heterologous epitope scaffold (ProSci Incorporated)

ProSci Incorporated heterologous epitope scaffold
Heterologous Epitope Scaffold, supplied by ProSci Incorporated, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/heterologous epitope scaffold/product/ProSci Incorporated
Average 93 stars, based on 1 article reviews

heterologous epitope scaffold - by Bioz Stars, 2026-05

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agarose conjugated pabs against caveolin 1 (Santa Cruz Biotechnology)

Santa Cruz Biotechnology agarose conjugated pabs against caveolin 1
$Cholesterol depletion of plasma membrane induces relocalization of <t>caveolin-1</t> and VEGFR-2. Serum-starved BAEC were incubated for 1 h in the presence of 10 mM CD and subjected to sucrose gradient sedimentation as described in “Material and Methods.” (A) Gradients were fractionated by collecting 1-ml fractions from the top, and 20 μl of each fraction was loaded onto polyacrylamide gels for the detection of caveolin-1. (B) Fractions corresponding to caveolae-enriched membranes (fractions 4 through 6) were diluted in Tris-HCl 10 mM (pH 7.5) and centrifuged at 100,000g. Membranes were resuspended in lysis buffer, and equal quantities of proteins were separated by SDS-PAGE electrophoresis.$
Agarose Conjugated Pabs Against Caveolin 1, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/agarose conjugated pabs against caveolin 1/product/Santa Cruz Biotechnology
Average 96 stars, based on 1 article reviews

agarose conjugated pabs against caveolin 1 - by Bioz Stars, 2026-05

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polyclonal caveolin 1 (Abcam)

Abcam polyclonal caveolin 1

Experimental protocol. Within 12 h of birth, litters of B6129SF2J mice were randomized to either room air (RA) or hyperoxia (50% O2) exposure with or without <t>caveolin-1</t> scaffolding domain (CSD) peptide treatment (10 µl of 0.25 mM CSD or PBS vehicle; intraperitoneal). After 7 days, all pups were allowed to recover for 14 days in RA before pulmonary function testing and tissue processing at 21 days of age. Thus, the four groups were RA/PBS, RA/CSD, O2/PBS, and O2/CSD. PND, postnatal day; AHR, airway hyperresponsiveness; LCM, laser capture microdissection.

Polyclonal Caveolin 1, supplied by Abcam, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/polyclonal caveolin 1/product/Abcam
Average 99 stars, based on 1 article reviews

polyclonal caveolin 1 - by Bioz Stars, 2026-05

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antibody rabbit α med26 proteintech 21 043 1 ap (Proteintech)

Proteintech antibody rabbit α med26 proteintech 21 043 1 ap

RSV Gag colocalized and co-immunoprecipitated with <t>Med26.</t> A Transfected RSV Gag-GFP (red) and FLAG-Med26 (green) colocalize (white) within QT6 cells. Image representative of average colocalization, as quantified in panel ( B ). Nuclei (blue) are outlined by a dotted white line, and regions boxed in the main images are enlarged below. White arrows are included to guide the eye. Scale bars = 2 µm. B Manders’ Overlap Coefficient values for image set represented by ( A ). Individual values are shown in addition mean ± SEM, n ≥ 17; ****, p < 0.0001 by unpaired two-tailed t-test. C 500 µg of RC.V8-infected QT6 nuclear lysates were incubated with an α-RSV Gag antibody (mouse α-RSV CA.A11, gift from Neil Christensen, Penn State College of Medicine), followed by antibody capture on Pierce™ Protein G Magnetic Beads. After extensive washing, proteins were eluted from beads by boiling in 1X SDS-PAGE sample buffer and run on a 10% SDS-PAGE gel, transferred to PVDF, and Western blotted first for Med26 (top) followed by RSV Gag (bottom). The position of molecular weight markers, in kilodaltons, are indicated on the left. FT, flow through; Beads, lysate only; Eluate, lysate plus antibody. Images representative of three independent experiments

Antibody Rabbit α Med26 Proteintech 21 043 1 Ap, supplied by Proteintech, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/antibody rabbit α med26 proteintech 21 043 1 ap/product/Proteintech
Average 92 stars, based on 1 article reviews

antibody rabbit α med26 proteintech 21 043 1 ap - by Bioz Stars, 2026-05

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caveolin-1 (Ushio)

Ushio caveolin-1

Caveolin 1, supplied by Ushio, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/caveolin-1/product/Ushio
Average 90 stars, based on 1 article reviews

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anti-hsv vp21/vp22a (CancerTools Org)

N/A

Herpes simplex virus (HSV) virions are multilayered, and their assembly requires several steps (reviewed in references 21 and 59). The double-stranded DNA viral genome is enclosed within a well-ordered protein capsid. A more amorphous layer

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hnrnpu antibody (ProSci Incorporated)

N/A

HNRNPU Antibody raised in Rabbit validated in WB,IF in Human, Rat.

