alexa fluor 568 conjugated goat anti rabbit igg  (Thermo Fisher)


Bioz Verified Symbol Thermo Fisher is a verified supplier  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 91

    Structured Review

    Thermo Fisher alexa fluor 568 conjugated goat anti rabbit igg
    Flow cytometry of transfected cells stained separately for the ORF2 or ORF3 protein. HepG2/C3A and LLC-PK cells electroporated with transcripts from P6 (A), Sar55 (B), or Sar/S17 (C, D) were plated in 6 wells of a 6-well culture plate, incubated at 34.5°C, and harvested 7 (A, B) or 5 (C, D) days later. Cells in triplicate wells were stained for the ORF2 protein, followed by goat anti-human <t>IgG</t> labeled with <t>Alexa</t> Fluor 488 (open bars); cells in the other 3 wells were stained for the ORF3 protein, followed by goat anti-rabbit IgG also labeled with Alexa Fluor 488 (hatched bars). Flow cytometry was performed with the same settings for all samples. (A to C) Mean percentage of positive cells, in triplicate; (D) mean of the geometric mean fluorescence intensity in the same triplicate samples assayed for panel C. Shaded bars, ORF2; dotted bars, ORF3. Error bars indicate standard deviations. P values were determined by Student's t test; P values of less than 0.05 were statistically significant.
    Alexa Fluor 568 Conjugated Goat Anti Rabbit Igg, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 91/100, based on 114 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/alexa fluor 568 conjugated goat anti rabbit igg/product/Thermo Fisher
    Average 91 stars, based on 114 article reviews
    Price from $9.99 to $1999.99
    alexa fluor 568 conjugated goat anti rabbit igg - by Bioz Stars, 2020-08
    91/100 stars

    Images

    1) Product Images from "Hepatitis E Virus Genotype 1 Infection of Swine Kidney Cells In Vitro Is Inhibited at Multiple Levels"

    Article Title: Hepatitis E Virus Genotype 1 Infection of Swine Kidney Cells In Vitro Is Inhibited at Multiple Levels

    Journal: Journal of Virology

    doi: 10.1128/JVI.02205-13

    Flow cytometry of transfected cells stained separately for the ORF2 or ORF3 protein. HepG2/C3A and LLC-PK cells electroporated with transcripts from P6 (A), Sar55 (B), or Sar/S17 (C, D) were plated in 6 wells of a 6-well culture plate, incubated at 34.5°C, and harvested 7 (A, B) or 5 (C, D) days later. Cells in triplicate wells were stained for the ORF2 protein, followed by goat anti-human IgG labeled with Alexa Fluor 488 (open bars); cells in the other 3 wells were stained for the ORF3 protein, followed by goat anti-rabbit IgG also labeled with Alexa Fluor 488 (hatched bars). Flow cytometry was performed with the same settings for all samples. (A to C) Mean percentage of positive cells, in triplicate; (D) mean of the geometric mean fluorescence intensity in the same triplicate samples assayed for panel C. Shaded bars, ORF2; dotted bars, ORF3. Error bars indicate standard deviations. P values were determined by Student's t test; P values of less than 0.05 were statistically significant.
    Figure Legend Snippet: Flow cytometry of transfected cells stained separately for the ORF2 or ORF3 protein. HepG2/C3A and LLC-PK cells electroporated with transcripts from P6 (A), Sar55 (B), or Sar/S17 (C, D) were plated in 6 wells of a 6-well culture plate, incubated at 34.5°C, and harvested 7 (A, B) or 5 (C, D) days later. Cells in triplicate wells were stained for the ORF2 protein, followed by goat anti-human IgG labeled with Alexa Fluor 488 (open bars); cells in the other 3 wells were stained for the ORF3 protein, followed by goat anti-rabbit IgG also labeled with Alexa Fluor 488 (hatched bars). Flow cytometry was performed with the same settings for all samples. (A to C) Mean percentage of positive cells, in triplicate; (D) mean of the geometric mean fluorescence intensity in the same triplicate samples assayed for panel C. Shaded bars, ORF2; dotted bars, ORF3. Error bars indicate standard deviations. P values were determined by Student's t test; P values of less than 0.05 were statistically significant.

    Techniques Used: Flow Cytometry, Cytometry, Transfection, Staining, Incubation, Labeling, Fluorescence

    2) Product Images from "The C-Terminal TDP-43 Fragments Have a High Aggregation Propensity and Harm Neurons by a Dominant-Negative Mechanism"

    Article Title: The C-Terminal TDP-43 Fragments Have a High Aggregation Propensity and Harm Neurons by a Dominant-Negative Mechanism

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0015878

    Expression of the various TDP-43-EGFP constructs in NSC-34 cells. ( A ) Forty eight hours after transfection, proteins were extracted from NSC-34 cells and the fusion proteins were detected by Western blot using an EGFP antibody. Fifteen µg of protein was loaded in each lane. α-Tubulin was detected as loading control. Left and right panels are two independent gels. ( B ) Cells was transfected with construct 1 alone and then stained with antiTDP-43 primary and Alexa Fluor®568-conjugated secondary antibodies. The nuclei are stained with DAPI. The scale bar marks 10 µm.
    Figure Legend Snippet: Expression of the various TDP-43-EGFP constructs in NSC-34 cells. ( A ) Forty eight hours after transfection, proteins were extracted from NSC-34 cells and the fusion proteins were detected by Western blot using an EGFP antibody. Fifteen µg of protein was loaded in each lane. α-Tubulin was detected as loading control. Left and right panels are two independent gels. ( B ) Cells was transfected with construct 1 alone and then stained with antiTDP-43 primary and Alexa Fluor®568-conjugated secondary antibodies. The nuclei are stained with DAPI. The scale bar marks 10 µm.

