fluorescent dolichos biflorus agglutinin  (Vector Laboratories)


Bioz Verified Symbol Vector Laboratories is a verified supplier
Bioz Manufacturer Symbol Vector Laboratories manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 95
    Name:
    Fluorescein labeled Dolichos Biflorus Agglutinin DBA
    Description:
    Dolichos biflorus agglutinin DBA is a glycoprotein with a molecular weight of about 111 kDa and consists of 4 subunits of approximately equal size This lectin has a carbohydrate specificity toward α linked N acetylgalactosamine It has been used to establish secretor status in blood group A individuals by hemagglutination inhibition techniques and for blood typing This lectin has also been used as a general marker of developing renal collecting ducts Fluorescein labeled Dolichos biflorus agglutinin has an appropriate number of fluorochromes bound to provide the optimum staining characteristics for this lectin This conjugate is supplied essentially free of unconjugated fluorochromes The excitation maximum is at 495 nm and the emission maximum is at 515 nm Accompanying each fluorescent lectin is an analysis data sheet summarizing the results of our quality control tests and providing pertinent information on the product All of these reagents are supplied as solutions perserved with sodium azide Inhibiting Eluting Sugar 200 mM N acetylgalactosamine
    Catalog Number:
    FL-1031
    Price:
    None
    Size:
    2 mg
    Category:
    Proteins
    Buy from Supplier


    Structured Review

    Vector Laboratories fluorescent dolichos biflorus agglutinin
    Fluorescein labeled Dolichos Biflorus Agglutinin DBA
    Dolichos biflorus agglutinin DBA is a glycoprotein with a molecular weight of about 111 kDa and consists of 4 subunits of approximately equal size This lectin has a carbohydrate specificity toward α linked N acetylgalactosamine It has been used to establish secretor status in blood group A individuals by hemagglutination inhibition techniques and for blood typing This lectin has also been used as a general marker of developing renal collecting ducts Fluorescein labeled Dolichos biflorus agglutinin has an appropriate number of fluorochromes bound to provide the optimum staining characteristics for this lectin This conjugate is supplied essentially free of unconjugated fluorochromes The excitation maximum is at 495 nm and the emission maximum is at 515 nm Accompanying each fluorescent lectin is an analysis data sheet summarizing the results of our quality control tests and providing pertinent information on the product All of these reagents are supplied as solutions perserved with sodium azide Inhibiting Eluting Sugar 200 mM N acetylgalactosamine
    https://www.bioz.com/result/fluorescent dolichos biflorus agglutinin/product/Vector Laboratories
    Average 95 stars, based on 193 article reviews
    Price from $9.99 to $1999.99
    fluorescent dolichos biflorus agglutinin - by Bioz Stars, 2020-08
    95/100 stars

    Images

    1) Product Images from "Aberrant Glycosylation and Localization of Polycystin-1 Cause Polycystic Kidney in an AQP11 Knockout Model"

    Article Title: Aberrant Glycosylation and Localization of Polycystin-1 Cause Polycystic Kidney in an AQP11 Knockout Model

    Journal: Journal of the American Society of Nephrology : JASN

    doi: 10.1681/ASN.2013060614

    AQP11 protein expression in Tg AQP11 mouse kidney and the segmental origin of cysts in AQP11(−/−) mouse kidney. Immunofluorescence with HA antibody of 3-week-old Tg AQP11 and WT mouse kidneys: (A) cortex and (B) medulla. The immunostaining, image capture, and image processing were carried out under the same conditions. AQP11 was present only at the cortex. Scale bar, 20 μ m. (C) Double immunofluorescence with HA antibody and AQP1 antibody (proximal tubule marker), NCC antibody (distal tubule marker), or dolichos biflorus agglutinin (DBA; collecting tubule and collecting duct marker) in the kidney of a 3-week-old Tg AQP11 mouse. AQP11 was localized in the cytoplasm of the proximal tubule cells. Scale bar, 10 μ m. (D) Fluorescent staining with lotus tetragonolobus lectin (LTL; proximal tubule marker) and DBA in 3-week-old AQP11(−/−) mouse kidney. Segmental origin of cysts in AQP11(−/−) kidney was mainly proximal tubules. Scale bar, 50 μ m.
    Figure Legend Snippet: AQP11 protein expression in Tg AQP11 mouse kidney and the segmental origin of cysts in AQP11(−/−) mouse kidney. Immunofluorescence with HA antibody of 3-week-old Tg AQP11 and WT mouse kidneys: (A) cortex and (B) medulla. The immunostaining, image capture, and image processing were carried out under the same conditions. AQP11 was present only at the cortex. Scale bar, 20 μ m. (C) Double immunofluorescence with HA antibody and AQP1 antibody (proximal tubule marker), NCC antibody (distal tubule marker), or dolichos biflorus agglutinin (DBA; collecting tubule and collecting duct marker) in the kidney of a 3-week-old Tg AQP11 mouse. AQP11 was localized in the cytoplasm of the proximal tubule cells. Scale bar, 10 μ m. (D) Fluorescent staining with lotus tetragonolobus lectin (LTL; proximal tubule marker) and DBA in 3-week-old AQP11(−/−) mouse kidney. Segmental origin of cysts in AQP11(−/−) kidney was mainly proximal tubules. Scale bar, 50 μ m.