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Image Search Results

$Cholesterol depletion of plasma membrane induces relocalization of caveolin-1 and VEGFR-2. Serum-starved BAEC were incubated for 1 h in the presence of 10 mM CD and subjected to sucrose gradient sedimentation as described in “Material and Methods.” (A) Gradients were fractionated by collecting 1-ml fractions from the top, and 20 μl of each fraction was loaded onto polyacrylamide gels for the detection of caveolin-1. (B) Fractions corresponding to caveolae-enriched membranes (fractions 4 through 6) were diluted in Tris-HCl 10 mM (pH 7.5) and centrifuged at 100,000g. Membranes were resuspended in lysis buffer, and equal quantities of proteins were separated by SDS-PAGE electrophoresis.$

Journal:

Article Title: Regulation of Vascular Endothelial Growth Factor Receptor-2 Activity by Caveolin-1 and Plasma Membrane Cholesterol

doi: 10.1091/mbc.E02-07-0379

Figure Lengend Snippet: Cholesterol depletion of plasma membrane induces relocalization of caveolin-1 and VEGFR-2. Serum-starved BAEC were incubated for 1 h in the presence of 10 mM CD and subjected to sucrose gradient sedimentation as described in “Material and Methods.” (A) Gradients were fractionated by collecting 1-ml fractions from the top, and 20 μl of each fraction was loaded onto polyacrylamide gels for the detection of caveolin-1. (B) Fractions corresponding to caveolae-enriched membranes (fractions 4 through 6) were diluted in Tris-HCl 10 mM (pH 7.5) and centrifuged at 100,000g. Membranes were resuspended in lysis buffer, and equal quantities of proteins were separated by SDS-PAGE electrophoresis.

Article Snippet: PAbs against neuropilin-1 (sc-7239), FAK (sc-557), RhoB (sc-180), pAbs N-998 (sc-505), and C-1158 (sc-504), directed against VEGFR-2, and agarose-conjugated pAbs against caveolin-1 (sc-894), VEGFR-2 (sc-504), and c-src (sc-19) were also purchased from Santa Cruz Biotechnology. mAbs against ACE and α v integrin, and pAb against β 3 integrin were from Chemicon International (Temecula, CA). mAbs against eNOS ( {"type":"entrez-nucleotide","attrs":{"text":"N30020","term_id":"1148540","term_text":"N30020"}} N30020 ), caveolin-1 ( {"type":"entrez-nucleotide","attrs":{"text":"C37120","term_id":"2373261","term_text":"C37120"}} C37120 ), paxillin ( {"type":"entrez-protein","attrs":{"text":"P13520","term_id":"6136282","term_text":"P13520"}} P13520 ), phosphocaveolin (P-Tyr 14 and {"type":"entrez-nucleotide","attrs":{"text":"C91520","term_id":"3060886","term_text":"C91520"}} C91520 ), and pAb against caveolin ( {"type":"entrez-nucleotide","attrs":{"text":"C13630","term_id":"1561183","term_text":"C13630"}} C13630 ) were from Transduction Laboratories (Lexington, KY). mAbs against Cbl (no. 05-44) and Src (no. 05-184) were from Upstate Biotechnology (Lake Placid, NY).

Techniques: Incubation, Sedimentation, Lysis, SDS Page, Electrophoresis

Cotransfection of VEGFR-2 and caveolin-1 in human embryonal kidney cells inhibits receptor autophosphorylation. 293T cells were transiently transfected with VEGFR-2 and caveolin-1 cDNAs, using the calcium phosphate precipitation procedure (Wigler et al., 1979 ). Forty-eight hours posttransfection, cells were serum-starved and lysed. (A) Caveolae membranes were purified using the hyperosmotic carbonate method (Song et al., 1996 ). Fractions were separated by SDS-PAGE electrophoresis, blotted, and tested for caveolin-1 or VEGFR-2, as indicated. (B and C) VEGFR-2 was immunoprecipitated from cell extracts (350 μg) and phosphorylation was monitored by immunoblotting with a monoclonal anti-Tyr(P) antibody. In C, cells were treated with 50 ng/ml VEGF for the periods indicated before lysis.