    Techniques Used: Expressing, Construct, Transfection, Western Blot, Staining

    3) Product Images from "The C-Terminal TDP-43 Fragments Have a High Aggregation Propensity and Harm Neurons by a Dominant-Negative Mechanism"

    Article Title: The C-Terminal TDP-43 Fragments Have a High Aggregation Propensity and Harm Neurons by a Dominant-Negative Mechanism

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0015878

    Expression of the various TDP-43-EGFP constructs in NSC-34 cells. ( A ) Forty eight hours after transfection, proteins were extracted from NSC-34 cells and the fusion proteins were detected by Western blot using an EGFP antibody. Fifteen µg of protein was loaded in each lane. α-Tubulin was detected as loading control. Left and right panels are two independent gels. ( B ) Cells was transfected with construct 1 alone and then stained with antiTDP-43 primary and Alexa Fluor®568-conjugated secondary antibodies. The nuclei are stained with DAPI. The scale bar marks 10 µm.
    Figure Legend Snippet: Expression of the various TDP-43-EGFP constructs in NSC-34 cells. ( A ) Forty eight hours after transfection, proteins were extracted from NSC-34 cells and the fusion proteins were detected by Western blot using an EGFP antibody. Fifteen µg of protein was loaded in each lane. α-Tubulin was detected as loading control. Left and right panels are two independent gels. ( B ) Cells was transfected with construct 1 alone and then stained with antiTDP-43 primary and Alexa Fluor®568-conjugated secondary antibodies. The nuclei are stained with DAPI. The scale bar marks 10 µm.

    Techniques Used: Expressing, Construct, Transfection, Western Blot, Staining

    4) Product Images from "Intracellular Trafficking of Clostridium perfringens Iota-Toxin b"

    Article Title: Intracellular Trafficking of Clostridium perfringens Iota-Toxin b

    Journal: Infection and Immunity

    doi: 10.1128/IAI.00483-12

    Colocalization of Ib and endosome markers in MDCK cells. (A) MDCK cells were incubated with Ib (1 μg/ml) at 4°C for 1 h, washed, and incubated at 37°C for the period indicated. Cells were fixed, permeabilized, and stained with DAPI and antibodies to EEA1, Lamp2, Golgi 58K, and Ib. MDCK cells were transiently transfected with pGFP-Rab11, pGFP-lysosome, or pER-GFP. After 24 h of transfection, the transfected cells were incubated with Ib as described above. Cells were fixed, permeabilized, and stained with anti-Ib antibody and DAPI. Ib (red), endosome markers (green), and the nucleus (blue) were viewed with a confocal microscope. The experiments were repeated three times, and a representative result is shown. Bar, 5 μm. (B) Negative-control preparation. Cells were fixed, permeabilized, and stained with Alexa Fluor 568-conjugated anti-rabbit IgG, FITC-conjugated anti-mouse IgG, and DAPI. (C) Quantification of colocalizations. The percentage of Ib/endocytic marker colocalization represents the ratio of the number of endosomal structures stained for Ib and for endocytic marker to the total number of endosomal structures stained for endocytic marker. The percentage of colocalization was determined for each cell, and the results represent the average ± standard error of the mean (SEM) for several cells ( n > 10) obtained from at least three independent experiments.
    Figure Legend Snippet: Colocalization of Ib and endosome markers in MDCK cells. (A) MDCK cells were incubated with Ib (1 μg/ml) at 4°C for 1 h, washed, and incubated at 37°C for the period indicated. Cells were fixed, permeabilized, and stained with DAPI and antibodies to EEA1, Lamp2, Golgi 58K, and Ib. MDCK cells were transiently transfected with pGFP-Rab11, pGFP-lysosome, or pER-GFP. After 24 h of transfection, the transfected cells were incubated with Ib as described above. Cells were fixed, permeabilized, and stained with anti-Ib antibody and DAPI. Ib (red), endosome markers (green), and the nucleus (blue) were viewed with a confocal microscope. The experiments were repeated three times, and a representative result is shown. Bar, 5 μm. (B) Negative-control preparation. Cells were fixed, permeabilized, and stained with Alexa Fluor 568-conjugated anti-rabbit IgG, FITC-conjugated anti-mouse IgG, and DAPI. (C) Quantification of colocalizations. The percentage of Ib/endocytic marker colocalization represents the ratio of the number of endosomal structures stained for Ib and for endocytic marker to the total number of endosomal structures stained for endocytic marker. The percentage of colocalization was determined for each cell, and the results represent the average ± standard error of the mean (SEM) for several cells ( n > 10) obtained from at least three independent experiments.

    Techniques Used: Incubation, Staining, Transfection, Microscopy, Negative Control, Marker

    5) Product Images from "Nuclear localization of Annexin A7 during murine brain development"

    Article Title: Nuclear localization of Annexin A7 during murine brain development

