anti cavin 1 antibody  (Addgene inc)

Journal: Neurobiology of disease

Article Title: Novel extracellular vesicle release pathway facilitated by toxic superoxide dismutase 1 oligomers

doi: 10.1016/j.nbd.2026.107309

Figure Lengend Snippet: Volcano plots display the distribution of differentially expressed genes in three conditions: (A) VAPB, blue circles, (B) VCP, pink circles, and (C) Stathmin-2, green circles. Genes with a ∣log 2 fold change∣ > 0.5 and p-value <0.05 were considered significantly differentially expressed. Significantly upregulated genes are shown in green, downregulated in orange, and non-significant genes in blue. Other proteins that were not significant hits in the mass-spectrometry data are shown with grey or orange (Caveolin-1 and Cavin-1) circles. Line darkness corresponds to the confidence in the known connections according to the string database.

Article Snippet: Cavin-1 , Cell Signaling , 69,036 T.

Techniques: Mass Spectrometry

Journal: Neurobiology of disease

Article Title: Novel extracellular vesicle release pathway facilitated by toxic superoxide dismutase 1 oligomers

doi: 10.1016/j.nbd.2026.107309

Figure Lengend Snippet: Proteins associated with distinct stages of EV biogenesis, membrane remodeling, and vesicle release were quantified on CD9+ EVs following incremental stabilization of trimeric SOD1. A) Twenty-two EV-related proteins were assessed using a sandwich ELISA to determine whether SOD1 trimer stabilization affects specific steps in EV formation or release. B) Only three proteins had significant changes with trimer stabilization and are presented as mean expression levels with individual replicates shown. RIM2 levels significantly decreased (p-value = 0.0006), while Caveolin-1 (p-value = 0.001) and Cavin-1 (p-value = 0.026) significantly increased with SOD1 trimer stabilization.

Article Snippet: Cavin-1 , Cell Signaling , 69,036 T.

Techniques: Membrane, Sandwich ELISA, Expressing

Journal: Neurobiology of disease

Article Title: Novel extracellular vesicle release pathway facilitated by toxic superoxide dismutase 1 oligomers

doi: 10.1016/j.nbd.2026.107309

Figure Lengend Snippet: Caveolin-1 oligomers increase with trimer stabilization (WT to A4V p-value = 0.039, WT to FH p-value =0.029), while Cavin-1 oligomers decrease with trimer stabilization (WT to A4V p-value = 0.036, WT to FH p-value =0.015). Caveolin-1 and Cavin-1 levels show a strong inverse correlation (Pearson's correlation coefficient r = −0.98, p = 0.021).

Article Snippet: Cavin-1 , Cell Signaling , 69,036 T.

Techniques:

Journal: bioRxiv

Article Title: Predictive and Experimental Motif Interaction Analysis Identifies Functions of the WNK-OSR1/SPAK Pathway

doi: 10.1101/2024.06.26.600905

Figure Lengend Snippet: (A-D) siRNA-mediated knockdown of WNK1 (72 hours) and inhibition with the pan-WNK inhibitor, WNK463 (18 hours, 1 µM), in human dermal microvascular endothelial cells (HDMEC). Data reported as mean ± SD (n=3). (E) 32P incorporation into MBP-Cavin1. MBP refers to affinity tag maltose binding protein. Following 15 min preincubation, ATP was added and Cavin1 (5 µM) phosphorylation was monitored in the presence of constitutively active SPAK 62-556 T243E (15 µM) and the SPAK allosteric activating protein Mo25/Cab39 (15 µM). 100 µM CCT blocking peptide (WNK1 1253-1265; NH 3 + -SAGRRFIVSPVPE-COO - ) was used to block the interaction between Cavin1 and SPAK. Phosphorylation reaction was run at varying NaCl concentrations for 10 minutes at 25 °C. Top panel is Coomassie stained gel and bottom two panels are 32P autoradiograms at different exposure times. MBP tag alone was used as a control (n=3). (F) Diagram indicating potential intramolecular interactions (dashed lines) between the acidic phospho-tyrosine 156 at the +5 position of the Cavin1 motif and multiple basic residues at the -4, -3, -2, and +1 positions. Such an interaction could potentially diminish the ability of CCT domains to interact with the motif. (G) Affinity determined by fluorescence anisotropy peptide competition assays. Unlabeled peptides were used to displace labeled peptide (NH 3 + -NLVGRF-[DAP-FAM]-VSPVPE-COO − ] [diaminopropionic acid (DAP)). Labeled peptide held constant at 25 nM, SPAK CCT and OSR1 CCT are constant at 1.5 μM and 3.0 μM, respectively. OSR1 CCT with Cavin1 peptide lacking p-Tyr156: solid red line; OSR1 CCT with p-Tyr156 Cavin1 peptide: dashed red line; SPAK CCT with Cavin1 peptide lacking p-Tyr156: solid blue line; SPAK CCT with p-Tyr156 Cavin1 peptide: dashed blue line. Higher line indicates weaker binding. Quantification unavailable due to instability of Cavin1 p-Tyr peptide at higher concentrations (n=3).

Article Snippet: Unless indicated elsewhere in methods antibodies were obtained from the following sources: WNK1, Cobb lab Q2561 ( ); Cavin1 #69036, OSR1 #3729, and GAPDH #97166L from Cell Signaling Technology (Beverly, MA, USA); phospho-SPAK Ser373 / phospho-OSR1 Ser325 07-2273 from Millipore Sigma (Darmstadt, Germany); phospho-Cavin1 Tyr156 PA5-99575 from Thermo Fisher Scientific (Waltham, MA, USA); Actin sc-8432 from Santa Cruz Biotechnology (Santa Cruz, CA, USA); TSC22D1 A303-582A from Bethyl Labs (Montgomery, TX, USA).

Techniques: Knockdown, Inhibition, Binding Assay, Phospho-proteomics, Blocking Assay, Staining, Control, Fluorescence, Labeling