Journal:

Article Title: Regulation of Vascular Endothelial Growth Factor Receptor-2 Activity by Caveolin-1 and Plasma Membrane Cholesterol

doi: 10.1091/mbc.E02-07-0379

Figure Lengend Snippet: Cotransfection of VEGFR-2 and caveolin-1 in human embryonal kidney cells inhibits receptor autophosphorylation. 293T cells were transiently transfected with VEGFR-2 and caveolin-1 cDNAs, using the calcium phosphate precipitation procedure (Wigler et al., 1979 ). Forty-eight hours posttransfection, cells were serum-starved and lysed. (A) Caveolae membranes were purified using the hyperosmotic carbonate method (Song et al., 1996 ). Fractions were separated by SDS-PAGE electrophoresis, blotted, and tested for caveolin-1 or VEGFR-2, as indicated. (B and C) VEGFR-2 was immunoprecipitated from cell extracts (350 μg) and phosphorylation was monitored by immunoblotting with a monoclonal anti-Tyr(P) antibody. In C, cells were treated with 50 ng/ml VEGF for the periods indicated before lysis.

Techniques: Cotransfection, Transfection, Purification, SDS Page, Electrophoresis, Immunoprecipitation, Western Blot, Lysis

The caveolin-1 scaffolding domain inhibits the in vitro kinase activity of VEGFR-2. Immunoprecipitated VEGFR-2 from serum-starved BAEC was incubated for 1 h on ice in the presence of GST or GST-Caveolin-161–101 and submitted to an in vitro kinase assay in the presence of 5 μCi of ATP (γ-32P) (A) or in the presence of nonradioactive ATP at a final concentration of 1 mM (B). After 15 min at 30°C, reactions were stopped by the addition of fivefold concentrated sample buffer. After electrophoresis on 7.5% acrylamide/bis-acrylamide gels, the gels were exposed to Fuji films (A) or transferred onto PVDF and subjected to Western blotting (B).

Journal:

Article Title: Regulation of Vascular Endothelial Growth Factor Receptor-2 Activity by Caveolin-1 and Plasma Membrane Cholesterol

doi: 10.1091/mbc.E02-07-0379

Figure Lengend Snippet: The caveolin-1 scaffolding domain inhibits the in vitro kinase activity of VEGFR-2. Immunoprecipitated VEGFR-2 from serum-starved BAEC was incubated for 1 h on ice in the presence of GST or GST-Caveolin-161–101 and submitted to an in vitro kinase assay in the presence of 5 μCi of ATP (γ-32P) (A) or in the presence of nonradioactive ATP at a final concentration of 1 mM (B). After 15 min at 30°C, reactions were stopped by the addition of fivefold concentrated sample buffer. After electrophoresis on 7.5% acrylamide/bis-acrylamide gels, the gels were exposed to Fuji films (A) or transferred onto PVDF and subjected to Western blotting (B).

Techniques: Scaffolding, In Vitro, Activity Assay, Immunoprecipitation, Incubation, Kinase Assay, Concentration Assay, Electrophoresis, Western Blot

$VEGF induces dissociation of caveolin-1 from VEGFR-2. (A) BAEC were serum-starved overnight and incubated in the presence of 50 ng/ml VEGF for the indicated times. After a 1 h sodium orthovanadate treatment, cells were lysed (700 μg) and subjected to immunoprecipitation with agarose-conjugated anti-VEGFR-2. Associated caveolin-1 was observed by Western blotting using a specific mAb. (B) After VEGF stimulation, caveolae membranes were prepared and fractions corresponding to caveolae-enriched membranes were diluted and concentrated by ultracentrifugation. Equal quantities of proteins were used for immunoprecipitation assays. (C) Before VEGF-stimulation, cells were incubated for 1 h in the presence of 10 mM CD.$

Journal:

Article Title: Regulation of Vascular Endothelial Growth Factor Receptor-2 Activity by Caveolin-1 and Plasma Membrane Cholesterol

doi: 10.1091/mbc.E02-07-0379

Figure Lengend Snippet: VEGF induces dissociation of caveolin-1 from VEGFR-2. (A) BAEC were serum-starved overnight and incubated in the presence of 50 ng/ml VEGF for the indicated times. After a 1 h sodium orthovanadate treatment, cells were lysed (700 μg) and subjected to immunoprecipitation with agarose-conjugated anti-VEGFR-2. Associated caveolin-1 was observed by Western blotting using a specific mAb. (B) After VEGF stimulation, caveolae membranes were prepared and fractions corresponding to caveolae-enriched membranes were diluted and concentrated by ultracentrifugation. Equal quantities of proteins were used for immunoprecipitation assays. (C) Before VEGF-stimulation, cells were incubated for 1 h in the presence of 10 mM CD.

Techniques: Incubation, Immunoprecipitation, Western Blot

VEGF induces Src-dependent tyrosine phosphorylation of caveolin-1. (A) BAEC were serum-starved 18 h and incubated in the presence of 50 ng/ml VEGF for the indicated times. After a 1-h sodium orthovanadate treatment, cells were lysed and subjected to immunoprecipitation with agarose-conjugated anti-caveolin-1 (350 μg of cell lysate) or anti-VEGFR-2 (200 μg). Incubation of BAEC was also performed before VEGF stimulation in the presence of 10 mM CD (B) or 10 μM PP2 (C). Phosphorylation was monitored by Western blotting using a specific anti-Tyr(P) mAb.

Journal:

Article Title: Regulation of Vascular Endothelial Growth Factor Receptor-2 Activity by Caveolin-1 and Plasma Membrane Cholesterol

doi: 10.1091/mbc.E02-07-0379

Figure Lengend Snippet: VEGF induces Src-dependent tyrosine phosphorylation of caveolin-1. (A) BAEC were serum-starved 18 h and incubated in the presence of 50 ng/ml VEGF for the indicated times. After a 1-h sodium orthovanadate treatment, cells were lysed and subjected to immunoprecipitation with agarose-conjugated anti-caveolin-1 (350 μg of cell lysate) or anti-VEGFR-2 (200 μg). Incubation of BAEC was also performed before VEGF stimulation in the presence of 10 mM CD (B) or 10 μM PP2 (C). Phosphorylation was monitored by Western blotting using a specific anti-Tyr(P) mAb.

Techniques: Incubation, Immunoprecipitation, Western Blot

VEGF induces association of Src to caveolin-1. BAEC were serum-starved overnight and incubated in the presence of 50 ng/ml VEGF for the indicated times. After a 1-h sodium orthovanadate treatment, cells were lysed (700 μg) and subjected to immunoprecipitation with agarose-conjugated anti-caveolin-1. Associated caveolin-1 was observed by Western-blotting with a specific mAb. (B) After lysis, Src was immunoprecipitated and Western blotted using a specific antibody against the form of Src phosphorylated on tyrosine 527.

Journal:

Article Title: Regulation of Vascular Endothelial Growth Factor Receptor-2 Activity by Caveolin-1 and Plasma Membrane Cholesterol

doi: 10.1091/mbc.E02-07-0379

Figure Lengend Snippet: VEGF induces association of Src to caveolin-1. BAEC were serum-starved overnight and incubated in the presence of 50 ng/ml VEGF for the indicated times. After a 1-h sodium orthovanadate treatment, cells were lysed (700 μg) and subjected to immunoprecipitation with agarose-conjugated anti-caveolin-1. Associated caveolin-1 was observed by Western-blotting with a specific mAb. (B) After lysis, Src was immunoprecipitated and Western blotted using a specific antibody against the form of Src phosphorylated on tyrosine 527.

Techniques: Incubation, Immunoprecipitation, Western Blot, Lysis

Journal: American Journal of Physiology - Lung Cellular and Molecular Physiology

Article Title: Caveolin-1 scaffolding domain peptide prevents hyperoxia-induced airway remodeling in a neonatal mouse model

doi: 10.1152/ajplung.00111.2018

Figure Lengend Snippet: Experimental protocol. Within 12 h of birth, litters of B6129SF2J mice were randomized to either room air (RA) or hyperoxia (50% O2) exposure with or without caveolin-1 scaffolding domain (CSD) peptide treatment (10 µl of 0.25 mM CSD or PBS vehicle; intraperitoneal). After 7 days, all pups were allowed to recover for 14 days in RA before pulmonary function testing and tissue processing at 21 days of age. Thus, the four groups were RA/PBS, RA/CSD, O2/PBS, and O2/CSD. PND, postnatal day; AHR, airway hyperresponsiveness; LCM, laser capture microdissection.