    Journal: BMC Neuroscience

    doi: 10.1186/1471-2202-6-25

    Annexin A7 immunoreactivity in early mouse embryos. ( A ) Phase contrast, embryo E5: The egg cylinder consists of an inner cell mass (a) representing the ectoderm and an outer layer of endoderm cells (b). (B) Immunostaining of the paraffin section was performed using purified mAb 203–217 and Cy3-conjugated anti-mouse IgG. Annexin A7 is expressed in both cell types of the egg cylinder with a strong staining of the endoderm and a weaker staining of the ectoderm. The nuclei are devoid of immune reactions. ( C ) Negative control using the secondary Cy3-antibody only. ( D-F ) Annexin A7 expression in the proximal neural tube (D) and nearby neural fold (E,F), embryo E8, transverse section. Immunolabeling of Annexin A7 was performed with purified mAb 203–217 and visualization was with an Alexa Fluor 488-conjugated anti-mouse IgG. ( D ) An intense Annexin A7 immunostaining is detectable in the neuroepithelium of the neural tube (a, lumen of neural tube). ( E,F ) Higher magnifications of the neuroepithelium show that Annexin A7 is expressed in the cytosol. Arrowheads point to Annexin A7 immunoreactivity in the cytosol. ( G ) Phase contrast, embryo E13, caudal neural tube. (H) Immunostaining of the paraffin section was performed using purified mAb 203–217 and Alexa Fluor 488-conjugated anti-mouse IgG. ( I ) Negative control using the secondary Alexa Fluor 488-antibody only. Bar, 20 μm.
    Figure Legend Snippet: Annexin A7 immunoreactivity in early mouse embryos. ( A ) Phase contrast, embryo E5: The egg cylinder consists of an inner cell mass (a) representing the ectoderm and an outer layer of endoderm cells (b). (B) Immunostaining of the paraffin section was performed using purified mAb 203–217 and Cy3-conjugated anti-mouse IgG. Annexin A7 is expressed in both cell types of the egg cylinder with a strong staining of the endoderm and a weaker staining of the ectoderm. The nuclei are devoid of immune reactions. ( C ) Negative control using the secondary Cy3-antibody only. ( D-F ) Annexin A7 expression in the proximal neural tube (D) and nearby neural fold (E,F), embryo E8, transverse section. Immunolabeling of Annexin A7 was performed with purified mAb 203–217 and visualization was with an Alexa Fluor 488-conjugated anti-mouse IgG. ( D ) An intense Annexin A7 immunostaining is detectable in the neuroepithelium of the neural tube (a, lumen of neural tube). ( E,F ) Higher magnifications of the neuroepithelium show that Annexin A7 is expressed in the cytosol. Arrowheads point to Annexin A7 immunoreactivity in the cytosol. ( G ) Phase contrast, embryo E13, caudal neural tube. (H) Immunostaining of the paraffin section was performed using purified mAb 203–217 and Alexa Fluor 488-conjugated anti-mouse IgG. ( I ) Negative control using the secondary Alexa Fluor 488-antibody only. Bar, 20 μm.

    Techniques Used: Immunostaining, Paraffin Section, Purification, Staining, Negative Control, Expressing, Immunolabeling

    6) Product Images from "UDP-glucose dehydrogenase as a novel field-specific candidate biomarker of prostate cancer"

    Article Title: UDP-glucose dehydrogenase as a novel field-specific candidate biomarker of prostate cancer

    Journal: International journal of cancer. Journal international du cancer

    doi: 10.1002/ijc.24820

    Stability of the imaging system and reproducibility of UGDH quantification across analytical runs System stability was determined by quantifying the fluorescence emission of standard microspheres in a set of three slides; prior to each imaging/image capture session. Fluorescence was corrected for background and expressed as AMPI of 200–300 microspheres. AMPI are given in grayscale units (gsu) on a 12-bit scale (0–4095 units). The data of four representative analytical runs are presented. Six slide specimens of standard PC3 cells and two slide specimens of a benign prostate gland were incorporated into each analytical run. Both standards were probed with rabbit anti-UGDH anti-serum and labeled with Alexa Fluor 568-conjugated goat anti-rabbit IgG. Background corrected fluorescence emission was expressed as AMPI of 400–700 single cells and 100–200 prostatic acini, per slide. Each bar represents the mean of the AMPI of three slides (microspheres), six slides (PC3 cells) or two slides (prostate tissue). Data of four representative analytical runs are presented. The standard errors for each set of three microsphere slides are 1, 10, 2, and 12 gsu; each set of six PC3 slides are 13, 19, 29 and 32 gsu; and each set of two prostate tissue slides are 15, 25, 18 and 24 gsu, for analytical run 1, 2, 3, and 4, respectively.
    Figure Legend Snippet: Stability of the imaging system and reproducibility of UGDH quantification across analytical runs System stability was determined by quantifying the fluorescence emission of standard microspheres in a set of three slides; prior to each imaging/image capture session. Fluorescence was corrected for background and expressed as AMPI of 200–300 microspheres. AMPI are given in grayscale units (gsu) on a 12-bit scale (0–4095 units). The data of four representative analytical runs are presented. Six slide specimens of standard PC3 cells and two slide specimens of a benign prostate gland were incorporated into each analytical run. Both standards were probed with rabbit anti-UGDH anti-serum and labeled with Alexa Fluor 568-conjugated goat anti-rabbit IgG. Background corrected fluorescence emission was expressed as AMPI of 400–700 single cells and 100–200 prostatic acini, per slide. Each bar represents the mean of the AMPI of three slides (microspheres), six slides (PC3 cells) or two slides (prostate tissue). Data of four representative analytical runs are presented. The standard errors for each set of three microsphere slides are 1, 10, 2, and 12 gsu; each set of six PC3 slides are 13, 19, 29 and 32 gsu; and each set of two prostate tissue slides are 15, 25, 18 and 24 gsu, for analytical run 1, 2, 3, and 4, respectively.

