vectashield  (Vector Laboratories)


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    VECTASHIELD Hardset Antifade Mounting Medium with Phalloidin
    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 No warming necessary Offered with nuclear or cytoskeletal counterstains Available in non hardening or hardening formulations Can be stored without sealing for long term analysis Easy to useVECTASHIELD HardSet Mounting Medium preserves fluorescence and hardens after coverslipping After approximately 15 minutes at room temperature the coverslip will become immobilized and optimal antifade ability and refractive index will be achieved VECTASHIELD HardSet Mounting Media are compatible with a wide array of fluorochromes enzymatic substrates and fluorescent proteins Please consult the compatibility table under the Protocol Data Sheet MSDS tab to determine if VECTASHIELD will be compatible in your system This special formulation of VECTASHIELD HardSet Mounting Medium contains TRITC phalloidin Phalloidin is a bicyclic heptapeptide that specifically binds at the interface between the F actin subunits Fluorescent derivatives of phalloidin are used to stain actin filaments TRITC tetramethylrhodamine is excited at 544 nm and emits at 572 nm producing an orange red fluorescence
    Catalog Number:
    H-1600
    Price:
    None
    Category:
    Histology reagents or solutions or stains
    Size:
    10 ml
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    Structured Review

    Vector Laboratories vectashield
    VECTASHIELD Hardset Antifade Mounting Medium with Phalloidin
    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 No warming necessary Offered with nuclear or cytoskeletal counterstains Available in non hardening or hardening formulations Can be stored without sealing for long term analysis Easy to useVECTASHIELD HardSet Mounting Medium preserves fluorescence and hardens after coverslipping After approximately 15 minutes at room temperature the coverslip will become immobilized and optimal antifade ability and refractive index will be achieved VECTASHIELD HardSet Mounting Media are compatible with a wide array of fluorochromes enzymatic substrates and fluorescent proteins Please consult the compatibility table under the Protocol Data Sheet MSDS tab to determine if VECTASHIELD will be compatible in your system This special formulation of VECTASHIELD HardSet Mounting Medium contains TRITC phalloidin Phalloidin is a bicyclic heptapeptide that specifically binds at the interface between the F actin subunits Fluorescent derivatives of phalloidin are used to stain actin filaments TRITC tetramethylrhodamine is excited at 544 nm and emits at 572 nm producing an orange red fluorescence
    https://www.bioz.com/result/vectashield/product/Vector Laboratories
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    Article Title: Alpha-Methylacyl-CoA Racemase (AMACR), a Potential New Biomarker for Glioblastoma
    Article Snippet: The secondary antibody, FITC-conjugated anti-rabbit antibody (BD Biosciences) was used. .. After appropriate rinsing, cover slips were mounted with Vectashield (Vector Laboratories) and visualized using a Leica confocal microscope. .. ImmunohistochemistryThe analysis of immunohistochemistry was performed as the described previously ( ).

    Article Title: Measurement of replication structures at the nanometer scale using super-resolution light microscopy
    Article Snippet: For 3D-SIM cells were typically postfixed with 2% formaldehyde in PBS in order to minimize background fluorescence and floating particles or antibody precipitates and counterstained with 100 ng/ml 4′,6-diamidino-2-phenylindole (DAPI; Sigma). .. Samples were mounted in Mowiol or Vectashield for confocal and conventional microscopy and in Vectashield (Vector Laboratories) for high-resolution microscopy. .. Anti-GFP immunostaining Cryosections were rinsed (3×) in PBS, incubated (15 min) in 20 mM glycine in PBS, rinsed (3×) in PBS, treated (10 min) with 0.1% Triton X-100 in PBS, blocked (30 min) with PBS+ (PBS supplemented with 1% BSA, 0.2% fish skin gelatin, 0.1% casein; pH 7.6), incubated (2 h) with rabbit antibodies anti-GFP (diluted 1:50 in PBS+; affinity-purified rabbit polyclonal antibodies raised against full-length GFPS65T), washed (5×, over 1 h) in PBS+, incubated (1 h) with Alexa Fluor 488-conjugated antibodies against rabbit IgGs (in PBS+; raised in donkey; Molecular Probes), rinsed (3×, 30 min) in PBS+, rinsed (3×) in PBS, counterstained (45 min) with TOTO-3 (2 µM, Molecular Probes) in 0.05% Tween-20 in PBS, rinsed successively in 0.05% Tween-20 in PBS and then PBS, before coverslips were mounted in Vectashield (Vector Laboratories) on glass slides coated with 0.1 µm FluoresbriteTM Carboxylate YG microspheres (Polysciences).

    Article Title: α-Tocopheryl succinate and TRAIL selectively synergise in induction of apoptosis in human malignant mesothelioma cells
    Article Snippet: .. The coverslips were mounted on glass slides with Vectashield (Vector Laboratories, Inc., Burlingame, CA 94010, USA) and viewed in a fluorescence microscope. .. Confocal microscope analysis Met-5A and MM-B1 cells were plated in a six-well plate at 2 × 105 and transiently transfected with pDsRed1-N1 harbouring RFP, and with GFP-expressing vector (pGFP) (BD Biosciences, Palo Alto, CA, USA), respectively.

    Article Title: Recognition of Transmembrane Protein 39A as a Tumor-Specific Marker in Brain Tumor
    Article Snippet: The secondary antibody, FITC-conjugated anti-rabbit antibody (BD Biosciences, NJ, USA) was used. .. After appropriate rinsing, cover slips were mounted with Vectashield (Vector Laboratories, CA, USA) and visualized using a Zeiss confocal microscope. ..

    Fluorescence:

    Article Title: α-Tocopheryl succinate and TRAIL selectively synergise in induction of apoptosis in human malignant mesothelioma cells
    Article Snippet: .. The coverslips were mounted on glass slides with Vectashield (Vector Laboratories, Inc., Burlingame, CA 94010, USA) and viewed in a fluorescence microscope. .. Confocal microscope analysis Met-5A and MM-B1 cells were plated in a six-well plate at 2 × 105 and transiently transfected with pDsRed1-N1 harbouring RFP, and with GFP-expressing vector (pGFP) (BD Biosciences, Palo Alto, CA, USA), respectively.

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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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    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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    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