Article Snippet: Samples were blocked in 4% normal donkey serum with 0.3% Triton Tris-buffered saline (TBS) for 30 min before overnight incubation in TBS (for unstained control) of 1 μg/ml monoclonal anti-α-smooth muscle actin (A2547; Sigma-Aldrich, St. Louis, MO), polyclonal caveolin-1 (AB18199; Abcam, Cambridge, MA), polyclonal cavin-1 (NB100-60635; Novus, Littleton, CO), polyclonal cavin-3 (AB76676; Abcam), or polyclonal fibronectin (AB2413; Abcam) primary antibodies.

Techniques: Scaffolding, Laser Capture Microdissection

Pulmonary resistance and compliance with methacholine dose response. A: O2/PBS exposed mice demonstrated increased pulmonary resistance (RL) at 21 days compared with room air (RA)/PBS control (*P < 0.05). Mice in the O2/caveolin-1 scaffolding domain (CSD) group had significantly decreased pulmonary resistance compared with O2/PBS mice (#P < 0.05). There was no difference noted between the RA/PBS, RA/CSD, and O2/CSD groups. B: O2/PBS mice had significantly lower compliance (CL) than RA/PBS (*P < 0.05). O2/CSD mice had a significantly higher compliance than O2/PBS mice (#P < 0.05). There was no difference in compliance noted between the RA/PBS, RA/CSD, and O2/CSD groups (P < 0.05). C: Newtonian resistance (RN) as a measurement of resistance of the central and conducting airways demonstrated a significant increase in RN in the O2/PBS group compared with RA/PBS control (*P < 0.05) while O2/CSD mice had a significant decrease in RN in comparison to O2/PBS mice (#P < 0.05). D: there was no significant difference in inspiratory capacity when normalized to body weight (BW) between treatment groups. Data are presented as means ± SE; n = 7–11 pups in each group. Two-way ANOVA with Tukey’s multiple comparison test was used for statistical analysis.

Journal: American Journal of Physiology - Lung Cellular and Molecular Physiology

Article Title: Caveolin-1 scaffolding domain peptide prevents hyperoxia-induced airway remodeling in a neonatal mouse model

doi: 10.1152/ajplung.00111.2018

Figure Lengend Snippet: Pulmonary resistance and compliance with methacholine dose response. A: O2/PBS exposed mice demonstrated increased pulmonary resistance (RL) at 21 days compared with room air (RA)/PBS control (*P < 0.05). Mice in the O2/caveolin-1 scaffolding domain (CSD) group had significantly decreased pulmonary resistance compared with O2/PBS mice (#P < 0.05). There was no difference noted between the RA/PBS, RA/CSD, and O2/CSD groups. B: O2/PBS mice had significantly lower compliance (CL) than RA/PBS (*P < 0.05). O2/CSD mice had a significantly higher compliance than O2/PBS mice (#P < 0.05). There was no difference in compliance noted between the RA/PBS, RA/CSD, and O2/CSD groups (P < 0.05). C: Newtonian resistance (RN) as a measurement of resistance of the central and conducting airways demonstrated a significant increase in RN in the O2/PBS group compared with RA/PBS control (*P < 0.05) while O2/CSD mice had a significant decrease in RN in comparison to O2/PBS mice (#P < 0.05). D: there was no significant difference in inspiratory capacity when normalized to body weight (BW) between treatment groups. Data are presented as means ± SE; n = 7–11 pups in each group. Two-way ANOVA with Tukey’s multiple comparison test was used for statistical analysis.

Techniques: Scaffolding

Caveolin-1 scaffolding domain (CSD) prevents hyperoxia-induced increase in airway thickness. A: O2/PBS exposure resulted in airway wall thickening characterized by a thicker airway smooth muscle (ASM) layer by hematoxylin and eosin staining. B: quantitative analysis showed significant increase in ASM thickness/airway diameter when compared with room air (RA)/PBS mice (*P < 0.05). CSD treatment abrogated these remodeling changes, resulting in a significant decrease in airway thickness/airway diameter in O2/CSD mice when compared with O2/PBS mice (#P < 0.05). C and D: average airway epithelial thickness/airway diameter and epithelial metaplasia (expressed as DAPI count) showed no significant difference between treatment groups. Data are presented as means ± SE; n = 6–8 in each group. One-way ANOVA with Tukey’s multiple comparisons test was used for statistical analysis.