    Techniques Used: Imaging, Fluorescence, Labeling

    UGDH expression determined by QFIA of archived prostate biopsies is significantly different among three classes of prostatic acini; normal acini (NA) of non-cancerous glands and normal appearing acini (NAA) and cancerous acini/epithelium (CA) of cancerous glands Panel A . Grayscale images of prostatic acini labeled with anti-UGDH anti-serum and Alexa Fluor 568 conjugated goat anti-rabbit IgG were captured with a 10x objective. Normal acini ( image 1 ) exhibited fluorescence intensity intermediate between cancerous acini ( image 2 ) and normal appearing acini ( image 3 ). Both cancerous and normal appearing acini were captured in image 4 . Panel B . UGDH was quantified in the CA and NAA of biopsies from 32 prostate cancer patients and in the NA of biopsies from 32 age-matched controls without clinical cancer. The average of the background-corrected mean pixel intensity (AMPI) for acini/epithelium within each class was determined for each case and control. The percentage of cases or controls at or below the selected threshold AMPIs was plotted for each class of acinus/epithelium.
    Figure Legend Snippet: UGDH expression determined by QFIA of archived prostate biopsies is significantly different among three classes of prostatic acini; normal acini (NA) of non-cancerous glands and normal appearing acini (NAA) and cancerous acini/epithelium (CA) of cancerous glands Panel A . Grayscale images of prostatic acini labeled with anti-UGDH anti-serum and Alexa Fluor 568 conjugated goat anti-rabbit IgG were captured with a 10x objective. Normal acini ( image 1 ) exhibited fluorescence intensity intermediate between cancerous acini ( image 2 ) and normal appearing acini ( image 3 ). Both cancerous and normal appearing acini were captured in image 4 . Panel B . UGDH was quantified in the CA and NAA of biopsies from 32 prostate cancer patients and in the NA of biopsies from 32 age-matched controls without clinical cancer. The average of the background-corrected mean pixel intensity (AMPI) for acini/epithelium within each class was determined for each case and control. The percentage of cases or controls at or below the selected threshold AMPIs was plotted for each class of acinus/epithelium.

    Techniques Used: Expressing, Labeling, Fluorescence

    Specificity of rabbit antiserum prepared against UGDH (A) A Western Blot of whole cell lysate of 22Rv1 prostate cancer cells and purified recombinant UGDH (rUGDH) was probed with rabbit anti-UGDH serum, yielding a single band. (B) Slide specimens of a benign hyperplastic prostate gland were probed with anti-UGDH serum alone or in combination with the indicated concentrations of rUGDH. After secondary labeling with Alexa Fluor-conjugated goat anti-rabbit IgG antibodies, fluorescence images were captured, and prostate acini were partitioned. Background-corrected MPI was determined for each acinus and average MPI was calculated for 50 to 70 acini per slide specimen.
    Figure Legend Snippet: Specificity of rabbit antiserum prepared against UGDH (A) A Western Blot of whole cell lysate of 22Rv1 prostate cancer cells and purified recombinant UGDH (rUGDH) was probed with rabbit anti-UGDH serum, yielding a single band. (B) Slide specimens of a benign hyperplastic prostate gland were probed with anti-UGDH serum alone or in combination with the indicated concentrations of rUGDH. After secondary labeling with Alexa Fluor-conjugated goat anti-rabbit IgG antibodies, fluorescence images were captured, and prostate acini were partitioned. Background-corrected MPI was determined for each acinus and average MPI was calculated for 50 to 70 acini per slide specimen.

    Techniques Used: Western Blot, Purification, Recombinant, Labeling, Fluorescence

    7) Product Images from "Receptor (CD155)-Dependent Endocytosis of Poliovirus and Retrograde Axonal Transport of the Endosome"

    Article Title: Receptor (CD155)-Dependent Endocytosis of Poliovirus and Retrograde Axonal Transport of the Endosome

    Journal: Journal of Virology

    doi: 10.1128/JVI.78.13.7186-7198.2004

    Localization of hPVRs in PC12 cells. hPVRα (A and E), hPVRMα (B), hPVRα-GFP (C), and hPVRMα-GFP (D) were introduced into PC12 cells. (A to D) The cells were incubated with PV. The cells transfected with hPVRα (A and E) or hPVRMα (B) were immunostained with anti-hPVR and anti-PV antibodies. These primary antibodies were stained with Alexa Fluor 488 (green)-conjugated antibody and Alexa Fluor 568 (red)-conjugated antibody, respectively. In the case of hPVRα-GFP (C) and hPVRMα-GFP (D), cells were incubated with only anti-PV antibody and detected using Alexa Fluor 568 (red)-conjugated antibody.
    Figure Legend Snippet: Localization of hPVRs in PC12 cells. hPVRα (A and E), hPVRMα (B), hPVRα-GFP (C), and hPVRMα-GFP (D) were introduced into PC12 cells. (A to D) The cells were incubated with PV. The cells transfected with hPVRα (A and E) or hPVRMα (B) were immunostained with anti-hPVR and anti-PV antibodies. These primary antibodies were stained with Alexa Fluor 488 (green)-conjugated antibody and Alexa Fluor 568 (red)-conjugated antibody, respectively. In the case of hPVRα-GFP (C) and hPVRMα-GFP (D), cells were incubated with only anti-PV antibody and detected using Alexa Fluor 568 (red)-conjugated antibody.

    Techniques Used: Incubation, Transfection, Staining

    8) Product Images from "Inhibition of Phagocytosis by Haemophilus ducreyi Requires Expression of the LspA1 and LspA2 Proteins "

    Article Title: Inhibition of Phagocytosis by Haemophilus ducreyi Requires Expression of the LspA1 and LspA2 Proteins

    Journal: Infection and Immunity

    doi: 10.1128/IAI.71.10.5994-6003.2003

    Differential staining to distinguish bacteria in intra- and extracellular locations. Murine J774A.1 macrophages were incubated with the antiserum-opsonized H. ducreyi lspA1 lspA2 mutant for 40 min at 37°C. (A) Extracellular bacteria were stained with Alexa 568 (red)-conjugated goat anti-rabbit IgG. (B) After fixing and permeabilization of the cells, intra- and extracellular bacteria were stained with Alexa 488 (green)-conjugated goat anti-rabbit IgG. The samples were examined by fluorescence microscopy.
    Figure Legend Snippet: Differential staining to distinguish bacteria in intra- and extracellular locations. Murine J774A.1 macrophages were incubated with the antiserum-opsonized H. ducreyi lspA1 lspA2 mutant for 40 min at 37°C. (A) Extracellular bacteria were stained with Alexa 568 (red)-conjugated goat anti-rabbit IgG. (B) After fixing and permeabilization of the cells, intra- and extracellular bacteria were stained with Alexa 488 (green)-conjugated goat anti-rabbit IgG. The samples were examined by fluorescence microscopy.

