vectashield mounting medium  (Vector Laboratories)


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    Name:
    VECTASHIELD Antifade Mounting Medium
    Description:
    VECTASHIELD Antifade Mounting Medium is a unique stable formula for preserving fluorescence VECTASHIELD Mounting Medium prevents rapid photobleaching of fluorescent proteins and fluorescent dyes Features Inhibits photobleaching of dyes and fluorescent proteins Ideal refractive index Ready to use Offered with nuclear or cytoskeletal counterstains Available in non hardening or hardening formulations No warming necessary Can be stored without sealing for long term analysis Easy to useThe original VECTASHIELD Mounting Medium does not solidify but remains a liquid on the slide and can be stored without sealing If desired coverslips can be sealed around the perimeter with nail polish or a plastic sealant Mounted slides should be stored at 4 °C protected from light
    Catalog Number:
    H-1000
    Price:
    None
    Category:
    Histology reagents or solutions or stains
    Size:
    10 ml
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    Structured Review

    Vector Laboratories vectashield mounting medium
    VECTASHIELD Antifade Mounting Medium
    VECTASHIELD Antifade Mounting Medium is a unique stable formula for preserving fluorescence VECTASHIELD Mounting Medium prevents rapid photobleaching of fluorescent proteins and fluorescent dyes Features Inhibits photobleaching of dyes and fluorescent proteins Ideal refractive index Ready to use Offered with nuclear or cytoskeletal counterstains Available in non hardening or hardening formulations No warming necessary Can be stored without sealing for long term analysis Easy to useThe original VECTASHIELD Mounting Medium does not solidify but remains a liquid on the slide and can be stored without sealing If desired coverslips can be sealed around the perimeter with nail polish or a plastic sealant Mounted slides should be stored at 4 °C protected from light
    https://www.bioz.com/result/vectashield mounting medium/product/Vector Laboratories
    Average 99 stars, based on 1 article reviews
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    Related Articles

    Incubation:

    Article Title: Sequential and synchronized hypertonicity-induced activation of Rel-family transcription factors is required for osmoprotection in renal cells
    Article Snippet: .. Fixed cells were incubated with a mixture of mouse monoclonal p65/RelA antibody; 1:100 (Becton-Dickinson), TonEBP, 1:75 (Santa Cruz Biotechnology) and 2.5 μM Hoechst 33258 (Sigma-Aldrich) for 60 min. After labeling, samples were washed with PBS and incubated with FITC-conjugated goat anti-mouse 1:200 (Vector Lab) and Alexa Fluor 546-conjugated donkey anti-rabbit 1:200 (Invitrogen) secondary antibodies for 60 min. Then, samples were washed with PBS and mounted with a drop of Vectashield Mounting Medium (Vector Laboratories). .. Specimens were examined with an Olympus FV300 Confocal Microscope (Model BX61), with an acquisition software FluoView version 3.3 provided by the manufacturer.

    Labeling:

    Article Title: Sequential and synchronized hypertonicity-induced activation of Rel-family transcription factors is required for osmoprotection in renal cells
    Article Snippet: .. Fixed cells were incubated with a mixture of mouse monoclonal p65/RelA antibody; 1:100 (Becton-Dickinson), TonEBP, 1:75 (Santa Cruz Biotechnology) and 2.5 μM Hoechst 33258 (Sigma-Aldrich) for 60 min. After labeling, samples were washed with PBS and incubated with FITC-conjugated goat anti-mouse 1:200 (Vector Lab) and Alexa Fluor 546-conjugated donkey anti-rabbit 1:200 (Invitrogen) secondary antibodies for 60 min. Then, samples were washed with PBS and mounted with a drop of Vectashield Mounting Medium (Vector Laboratories). .. Specimens were examined with an Olympus FV300 Confocal Microscope (Model BX61), with an acquisition software FluoView version 3.3 provided by the manufacturer.

