-21-28
Average 92 stars, based on 8 article reviews
flotillin - by Bioz Stars,
2026-09
92/100 stars
Images
1) Product Images from "Dysregulation of Extracellular Vesicle Concentration, MicroRNAs, and Surface Proteins in Patients With Niemann‐Pick Disease Type C"
Article Title: Dysregulation of Extracellular Vesicle Concentration, MicroRNAs, and Surface Proteins in Patients With Niemann‐Pick Disease Type C
Journal: Journal of Extracellular Biology
doi: 10.1002/jex2.70136
Figure Legend Snippet: SEC enriches for EVs from fibroblast conditioned media . ( A ) EV enrichment method for fibroblast conditioned media. ( B, C ) Immunoblots of individual ( B ) or pooled ( C ) SEC fractions from CTL fibroblast media show enrichment for EV proteins Flotillin‐1, CD63, and CD81, without detectable levels of other proteins (total protein stain) or cell lysate protein GM130. ( D ) MRPS histogram shows the distribution of particles in pooled EV fractions isolated from CTL fibroblast media. Mean particle count, size, and coefficient of variation are listed.
Techniques Used: Western Blot, Staining, Isolation
Figure Legend Snippet: SEC enriches for EVs from human CSF . ( A ) EV enrichment method for CSF. ( B, C ) Immunoblots of individual ( B ) or pooled ( C ) SEC fractions from CTL CSF show enrichment for EV proteins Flotillin‐1 and CD81 without detectable levels of bulk CSF proteins (total protein stain, albumin, ApoA1). ( D ) MRPS histogram shows the distribution of particles in pooled EV fractions from CTL CSF. Mean particle count, size, and coefficient of variation are listed. ( E ) TEM of representative NPC CSF EV sample. Black arrows indicate particles of ∼100 nm; white arrows indicate particles of ∼50 nm.
Techniques Used: Western Blot, Staining
Related Articles
Incubation:Article Title: Detection of circulating KRAS mutant DNA in extracellular vesicles using droplet digital PCR in patients with colon cancer. Article Snippet: Denatured proteins were mixed with NuPAGE LDS Sample Buffer (Invitrogen, Waltham, MA, USA) and b-mercaptoethanol, and then heated at 95°C for 5 min. Proteins were electrophoresed on Bolt Bis-Tris Plus gels (Invitrogen) and electroblotted onto polyvinylidene difluoride (PVDF) membranes. .. The membranes were blocked and incubated overnight at 4°C with the following primary antibodies: Recombinant:Article Title: Screening for Interacting Proteins with Peptide Biomarker of Blood–Brain Barrier Alteration under Inflammatory Conditions Article Snippet: .. The commercial recombinant proteins tested include fibronectin (ACFP4305B, R&D systems, Minneapolis, MN, USA), laminin α5 (H00003911-Q01, Novus Biologicals, Centennial, CO, USA), laminin β1 (NBP2-42385PEP, Novus Biologicals, Centennial, CO, USA), and Negative Control:Article Title: Screening for Interacting Proteins with Peptide Biomarker of Blood–Brain Barrier Alteration under Inflammatory Conditions Article Snippet: .. The commercial recombinant proteins tested include fibronectin (ACFP4305B, R&D systems, Minneapolis, MN, USA), laminin α5 (H00003911-Q01, Novus Biologicals, Centennial, CO, USA), laminin β1 (NBP2-42385PEP, Novus Biologicals, Centennial, CO, USA), and |
![N-linked glycosylation of NS3/NS3A facilitates its raft-enriched membrane association and efficient BTV release. ( A ) Representative confocal images of HeLa cells transfected with NS3/NS3A WT or the N150Q mutant. Cells were fixed and stained 20 h post-transfection. NS3/NS3A was detected using anti-NS3/NS3A (red), and lipid raft-enriched membrane domains were <t>labeled</t> <t>with</t> <t>anti-flotillin-1</t> (green). Scale bars, 5 μm. ( B and C ) Confocal images of HeLa cells expressing NS3/NS3A treated with trifluoperazine (TFP) ( B ) or methyl-β-cyclodextrin (MβCD) ( C ). Cells were fixed and stained 20 h post-transfection. NS3/NS3A is shown in red and flotillin-1 in green. Fluorescence intensity profiles were analyzed along the indicated line scans. Scale bars, 5 μm. ( D ) Localization of NS3/NS3A at the plasma membrane of HeLa cells with or without MβCD or TFP treatment. The plasma membrane was stained using WGA-Alexa Fluor 488 (green), and NS3/NS3A was visualized in red. Scale bars, 5 μm. ( E ) Quantification of plasma membrane (PM) localization from panel D, shown as the ratio of PM-associated NS3/NS3A fluorescence intensity (defined by WGA staining) to total cellular NS3/NS3A intensity. Values were normalized to vehicle-treated controls and are presented as mean ± SD. Statistical analysis was performed using one-way ANOVA with Dunnett’s multiple comparisons test (** P < 0.01, **** P < 0.0001). ( F ) MDOK or HEK-293T cells were infected with BTV-20 WT or BTV-20 N150Q at an MOI of 5. At 6 h post-infection, the cells were treated with MβCD or TFP, and viral titers were determined at 12 h post-infection. Data represent mean ± SD ( n = 3 biological replicates). Statistical significance was determined by two-way ANOVA with Šídák’s multiple comparisons test (ns, not significant; *** P < 0.001; **** P < 0.0001). ( G ) Analysis of BTV-20 release efficiency following raft disruption. MDOK cells were infected with BTV-20 (MOI = 5) and then treated with MβCD or TFP. Extracellular and intracellular viral titers were determined at the indicated time points. Release efficiency was calculated as [extracellular titer/(extracellular + intracellular titer)] × 100%. Data are presented as mean ± SD ( n = 3 biological replicates). Statistical significance was determined using two-way ANOVA with Šídák’s multiple comparisons test (ns, not significant; * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001). ( H ) A total of 1,136 host proteins were identified by quantitative proteomics, of which 102 proteins were enriched in the NS3/NS3A WT interactome relative to the N150Q mutant (log₂ FC > 4 or unique to WT). Highlighted are the top eight candidates. ( I ) Gene Ontology (GO) enrichment analysis of proteins enriched in the NS3/NS3A WT interactome. Significantly overrepresented terms are shown for the biological process, cellular component, and molecular function categories. Bars represent −log₁₀ ( P value). ( J ) Sucrose gradient fractionation followed by immunoblotting of lysates from transfected HEK-293T cells, or from infected MDOK cells. DRM (raft-enriched) fractions correspond to fractions 5–12, whereas detergent-soluble membrane (DSM) fractions correspond to fractions 13–20. ( K ) Co-immunoprecipitation analysis of NS3/NS3A WT , NS3/NS3A N150Q , and FLNA. Cells were transfected with NS3/NS3A variants, followed by Co-IP.](https://pub-med-central-images-cdn.bioz.com/pub_med_central_ids_ending_with_1428/pmc13011428/pmc13011428__jvi.02144-25.f005.jpg)