    Techniques Used: Staining, Incubation, Mutagenesis, Fluorescence, Microscopy

    9) Product Images from "The NFκB subunit RELA is a master transcriptional regulator of the committed epithelial-mesenchymal transition in airway epithelial cells"

    Article Title: The NFκB subunit RELA is a master transcriptional regulator of the committed epithelial-mesenchymal transition in airway epithelial cells

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.RA118.003662

    Kinetics of RELA translocation and activating phosphorylation. hSAECs were stimulated with TGFβ (10 ng/ml) for the indicated times (in hours). Untreated cells were negative controls (time 0). A , cells were fixed and stained with Alexa Fluor 488–phalloidin ( green ). Nuclei were counterstained with DAPI ( blue ) and imaged by CFM at 63× magnification. B , hSAECs were stained with rabbit anti-RELA Ab, and secondary detection was performed with Alexa Fluor 568–labeled goat anti-rabbit IgG ( red ). Nuclei were DAPI-counterstained and imaged by CFM. Top panel , Alexa Fluor 568 and DAPI merged image; bottom panel , Alexa Fluor 568 staining only. C , CFM for phospho-Ser-276 RELA. Top panel , Alexa Fluor 568 and DAPI merged image; bottom panel , Alexa Fluor 568 staining only. D and E , quantification of nuclear fluorescence intensity. Shown are scatter plots and median nuclear fluorescence intensities for RELA and phospho-Ser-276 RELA, respectively, for individual cell quantifications using ImageJ. AU , absorbance units. F , Western immunoblot for 65-kDa RELA ( top ). Lamin B was stained as a loading control ( bottom ). d , days. G , quantification of normalized fluorescence intensity of RELA signal. *, p
    Figure Legend Snippet: Kinetics of RELA translocation and activating phosphorylation. hSAECs were stimulated with TGFβ (10 ng/ml) for the indicated times (in hours). Untreated cells were negative controls (time 0). A , cells were fixed and stained with Alexa Fluor 488–phalloidin ( green ). Nuclei were counterstained with DAPI ( blue ) and imaged by CFM at 63× magnification. B , hSAECs were stained with rabbit anti-RELA Ab, and secondary detection was performed with Alexa Fluor 568–labeled goat anti-rabbit IgG ( red ). Nuclei were DAPI-counterstained and imaged by CFM. Top panel , Alexa Fluor 568 and DAPI merged image; bottom panel , Alexa Fluor 568 staining only. C , CFM for phospho-Ser-276 RELA. Top panel , Alexa Fluor 568 and DAPI merged image; bottom panel , Alexa Fluor 568 staining only. D and E , quantification of nuclear fluorescence intensity. Shown are scatter plots and median nuclear fluorescence intensities for RELA and phospho-Ser-276 RELA, respectively, for individual cell quantifications using ImageJ. AU , absorbance units. F , Western immunoblot for 65-kDa RELA ( top ). Lamin B was stained as a loading control ( bottom ). d , days. G , quantification of normalized fluorescence intensity of RELA signal. *, p

    Techniques Used: Translocation Assay, Staining, Labeling, Fluorescence, Western Blot

    Related Articles

    Staining:

    Article Title: The C-Terminal TDP-43 Fragments Have a High Aggregation Propensity and Harm Neurons by a Dominant-Negative Mechanism
    Article Snippet: .. Cells were then fixed and immunofluorescent staining was done using an antibody against activated caspase-3 (1∶200; Cell Signaling Technology) and an Alexa Fluor®568-conjugated goat anti-rabbit IgG (1∶400; Invitrogen). .. Immunofluorescence microscopy After fixation for 15 min at room temperature, cells were permeabilized by using 0.5% Triton in PBS for 5 min.

    Article Title: Inhibition of Phagocytosis by Haemophilus ducreyi Requires Expression of the LspA1 and LspA2 Proteins
    Article Snippet: .. To stain extracellular targets, the phagocytosis samples were covered for 1 h at room temperature with Alexa Fluor 568-conjugated goat anti-rabbit IgG (10 μg/ml; Molecular Probes). .. After four washes with PBS, the samples were fixed with 3.7% (vol/vol) formaldehyde and permeabilized by treatment with ice-cold methanol for 90 s. The samples were then covered for 1 h at room temperature with Alexa Fluor 488-conjugated goat anti-rabbit IgG (20 μg/ml; Molecular Probes) to stain both intracellular and extracellular targets.

    Incubation:

    Article Title: The C-Terminal TDP-43 Fragments Have a High Aggregation Propensity and Harm Neurons by a Dominant-Negative Mechanism
    Article Snippet: .. After overnight incubation, cells were washed and incubated with Alexa Fluor®568-conjugated goat anti-rabbit IgG (invitrogen) at room temperature for 1 hour. .. To stain Tubulin, a mouse monoclonal anti-α-tubulin (1∶100) and Alexa Fluor®488-conjugated goat anti-mouse IgG (invitrogen) were used.

    Labeling:

    Article Title: UDP-glucose dehydrogenase as a novel field-specific candidate biomarker of prostate cancer
    Article Snippet: .. Briefly, moist slides were soaked in Super Sensitive Wash Buffer™ (BioGenex, San Ramon, CA) for 15 min, blocked with 10% goat serum (Zymed Laboratories, Inc., San Francisco, CA) for 20 min, treated overnight at 4°C with an epitope-saturating dilution of anti-UGDH (1:500) and then labeled at room temperature for one hour with Alexa Fluor® 568 conjugated goat anti-rabbit IgG (200 μg/mL; Molecular Probes, Inc., Eugene, OR). ..

    Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 84
    Thermo Fisher goat anti rabbit igg alexafluor 568 conjugated secondary antibody
    Twinfilin regulates capping protein localization and dynamics. (A) Localization of EGFP-CP in wild-type and twf1/twf2-KO B16-F1 cells, where F-actin was visualized with <t>AlexaFluor-568</t> phalloidin. Panels in the middle and right are magnifications of lamellipodial regions highlighted in the whole cell images in left. Scale bars = 10 μ m. (B) Examples of line profiles generated across the center of lamellipodia as indicated with dotted lines. Data represent mean of 5 measurements of individual lamellipodia, with standard deviations shown. The ‘0 μ m’ value in x-axis is set to correspond the peak intensity of phalloidin. (C) The ratio of CP and F-actin co-localization widths were detected by measuring the width of localization at 50% of maximum intensity. Data points represent measurements from individual lamellipodia with mean values and standard deviations shown. Statistical significance was calculated with Student’s unpaired, two-tailed t-test. ****, p
    Goat Anti Rabbit Igg Alexafluor 568 Conjugated Secondary Antibody, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 84/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/goat anti rabbit igg alexafluor 568 conjugated secondary antibody/product/Thermo Fisher
    Average 84 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    goat anti rabbit igg alexafluor 568 conjugated secondary antibody - by Bioz Stars, 2020-08
    84/100 stars
      Buy from Supplier

    91
    Thermo Fisher alexa fluor 568 conjugated goat anti rabbit igg
    Twinfilin regulates capping protein localization and dynamics. (A) Localization of EGFP-CP in wild-type and twf1/twf2-KO B16-F1 cells, where F-actin was visualized with <t>AlexaFluor-568</t> phalloidin. Panels in the middle and right are magnifications of lamellipodial regions highlighted in the whole cell images in left. Scale bars = 10 μ m. (B) Examples of line profiles generated across the center of lamellipodia as indicated with dotted lines. Data represent mean of 5 measurements of individual lamellipodia, with standard deviations shown. The ‘0 μ m’ value in x-axis is set to correspond the peak intensity of phalloidin. (C) The ratio of CP and F-actin co-localization widths were detected by measuring the width of localization at 50% of maximum intensity. Data points represent measurements from individual lamellipodia with mean values and standard deviations shown. Statistical significance was calculated with Student’s unpaired, two-tailed t-test. ****, p
    Alexa Fluor 568 Conjugated Goat Anti Rabbit Igg, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 91/100, based on 130 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/alexa fluor 568 conjugated goat anti rabbit igg/product/Thermo Fisher
    Average 91 stars, based on 130 article reviews
    Price from $9.99 to $1999.99
    alexa fluor 568 conjugated goat anti rabbit igg - by Bioz Stars, 2020-08
    91/100 stars
      Buy from Supplier

    Image Search Results


    Twinfilin regulates capping protein localization and dynamics. (A) Localization of EGFP-CP in wild-type and twf1/twf2-KO B16-F1 cells, where F-actin was visualized with AlexaFluor-568 phalloidin. Panels in the middle and right are magnifications of lamellipodial regions highlighted in the whole cell images in left. Scale bars = 10 μ m. (B) Examples of line profiles generated across the center of lamellipodia as indicated with dotted lines. Data represent mean of 5 measurements of individual lamellipodia, with standard deviations shown. The ‘0 μ m’ value in x-axis is set to correspond the peak intensity of phalloidin. (C) The ratio of CP and F-actin co-localization widths were detected by measuring the width of localization at 50% of maximum intensity. Data points represent measurements from individual lamellipodia with mean values and standard deviations shown. Statistical significance was calculated with Student’s unpaired, two-tailed t-test. ****, p

    Journal: bioRxiv

    Article Title: Twinfilin uncaps filament barbed ends to promote turnover of lamellipodial actin networks

    doi: 10.1101/864769

    Figure Lengend Snippet: Twinfilin regulates capping protein localization and dynamics. (A) Localization of EGFP-CP in wild-type and twf1/twf2-KO B16-F1 cells, where F-actin was visualized with AlexaFluor-568 phalloidin. Panels in the middle and right are magnifications of lamellipodial regions highlighted in the whole cell images in left. Scale bars = 10 μ m. (B) Examples of line profiles generated across the center of lamellipodia as indicated with dotted lines. Data represent mean of 5 measurements of individual lamellipodia, with standard deviations shown. The ‘0 μ m’ value in x-axis is set to correspond the peak intensity of phalloidin. (C) The ratio of CP and F-actin co-localization widths were detected by measuring the width of localization at 50% of maximum intensity. Data points represent measurements from individual lamellipodia with mean values and standard deviations shown. Statistical significance was calculated with Student’s unpaired, two-tailed t-test. ****, p

    Article Snippet: Other antibodies used in the study were: Rabbit anti-twinfilin-2 antibody (Sigma-Aldrich #HPA053874, WB, 1:100), rabbit anti-CAPZß antibody (Sigma-Aldrich, #HPA031531, WB, 1:100), mouse anti-α-tubulin antibody (Sigma-Aldrich, #T5168, WB 1:10,000), mouse anti-ß-actin antibody (Sigma-Aldrich, #A5441, WB, 1:10,000), Rabbit anti-p34-Arc/ARPC2 (Merck Millipore, #07-227, dilution in immunofluorescence (IF), 1:200), goat anti-Rabbit IgG AlexaFluor-488 conjugated secondary antibody (Thermo Fisher, #A-11034, IF, 1:400), goat anti-Rabbit IgG AlexaFluor-568 conjugated secondary antibody (Thermo Fisher, #A-11011, IF, 1:400), goat anti-Rabbit IgG AlexaFluor-647 conjugated secondary antibody (Thermo Fisher, #A-32733, IF, 1:400), goat anti-Mouse IgG HRP conjugated secondary antibody (Thermo Fisher, #31430, WB, 1:10,000), goat anti-Rabbit IgG HRP conjugated secondary antibody (Thermo Fisher, #32460, WB, 1:1,000).