    Immunostaining:

    Article Title: Fgf10-Hippo epithelial mesenchymal crosstalk maintains and recruits lung basal stem cells
    Article Snippet: All fluorescent staining was performed with appropriate secondary antibodies from Jackson Immunoresearch, except for goat anti-chicken FITC (1:200; F-1005; Aves Labs, Inc.). .. Slides were mounted using Vectashield with (Vector Labs, H-1200) or without DAPI (Vector Labs, H-1000) depending on immunostaining. ..

    Staining:

    Article Title: Multimodal super-resolution optical microscopy visualizes the close connection between membrane and the cytoskeleton in liver sinusoidal endothelial cell fenestrations
    Article Snippet: This will provide us with an initial approach allowing us to overcome one of the current limitations of super-resolution microscopy, i.e. the combination of rapid live cell imaging of cellular processes with the highest spatial resolution possible. .. Materials Reagents included Type 1 A Collagenase (Sigma Chemical, St. Louis, MO #C2674,) RPMI (Gibco Invitrogen #11875-093), CellMask Deep Red Plasma Membrane Stain, Invitrogen, #C10046 Mouse monoclonal Anti-β-Tubulin antibody, SIGMA, T8328 Alexa Fluor® 647 F(ab’)2 Fragment of Goat Anti-Mouse IgG (H + L), Invitrogen, A-21237, Lot# 1094366 CellMask Orange 5 mg/ml, Invitrogen, C10045, Lot# 1159930 Alexa Fluor 488 – phalloidin 300 u in 1.5 ml Methanol, Invitrogen, A12379, Lot# 1120408 Vybrant DiD cell-labeling solution 1 mM, Invitrogen, V22887, Lot# 1046290 VECTASHIELD Mounting Medium with DAPI, Vector Laboratories, H-1200, Collagen and Fibronectin were purchased from Sigma Chemical. .. Isolation and culture of LSECs Sprague Dawley male rats (Scanbur BK, Sollentuna, Sweden) were kept under standard conditions and fed standard chow ad libitum (Scanbur, Nittedal, Norway).