Journal: American Journal of Physiology - Lung Cellular and Molecular Physiology

Article Title: Caveolin-1 scaffolding domain peptide prevents hyperoxia-induced airway remodeling in a neonatal mouse model

doi: 10.1152/ajplung.00111.2018

Figure Lengend Snippet: Caveolin-1 scaffolding domain (CSD) prevents hyperoxia-induced increase in airway thickness. A: O2/PBS exposure resulted in airway wall thickening characterized by a thicker airway smooth muscle (ASM) layer by hematoxylin and eosin staining. B: quantitative analysis showed significant increase in ASM thickness/airway diameter when compared with room air (RA)/PBS mice (*P < 0.05). CSD treatment abrogated these remodeling changes, resulting in a significant decrease in airway thickness/airway diameter in O2/CSD mice when compared with O2/PBS mice (#P < 0.05). C and D: average airway epithelial thickness/airway diameter and epithelial metaplasia (expressed as DAPI count) showed no significant difference between treatment groups. Data are presented as means ± SE; n = 6–8 in each group. One-way ANOVA with Tukey’s multiple comparisons test was used for statistical analysis.

Techniques: Scaffolding, Staining

Caveolin-1 scaffolding domain (CSD) reduces extracellular matrix deposition in hyperoxia-treated mice. A: Masson trichome staining showed greater collagen staining in the airways of 21-day-old O2/PBS mice, which was reduced by CSD. B: assessment of fibronectin deposition in immunohistochemically stained sections showed that compared with room air (RA)/PBS mice, O2/PBS mice have significantly greater fibronectin deposition (*P < 0.05). This increase was substantially reduced by treatment with CSD (#P < 0.05); n = 5–6 in each group. One-way ANOVA was performed for statistical analysis. RFU, relative fluorescence units.

Journal: American Journal of Physiology - Lung Cellular and Molecular Physiology

Article Title: Caveolin-1 scaffolding domain peptide prevents hyperoxia-induced airway remodeling in a neonatal mouse model

doi: 10.1152/ajplung.00111.2018

Figure Lengend Snippet: Caveolin-1 scaffolding domain (CSD) reduces extracellular matrix deposition in hyperoxia-treated mice. A: Masson trichome staining showed greater collagen staining in the airways of 21-day-old O2/PBS mice, which was reduced by CSD. B: assessment of fibronectin deposition in immunohistochemically stained sections showed that compared with room air (RA)/PBS mice, O2/PBS mice have significantly greater fibronectin deposition (*P < 0.05). This increase was substantially reduced by treatment with CSD (#P < 0.05); n = 5–6 in each group. One-way ANOVA was performed for statistical analysis. RFU, relative fluorescence units.

Techniques: Scaffolding, Staining, Fluorescence

Caveolin-1 scaffolding domain (CSD) attenuates hyperoxia-mediated increase in airway α smooth muscle actin area. A: imaging of immunofluorescently tagged smooth muscle actin demonstrated increased area in O2/PBS mice at 21 days. B: O2/PBS smooth muscle actin expression was significantly increased from room air (RA)/PBS control (*P < 0.05). CSD-abrogated hyperoxia-mediated increase and O2/CSD airways showed significantly less smooth muscle actin expression than O2/PBS airways (#P < 0.05). There were no significant differences between RA/PBS, RA/CSD, and O2/CSD groups. Data are presented as means ± SE; n = 6–9 in each group. One-way ANOVA with Tukey’s multiple comparisons test was used for statistical analysis. AU, arbitrary units.

Journal: American Journal of Physiology - Lung Cellular and Molecular Physiology

Article Title: Caveolin-1 scaffolding domain peptide prevents hyperoxia-induced airway remodeling in a neonatal mouse model

doi: 10.1152/ajplung.00111.2018

Figure Lengend Snippet: Caveolin-1 scaffolding domain (CSD) attenuates hyperoxia-mediated increase in airway α smooth muscle actin area. A: imaging of immunofluorescently tagged smooth muscle actin demonstrated increased area in O2/PBS mice at 21 days. B: O2/PBS smooth muscle actin expression was significantly increased from room air (RA)/PBS control (*P < 0.05). CSD-abrogated hyperoxia-mediated increase and O2/CSD airways showed significantly less smooth muscle actin expression than O2/PBS airways (#P < 0.05). There were no significant differences between RA/PBS, RA/CSD, and O2/CSD groups. Data are presented as means ± SE; n = 6–9 in each group. One-way ANOVA with Tukey’s multiple comparisons test was used for statistical analysis. AU, arbitrary units.