    Techniques: Generated, Two Tailed Test

    Examples of high-content and lamellipodia protrusion analysis. (A) Representative images of segmentation procedure in high-content image analysis. Wild-type and twinfilin-deficient B16-F1 cells were stained with DAPI and CellMask Deep Red to segment nuclei (outlined with blue) and cytoplasm (outlined with yellow). The Arp2/3-complex positive structures were detected with anti-p34 antibody staining and used as a mask for the Arp2/3-complex positive F-actin structures (the most-right panel). F-actin was stained with AlexaFluor-568 phalloidin. Cells touching the border of images were excluded from analysis. (B) A representative example of twf1/twf2-KO cell migrating on laminin coated glass imaged with DIC. Direction of migration is indicated with an arrow and kymographs were generated with line drawn across the lamellipodium as indicated with dotted red line. (C) Representative examples of kymographs generated from DIC time-lapse images of wild-type, twf1/twf2 knockout, and EGFP-TWF-1 rescue cells. Protrusions velocities were measured from the overall cell front protrusion as indicated with dotted red lines.

    Journal: bioRxiv

    Article Title: Twinfilin uncaps filament barbed ends to promote turnover of lamellipodial actin networks

    doi: 10.1101/864769

    Figure Lengend Snippet: Examples of high-content and lamellipodia protrusion analysis. (A) Representative images of segmentation procedure in high-content image analysis. Wild-type and twinfilin-deficient B16-F1 cells were stained with DAPI and CellMask Deep Red to segment nuclei (outlined with blue) and cytoplasm (outlined with yellow). The Arp2/3-complex positive structures were detected with anti-p34 antibody staining and used as a mask for the Arp2/3-complex positive F-actin structures (the most-right panel). F-actin was stained with AlexaFluor-568 phalloidin. Cells touching the border of images were excluded from analysis. (B) A representative example of twf1/twf2-KO cell migrating on laminin coated glass imaged with DIC. Direction of migration is indicated with an arrow and kymographs were generated with line drawn across the lamellipodium as indicated with dotted red line. (C) Representative examples of kymographs generated from DIC time-lapse images of wild-type, twf1/twf2 knockout, and EGFP-TWF-1 rescue cells. Protrusions velocities were measured from the overall cell front protrusion as indicated with dotted red lines.

    Article Snippet: Other antibodies used in the study were: Rabbit anti-twinfilin-2 antibody (Sigma-Aldrich #HPA053874, WB, 1:100), rabbit anti-CAPZß antibody (Sigma-Aldrich, #HPA031531, WB, 1:100), mouse anti-α-tubulin antibody (Sigma-Aldrich, #T5168, WB 1:10,000), mouse anti-ß-actin antibody (Sigma-Aldrich, #A5441, WB, 1:10,000), Rabbit anti-p34-Arc/ARPC2 (Merck Millipore, #07-227, dilution in immunofluorescence (IF), 1:200), goat anti-Rabbit IgG AlexaFluor-488 conjugated secondary antibody (Thermo Fisher, #A-11034, IF, 1:400), goat anti-Rabbit IgG AlexaFluor-568 conjugated secondary antibody (Thermo Fisher, #A-11011, IF, 1:400), goat anti-Rabbit IgG AlexaFluor-647 conjugated secondary antibody (Thermo Fisher, #A-32733, IF, 1:400), goat anti-Mouse IgG HRP conjugated secondary antibody (Thermo Fisher, #31430, WB, 1:10,000), goat anti-Rabbit IgG HRP conjugated secondary antibody (Thermo Fisher, #32460, WB, 1:1,000).

    Techniques: Staining, Migration, Generated, Knock-Out

    Representative images of wild-type and twinfilin knockout B16-F1 cells. (A) B16-F1 cells were stained with AlexaFluor-568 phalloidin (F-actin) and anti-p34 antibody (the Arp2/3 complex). Scale bars = 10 μ M. (B) Mean F-actin intensity in B16-F1 wild-type and twinfilin knockout cells. Number of measured cells were: B16-F1 wt = 1,958, twf1-KO-g1 = 1,045, twf2-KO-g3#1 = 1,285, twf1/2-KO-g3 = 1,265, twf1/2-KO-g4 = 1,707. (C) Mean F-actin intensity in the Arp2/3 complex positive regions of B16-F1 wild-type and knockout cells. The Arp2/3 complex positive regions were identified based on p34-antibody staining. Number of measured cells were: B16-F1 wt = 1,658, twf1-KO-g1 = 884, twf2-KO-g3#1 = 1,009, twf1/2-KO-g3 = 1,100, twf1/2-KO-g4 = 1157. Statistical significances in panels B and C were calculated with Mann-Whitney two-tailed test. ****, p