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    Vector Laboratories vectashield with 4
    Rearrangement of actin cytoskeleton in infected ED cells. ( A ) ED cells were infected with parental, US3_1 -deleted, EHV-1 D207A , US3_4 -recombinant, or revertant viruses and imaged by immunofluorescence microscopy using a Zeiss Axiovert fluorescence microscope. Pictures were taken with a 63x oil objective. The nucleus was stained with <t>4′,6-diamidino-2-phenylindole</t> (DAPI, blue ), the actin cytoskeleton was stained with phalloidin-Alexa 568 ( red ), and the virus-infected cells were visualized through enhanced GFP (eGFP) expression ( green ). ( B and C ) A total of 200 infected cells for each virus in three independent experiments were inspected and the percentage of infected cells with or without changes in actin cytoskeleton was calculated. A significant change in actin cytoskeleton rearrangement was detected for either EHV-1ΔUS3 or EHV-1 D207A when compared to parental, recombinant, or revertant viruses (one-way ANOVA; p
    Vectashield With 4, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 99 stars, based on 1 article reviews
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    95
    Vector Laboratories propidium iodide
    PPARD is required for claudin-11 expression in Sertoli cells in vivo . A and B , representative photomicrographs of testicular sections from Ppard +/+ and Ppard −/− mice from PND14 to PND28 showing expression of claudin-11 as assessed by immunohistochemistry ( A ) or immunofluorescence ( green is claudin-11 and red is counterstain with <t>propidium</t> iodide) ( B ). A , the photomicrographs show expression of claudin-11 that forms a ring structure along the blood-testis barrier ( brown color). Magnification , 40×. Scale bars , 100 μm. B , representative photomicrographs showing that cytoplasmic claudin-11 expression of Sertoli cells is higher in Ppard +/+ compared with Ppard −/− mice. Magnification , 60×. Scale bars , 10 μm. C , quantitative Western blot analysis of claudin-11 expression in whole testis homogenates of Ppard +/+ and Ppard −/− mice from PND1 to PND28. The relative expression level of claudin was normalized to that of actin and represents the mean ± S.E. Values with different superscript letters are significantly different at p ≤ 0.05.
    Propidium Iodide, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Vector Laboratories 6 diamidino 2 phenylindole
    Expression of Rit2 mRNA and protein in the mouse retina. The top panels show immunohistochemistry of retinal flat-mounts ( A - D ) and retinal sections ( E - H ). Images are staining with anti-RIT2 antibody ( A , E ), anti-POU4F2 antibody ( B , F ), merged image of RIT2 and POU4F2 ( C , G ), and nuclear staining by 4', <t>6-diamidino-2-phenylindole</t> (DAPI; D , H ). RIT2-positive cells are more numerous than POU4F2-positive RGCs. E : RIT2 protein is detected in the ganglion cell layer (GCL), inner plexiform layer (IPL), and cells in the inner nuclear layer (INL). Short arrowheads point to RIT2-positive cells located at the inner border of the INL; long arrowheads point to RIT2-positive cells at the outer aspect of the INL. Scale bar: 50 μm. I : This panel shows Rit2 mRNA expression. Laser capture microdissection was used to collect tissues of GCL, INL, and outer nuclear layer (ONL) from mouse retinal sections, and RNA of each layer was analyzed by reverse transcription-quantitative polymerase chain reaction. The mRNA level of Rit2 , Pou4f1 , and Pou4f2 was normalized by that of Gapdh . J : RIT2 protein levels were analyzed at different ages. Protein lysates were prepared from mouse retinas at postnatal day 2 (P2), P5, P15, and adult (8 weeks old), and analyzed by western blotting with anti-RIT2 antibody and anti-α tubulin antibody for control. Protein signals were visualized by chemiluminescence with X-ray films. K : This panel shows relative quantification of RIT2 protein levels. Western blot signals on the X-ray films were scanned and analyzed with ImageJ software. The signal intensity of RIT2 was normalized by that of α tubulin and presented as the RIT2/tubulin ratio. RIT2 protein levels increased from P2 to adults by more than 15 fold.
    6 Diamidino 2 Phenylindole, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Rearrangement of actin cytoskeleton in infected ED cells. ( A ) ED cells were infected with parental, US3_1 -deleted, EHV-1 D207A , US3_4 -recombinant, or revertant viruses and imaged by immunofluorescence microscopy using a Zeiss Axiovert fluorescence microscope. Pictures were taken with a 63x oil objective. The nucleus was stained with 4′,6-diamidino-2-phenylindole (DAPI, blue ), the actin cytoskeleton was stained with phalloidin-Alexa 568 ( red ), and the virus-infected cells were visualized through enhanced GFP (eGFP) expression ( green ). ( B and C ) A total of 200 infected cells for each virus in three independent experiments were inspected and the percentage of infected cells with or without changes in actin cytoskeleton was calculated. A significant change in actin cytoskeleton rearrangement was detected for either EHV-1ΔUS3 or EHV-1 D207A when compared to parental, recombinant, or revertant viruses (one-way ANOVA; p

    Journal: Viruses

    Article Title: The Role of the Equine Herpesvirus Type 1 (EHV-1) US3-Encoded Protein Kinase in Actin Reorganization and Nuclear Egress

    doi: 10.3390/v8100275

    Figure Lengend Snippet: Rearrangement of actin cytoskeleton in infected ED cells. ( A ) ED cells were infected with parental, US3_1 -deleted, EHV-1 D207A , US3_4 -recombinant, or revertant viruses and imaged by immunofluorescence microscopy using a Zeiss Axiovert fluorescence microscope. Pictures were taken with a 63x oil objective. The nucleus was stained with 4′,6-diamidino-2-phenylindole (DAPI, blue ), the actin cytoskeleton was stained with phalloidin-Alexa 568 ( red ), and the virus-infected cells were visualized through enhanced GFP (eGFP) expression ( green ). ( B and C ) A total of 200 infected cells for each virus in three independent experiments were inspected and the percentage of infected cells with or without changes in actin cytoskeleton was calculated. A significant change in actin cytoskeleton rearrangement was detected for either EHV-1ΔUS3 or EHV-1 D207A when compared to parental, recombinant, or revertant viruses (one-way ANOVA; p