Techniques: Scaffolding, Imaging, Expressing

Airway smooth muscle (ASM) mRNA expression of caveolar proteins with hyperoxia exposure. mRNA expression changes were assessed in ASM isolated using laser capture microdissection. A: caveolin-1 expression was significantly reduced in all treatment groups in comparison to RA/PBS (*P < 0.05). B and C: while O2/PBS significantly decreased cavin-1 (*P < 0.05; B), O2/PBS treatment significantly increased cavin-3 (*P < 0.05; C): the effect was alleviated in O2/caveolin-1 scaffolding domain (CSD) animals (#P < 0.05). Data are presented as means ± SE; n = 8–14 pups per group. One-way ANOVA with Tukey’s multiple comparisons test was used for data analysis. FC, fold change.

Journal: American Journal of Physiology - Lung Cellular and Molecular Physiology

Article Title: Caveolin-1 scaffolding domain peptide prevents hyperoxia-induced airway remodeling in a neonatal mouse model

doi: 10.1152/ajplung.00111.2018

Figure Lengend Snippet: Airway smooth muscle (ASM) mRNA expression of caveolar proteins with hyperoxia exposure. mRNA expression changes were assessed in ASM isolated using laser capture microdissection. A: caveolin-1 expression was significantly reduced in all treatment groups in comparison to RA/PBS (*P < 0.05). B and C: while O2/PBS significantly decreased cavin-1 (*P < 0.05; B), O2/PBS treatment significantly increased cavin-3 (*P < 0.05; C): the effect was alleviated in O2/caveolin-1 scaffolding domain (CSD) animals (#P < 0.05). Data are presented as means ± SE; n = 8–14 pups per group. One-way ANOVA with Tukey’s multiple comparisons test was used for data analysis. FC, fold change.

Techniques: Expressing, Isolation, Laser Capture Microdissection, Scaffolding

Caveolin-1 (CAV1) and cavin-1 and -3 protein expression changes with hyperoxia exposure. Changes in protein expression were assessed in tissue samples using semiquantitative immunofluorescence with normalization to airway diameter. A: O2/PBS significantly decreased CAV1 expression (*P < 0.05) while O2/caveolin-1 scaffolding domain (CSD) reversed this effect (#P < 0.05). B: while cavin-1 did not change with O2/PBS, CSD did increase cavin-1 in both RA (*P < 0.05) and O2 (#P < 0.05) subgroups. C: cavin-3 expression also showed a pattern similar to cavin-1 (*P < 0.05). Data are presented as means ± SE; n = 5–9 pups per group. Data were analyzed using one-way ANOVA with Tukey’s multiple comparisons test.

Journal: American Journal of Physiology - Lung Cellular and Molecular Physiology

Article Title: Caveolin-1 scaffolding domain peptide prevents hyperoxia-induced airway remodeling in a neonatal mouse model

doi: 10.1152/ajplung.00111.2018

Figure Lengend Snippet: Caveolin-1 (CAV1) and cavin-1 and -3 protein expression changes with hyperoxia exposure. Changes in protein expression were assessed in tissue samples using semiquantitative immunofluorescence with normalization to airway diameter. A: O2/PBS significantly decreased CAV1 expression (*P < 0.05) while O2/caveolin-1 scaffolding domain (CSD) reversed this effect (#P < 0.05). B: while cavin-1 did not change with O2/PBS, CSD did increase cavin-1 in both RA (*P < 0.05) and O2 (#P < 0.05) subgroups. C: cavin-3 expression also showed a pattern similar to cavin-1 (*P < 0.05). Data are presented as means ± SE; n = 5–9 pups per group. Data were analyzed using one-way ANOVA with Tukey’s multiple comparisons test.