    Journal: bioRxiv

    Article Title: Twinfilin uncaps filament barbed ends to promote turnover of lamellipodial actin networks

    doi: 10.1101/864769

    Figure Lengend Snippet: Representative images of wild-type and twinfilin knockout B16-F1 cells. (A) B16-F1 cells were stained with AlexaFluor-568 phalloidin (F-actin) and anti-p34 antibody (the Arp2/3 complex). Scale bars = 10 μ M. (B) Mean F-actin intensity in B16-F1 wild-type and twinfilin knockout cells. Number of measured cells were: B16-F1 wt = 1,958, twf1-KO-g1 = 1,045, twf2-KO-g3#1 = 1,285, twf1/2-KO-g3 = 1,265, twf1/2-KO-g4 = 1,707. (C) Mean F-actin intensity in the Arp2/3 complex positive regions of B16-F1 wild-type and knockout cells. The Arp2/3 complex positive regions were identified based on p34-antibody staining. Number of measured cells were: B16-F1 wt = 1,658, twf1-KO-g1 = 884, twf2-KO-g3#1 = 1,009, twf1/2-KO-g3 = 1,100, twf1/2-KO-g4 = 1157. Statistical significances in panels B and C were calculated with Mann-Whitney two-tailed test. ****, p

    Article Snippet: Other antibodies used in the study were: Rabbit anti-twinfilin-2 antibody (Sigma-Aldrich #HPA053874, WB, 1:100), rabbit anti-CAPZß antibody (Sigma-Aldrich, #HPA031531, WB, 1:100), mouse anti-α-tubulin antibody (Sigma-Aldrich, #T5168, WB 1:10,000), mouse anti-ß-actin antibody (Sigma-Aldrich, #A5441, WB, 1:10,000), Rabbit anti-p34-Arc/ARPC2 (Merck Millipore, #07-227, dilution in immunofluorescence (IF), 1:200), goat anti-Rabbit IgG AlexaFluor-488 conjugated secondary antibody (Thermo Fisher, #A-11034, IF, 1:400), goat anti-Rabbit IgG AlexaFluor-568 conjugated secondary antibody (Thermo Fisher, #A-11011, IF, 1:400), goat anti-Rabbit IgG AlexaFluor-647 conjugated secondary antibody (Thermo Fisher, #A-32733, IF, 1:400), goat anti-Mouse IgG HRP conjugated secondary antibody (Thermo Fisher, #31430, WB, 1:10,000), goat anti-Rabbit IgG HRP conjugated secondary antibody (Thermo Fisher, #32460, WB, 1:1,000).

    Techniques: Knock-Out, Staining, MANN-WHITNEY, Two Tailed Test

    Knockout of twinfilins leads to abnormal F-actin accumulation in lamellipodia and perinuclear region. (A) Representative images of wild-type and twf1/twf2-KO mouse B16-F1 cells stained with AlexaFluor-568 phalloidin and anti-p34 antibody to visualize F-actin and the Arp2/3 complex, respectively. Scale bar = 10 μ m. (B) F-actin intensities in the cytoplasmic regions of wild-type, twf1/twf2-KO, and knockout cells expressing EGFP-TWF-1 measured by high-content image analysis. Number of cells analyzed were: B16-F1 wt = 4,875, twf1/twf2-KO-g3 = 5,731, twf1/twf2-KO-g3 + EGFP-TWF-1 = 197. (C) Lamellipodia protrusion velocities of wild-type, twf1/twf-2 knockout, and knockout cells expressing EGFP-TWF-1. Data represent individual cells with mean and standard deviations shown. Statistical significances in panels B and D were calculated with Mann-Whitney two-tailed test. ****, p

    Journal: bioRxiv

    Article Title: Twinfilin uncaps filament barbed ends to promote turnover of lamellipodial actin networks

    doi: 10.1101/864769

    Figure Lengend Snippet: Knockout of twinfilins leads to abnormal F-actin accumulation in lamellipodia and perinuclear region. (A) Representative images of wild-type and twf1/twf2-KO mouse B16-F1 cells stained with AlexaFluor-568 phalloidin and anti-p34 antibody to visualize F-actin and the Arp2/3 complex, respectively. Scale bar = 10 μ m. (B) F-actin intensities in the cytoplasmic regions of wild-type, twf1/twf2-KO, and knockout cells expressing EGFP-TWF-1 measured by high-content image analysis. Number of cells analyzed were: B16-F1 wt = 4,875, twf1/twf2-KO-g3 = 5,731, twf1/twf2-KO-g3 + EGFP-TWF-1 = 197. (C) Lamellipodia protrusion velocities of wild-type, twf1/twf-2 knockout, and knockout cells expressing EGFP-TWF-1. Data represent individual cells with mean and standard deviations shown. Statistical significances in panels B and D were calculated with Mann-Whitney two-tailed test. ****, p

    Article Snippet: Other antibodies used in the study were: Rabbit anti-twinfilin-2 antibody (Sigma-Aldrich #HPA053874, WB, 1:100), rabbit anti-CAPZß antibody (Sigma-Aldrich, #HPA031531, WB, 1:100), mouse anti-α-tubulin antibody (Sigma-Aldrich, #T5168, WB 1:10,000), mouse anti-ß-actin antibody (Sigma-Aldrich, #A5441, WB, 1:10,000), Rabbit anti-p34-Arc/ARPC2 (Merck Millipore, #07-227, dilution in immunofluorescence (IF), 1:200), goat anti-Rabbit IgG AlexaFluor-488 conjugated secondary antibody (Thermo Fisher, #A-11034, IF, 1:400), goat anti-Rabbit IgG AlexaFluor-568 conjugated secondary antibody (Thermo Fisher, #A-11011, IF, 1:400), goat anti-Rabbit IgG AlexaFluor-647 conjugated secondary antibody (Thermo Fisher, #A-32733, IF, 1:400), goat anti-Mouse IgG HRP conjugated secondary antibody (Thermo Fisher, #31430, WB, 1:10,000), goat anti-Rabbit IgG HRP conjugated secondary antibody (Thermo Fisher, #32460, WB, 1:1,000).

    Techniques: Knock-Out, Staining, Expressing, MANN-WHITNEY, Two Tailed Test