    Article Snippet: After blocking with 2% bovine serum albumin (BSA, AppliChem, Berlin, Germany), polymerized actin of infected cells was detected by staining with phalloidin-Alexa-Fluor-568 (1:40; Invitrogen) for 20 min. After washing three times, coverslips were mounted onto glass slides using Vectashield-with 4′,6-diamidino-2-phenylindole (DAPI; Vector Laboratories, Peterborough, UK).

    Techniques: Infection, Recombinant, Immunofluorescence, Microscopy, Fluorescence, Staining, Expressing

    Molecular bitter taste signalling elements are expressed in the mouse Grueneberg ganglion. a RT-PCR experiments revealing expression of three bitter taste receptors ( Tas2r115 , Tas2r131 and Tas2r143 ) and Gnat3 transcripts in the tongue ( T ) and in the mouse Grueneberg ganglion ( GG ). b Tas2r115 , Tas2r131, Tas2r143, Gnat3 and B2m expression in the GG and tongue of mice. + cDNA sample, – negative control omitting the reverse transcription. c Transcripts of sweet and umami taste receptors ( Tas1r1, Tas1r2 and Tas1r3) , phospholipase-C β2 ( Plcβ2 ) and of the transient receptor potential channel M5 ( Trpm5 ) were found in the tongue, but not in the GG. d Immunohistochemistries on mice tongue tissue section (circumvallate papillae) with antibodies against TAS2R143 and GNAT3. e Immunohistochemistries on mice GG sections with antibodies against TAS2R143 and GNAT3. GG cells expressing GFP are visible in green due to the intrinsic expression of the GFP. In a – c , M is 100-bp ladder and H is H 2 O. In d , e , white arrowheads correspond to enlarged views displayed in insets; nuclei are counterstained in blue with 4’,6-diamidino-2-phenylindole (DAPI); scale bars are 20 μm

    Journal: BMC Biology

    Article Title: Alarm pheromone and kairomone detection via bitter taste receptors in the mouse Grueneberg ganglion

    doi: 10.1186/s12915-017-0479-y

    Figure Lengend Snippet: Molecular bitter taste signalling elements are expressed in the mouse Grueneberg ganglion. a RT-PCR experiments revealing expression of three bitter taste receptors ( Tas2r115 , Tas2r131 and Tas2r143 ) and Gnat3 transcripts in the tongue ( T ) and in the mouse Grueneberg ganglion ( GG ). b Tas2r115 , Tas2r131, Tas2r143, Gnat3 and B2m expression in the GG and tongue of mice. + cDNA sample, – negative control omitting the reverse transcription. c Transcripts of sweet and umami taste receptors ( Tas1r1, Tas1r2 and Tas1r3) , phospholipase-C β2 ( Plcβ2 ) and of the transient receptor potential channel M5 ( Trpm5 ) were found in the tongue, but not in the GG. d Immunohistochemistries on mice tongue tissue section (circumvallate papillae) with antibodies against TAS2R143 and GNAT3. e Immunohistochemistries on mice GG sections with antibodies against TAS2R143 and GNAT3. GG cells expressing GFP are visible in green due to the intrinsic expression of the GFP. In a – c , M is 100-bp ladder and H is H 2 O. In d , e , white arrowheads correspond to enlarged views displayed in insets; nuclei are counterstained in blue with 4’,6-diamidino-2-phenylindole (DAPI); scale bars are 20 μm

    Article Snippet: Tissue slices were finally washed three times in a decreasing concentration solution of NGS in PBS (2% NGS, 1% NGS and PBS) 5 min at room temperature and mounted in Vectashield with 4’,6-diamidino-2-phenylindole (DAPI) (H-1200, Vector Labs) mounting medium.