Techniques: Expressing, Immunofluorescence, Scaffolding

RSV Gag colocalized and co-immunoprecipitated with Med26. A Transfected RSV Gag-GFP (red) and FLAG-Med26 (green) colocalize (white) within QT6 cells. Image representative of average colocalization, as quantified in panel ( B ). Nuclei (blue) are outlined by a dotted white line, and regions boxed in the main images are enlarged below. White arrows are included to guide the eye. Scale bars = 2 µm. B Manders’ Overlap Coefficient values for image set represented by ( A ). Individual values are shown in addition mean ± SEM, n ≥ 17; ****, p < 0.0001 by unpaired two-tailed t-test. C 500 µg of RC.V8-infected QT6 nuclear lysates were incubated with an α-RSV Gag antibody (mouse α-RSV CA.A11, gift from Neil Christensen, Penn State College of Medicine), followed by antibody capture on Pierce™ Protein G Magnetic Beads. After extensive washing, proteins were eluted from beads by boiling in 1X SDS-PAGE sample buffer and run on a 10% SDS-PAGE gel, transferred to PVDF, and Western blotted first for Med26 (top) followed by RSV Gag (bottom). The position of molecular weight markers, in kilodaltons, are indicated on the left. FT, flow through; Beads, lysate only; Eluate, lysate plus antibody. Images representative of three independent experiments

Journal: Retrovirology

Article Title: Comparative analysis of retroviral Gag-host cell interactions: focus on the nuclear interactome

doi: 10.1186/s12977-024-00645-y

Figure Lengend Snippet: RSV Gag colocalized and co-immunoprecipitated with Med26. A Transfected RSV Gag-GFP (red) and FLAG-Med26 (green) colocalize (white) within QT6 cells. Image representative of average colocalization, as quantified in panel ( B ). Nuclei (blue) are outlined by a dotted white line, and regions boxed in the main images are enlarged below. White arrows are included to guide the eye. Scale bars = 2 µm. B Manders’ Overlap Coefficient values for image set represented by ( A ). Individual values are shown in addition mean ± SEM, n ≥ 17; ****, p < 0.0001 by unpaired two-tailed t-test. C 500 µg of RC.V8-infected QT6 nuclear lysates were incubated with an α-RSV Gag antibody (mouse α-RSV CA.A11, gift from Neil Christensen, Penn State College of Medicine), followed by antibody capture on Pierce™ Protein G Magnetic Beads. After extensive washing, proteins were eluted from beads by boiling in 1X SDS-PAGE sample buffer and run on a 10% SDS-PAGE gel, transferred to PVDF, and Western blotted first for Med26 (top) followed by RSV Gag (bottom). The position of molecular weight markers, in kilodaltons, are indicated on the left. FT, flow through; Beads, lysate only; Eluate, lysate plus antibody. Images representative of three independent experiments

Article Snippet: Samples were run on 10% SDS-PAGE gels, transferred to PVDF, blocked for 30 min with 5% Milk/0.1% TBS-Tween, and then incubated with primary antibody (rabbit α-Med26, Proteintech, 21,043–1-AP) in 0.5% Milk/0.1% TBS-Tween at 4 °C with rocking overnight.

Techniques: Immunoprecipitation, Transfection, Two Tailed Test, Infection, Incubation, Magnetic Beads, SDS Page, Western Blot, Molecular Weight

Names and functions of the 57 cellular proteins identified in both the RSV and HIV-1 Gag protein interactomes

Journal: Retrovirology

Article Title: Comparative analysis of retroviral Gag-host cell interactions: focus on the nuclear interactome

doi: 10.1186/s12977-024-00645-y

Figure Lengend Snippet: Names and functions of the 57 cellular proteins identified in both the RSV and HIV-1 Gag protein interactomes

Techniques: Binding Assay, Membrane, Expressing, Cell Differentiation, Methylation, Modification, Migration, Activation Assay, Infection, Sequencing, Scaffolding, Inhibition, Activity Assay, Residue, Functional Assay, Translocation Assay, Alternative Splicing, RNA Binding Assay, Control, Selection

Proteins identified in the present HIV-1 Gag affinity purification and found in at least one of the previously published HIV-1 Gag proteomic publications

Journal: Retrovirology

Article Title: Comparative analysis of retroviral Gag-host cell interactions: focus on the nuclear interactome

doi: 10.1186/s12977-024-00645-y

Figure Lengend Snippet: Proteins identified in the present HIV-1 Gag affinity purification and found in at least one of the previously published HIV-1 Gag proteomic publications

Techniques: Affinity Purification, Binding Assay, RNA Binding Assay, Sequencing, Protein Binding, Marker, Derivative Assay, Transformation Assay

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