    Techniques: Reverse Transcription Polymerase Chain Reaction, Expressing, Mouse Assay, Negative Control

    PPARD is required for claudin-11 expression in Sertoli cells in vivo . A and B , representative photomicrographs of testicular sections from Ppard +/+ and Ppard −/− mice from PND14 to PND28 showing expression of claudin-11 as assessed by immunohistochemistry ( A ) or immunofluorescence ( green is claudin-11 and red is counterstain with propidium iodide) ( B ). A , the photomicrographs show expression of claudin-11 that forms a ring structure along the blood-testis barrier ( brown color). Magnification , 40×. Scale bars , 100 μm. B , representative photomicrographs showing that cytoplasmic claudin-11 expression of Sertoli cells is higher in Ppard +/+ compared with Ppard −/− mice. Magnification , 60×. Scale bars , 10 μm. C , quantitative Western blot analysis of claudin-11 expression in whole testis homogenates of Ppard +/+ and Ppard −/− mice from PND1 to PND28. The relative expression level of claudin was normalized to that of actin and represents the mean ± S.E. Values with different superscript letters are significantly different at p ≤ 0.05.

    Journal: The Journal of Biological Chemistry

    Article Title: Peroxisome Proliferator-activated Receptor-D (PPARD) Coordinates Mouse Spermatogenesis by Modulating Extracellular Signal-regulated Kinase (ERK)-dependent Signaling *

    doi: 10.1074/jbc.M115.664508

    Figure Lengend Snippet: PPARD is required for claudin-11 expression in Sertoli cells in vivo . A and B , representative photomicrographs of testicular sections from Ppard +/+ and Ppard −/− mice from PND14 to PND28 showing expression of claudin-11 as assessed by immunohistochemistry ( A ) or immunofluorescence ( green is claudin-11 and red is counterstain with propidium iodide) ( B ). A , the photomicrographs show expression of claudin-11 that forms a ring structure along the blood-testis barrier ( brown color). Magnification , 40×. Scale bars , 100 μm. B , representative photomicrographs showing that cytoplasmic claudin-11 expression of Sertoli cells is higher in Ppard +/+ compared with Ppard −/− mice. Magnification , 60×. Scale bars , 10 μm. C , quantitative Western blot analysis of claudin-11 expression in whole testis homogenates of Ppard +/+ and Ppard −/− mice from PND1 to PND28. The relative expression level of claudin was normalized to that of actin and represents the mean ± S.E. Values with different superscript letters are significantly different at p ≤ 0.05.

    Article Snippet: Sections were then incubated with Alexa Fluor-conjugated secondary antibodies (PCNA, Alexa Fluor 647; SOX9, Alexa Fluor 488; claudin-11, Alexa Fluor 488; Invitrogen) for 1 h and mounted with Vectashield mounting medium containing propidium iodide (Vector Labs, Burlingame, CA).

    Techniques: Expressing, In Vivo, Mouse Assay, Immunohistochemistry, Immunofluorescence, Western Blot

    Expression of Rit2 mRNA and protein in the mouse retina. The top panels show immunohistochemistry of retinal flat-mounts ( A - D ) and retinal sections ( E - H ). Images are staining with anti-RIT2 antibody ( A , E ), anti-POU4F2 antibody ( B , F ), merged image of RIT2 and POU4F2 ( C , G ), and nuclear staining by 4', 6-diamidino-2-phenylindole (DAPI; D , H ). RIT2-positive cells are more numerous than POU4F2-positive RGCs. E : RIT2 protein is detected in the ganglion cell layer (GCL), inner plexiform layer (IPL), and cells in the inner nuclear layer (INL). Short arrowheads point to RIT2-positive cells located at the inner border of the INL; long arrowheads point to RIT2-positive cells at the outer aspect of the INL. Scale bar: 50 μm. I : This panel shows Rit2 mRNA expression. Laser capture microdissection was used to collect tissues of GCL, INL, and outer nuclear layer (ONL) from mouse retinal sections, and RNA of each layer was analyzed by reverse transcription-quantitative polymerase chain reaction. The mRNA level of Rit2 , Pou4f1 , and Pou4f2 was normalized by that of Gapdh . J : RIT2 protein levels were analyzed at different ages. Protein lysates were prepared from mouse retinas at postnatal day 2 (P2), P5, P15, and adult (8 weeks old), and analyzed by western blotting with anti-RIT2 antibody and anti-α tubulin antibody for control. Protein signals were visualized by chemiluminescence with X-ray films. K : This panel shows relative quantification of RIT2 protein levels. Western blot signals on the X-ray films were scanned and analyzed with ImageJ software. The signal intensity of RIT2 was normalized by that of α tubulin and presented as the RIT2/tubulin ratio. RIT2 protein levels increased from P2 to adults by more than 15 fold.

    Journal: Molecular Vision

    Article Title: RIT2, a neuron-specific small guanosine triphosphatase, is expressed in retinal neuronal cells and its promoter is modulated by the POU4 transcription factors

    doi:

    Figure Lengend Snippet: Expression of Rit2 mRNA and protein in the mouse retina. The top panels show immunohistochemistry of retinal flat-mounts ( A - D ) and retinal sections ( E - H ). Images are staining with anti-RIT2 antibody ( A , E ), anti-POU4F2 antibody ( B , F ), merged image of RIT2 and POU4F2 ( C , G ), and nuclear staining by 4', 6-diamidino-2-phenylindole (DAPI; D , H ). RIT2-positive cells are more numerous than POU4F2-positive RGCs. E : RIT2 protein is detected in the ganglion cell layer (GCL), inner plexiform layer (IPL), and cells in the inner nuclear layer (INL). Short arrowheads point to RIT2-positive cells located at the inner border of the INL; long arrowheads point to RIT2-positive cells at the outer aspect of the INL. Scale bar: 50 μm. I : This panel shows Rit2 mRNA expression. Laser capture microdissection was used to collect tissues of GCL, INL, and outer nuclear layer (ONL) from mouse retinal sections, and RNA of each layer was analyzed by reverse transcription-quantitative polymerase chain reaction. The mRNA level of Rit2 , Pou4f1 , and Pou4f2 was normalized by that of Gapdh . J : RIT2 protein levels were analyzed at different ages. Protein lysates were prepared from mouse retinas at postnatal day 2 (P2), P5, P15, and adult (8 weeks old), and analyzed by western blotting with anti-RIT2 antibody and anti-α tubulin antibody for control. Protein signals were visualized by chemiluminescence with X-ray films. K : This panel shows relative quantification of RIT2 protein levels. Western blot signals on the X-ray films were scanned and analyzed with ImageJ software. The signal intensity of RIT2 was normalized by that of α tubulin and presented as the RIT2/tubulin ratio. RIT2 protein levels increased from P2 to adults by more than 15 fold.

    Article Snippet: The flat mounts were washed with 0.1% PBST, mounted in VECTASHIELD HardSet Mounting Medium with 4', 6-diamidino-2-phenylindole (H-1500, Vector Laboratories, Burlingame, CA), and examined on an LSM 510 inverted laser scanning confocal microscope (Carl Zeiss, Thornwood, NY).

    Techniques: Expressing, Immunohistochemistry, Staining, Laser Capture Microdissection, Real-time Polymerase Chain Reaction, Western Blot, Software