    Techniques Used: Expressing, Immunofluorescence, Immunostaining, Marker, Staining

    2) Product Images from "Toxoplasma gondii bradyzoites induce transcriptional changes to host cells and prevent IFNγ-mediated cell death"

    Article Title: Toxoplasma gondii bradyzoites induce transcriptional changes to host cells and prevent IFNγ-mediated cell death

    Journal: bioRxiv

    doi: 10.1101/669689

    MYR1 plays a role regulating host cell transcriptional changes in bradyzoites containing cells. ( A ) Differences in the expressional profile (Log 2 CPM) of MYR1, MYR2, and MYR3 between tachyzoites (24 hours) and bradyzoites (7 days in vitro ). Expression drops during bradyzoite stages for all proteins. ( B ) PruΔ ku80 and PruΔ ku80 MYR1-HA parasites were induced under alkaline conditions for 7 days before fixation. MYR1-HA (αHA; white) in bradyzoites (pLDH2-eGFP; green) is localised to the PV space and co-localises to cyst wall marker CST1 (αCST1; magenta). Brightness and contrast was edited on single colour channels prior to merging. ( C ) (i) WT and Δ myr1 parasites were fixed after 7 days of differentiation under alkaline conditions. Both WT and Δ myr1 were able to form intact cysts (DBA; green) containing health bradyzoites (αSRS9; magenta) and showed the presence of amylopectin granules (black arrows). Scale bar = 10μM; MYR, Myc Regulationr; PV, parasitophorous vacuole; DAPI, 4’,6-diamidino-2-phenylindole; DBA, fluorescein conjugated Dolichos biflorus agglutinin. Brightness and contrast was edited on single colour channels prior to merging. (ii) The number of bradyzoite containing cells after 7 days of differentiation between WT (Pru) and Δ myr1 was analysed by FACS (mean ± SD, n = 3 experiments, unpaired, two-sided Student’s t-test with Welch’s correction; **p=0.0058). (iii). The size of PruΔ ku80 Δ myr1 cysts were compared to WT by quantification of from immuno-fluorescence images (mean ± SD, n = 3 experiments, each experiment analysed on average between 20-40 bradyzoite cysts, unpaired, two-sided Student’s t-test with Mann-Whitney correction; p=0.156) ( D ) WT (Pru) and Δ myr1 inoculated human foreskin fibroblast (HFF) cells were FACS sorted into infected and uninfected samples before RNA extraction and sequencing (as per Fig. 1A ). Heat map of log 2 RPKM expression for the top 100 differentially regulated genes between WT bradyzoite infected and Δ myr1 bradyzoite infected cells. Expression has been scaled to have mean 0 and standard deviation 1 for each gene. In the absence of MYR1, bradyzoite specific host expression appears to somewhat mimic the bystander cell population (from both WT and Δ myr1 ). See also Figure S2 and Table S4 for gene list. ( E ) Venn diagram of bradyzoite WT infected vs uninfected DEGs (grey) and bradyzoite Δ myr1 infected vs uninfected DEGs (green); the number of up-regulated genes are identified in red and down-regulated genes in blue. Dotted lines indicated shared DEGs deemed as independent of MYR1.
    Figure Legend Snippet: MYR1 plays a role regulating host cell transcriptional changes in bradyzoites containing cells. ( A ) Differences in the expressional profile (Log 2 CPM) of MYR1, MYR2, and MYR3 between tachyzoites (24 hours) and bradyzoites (7 days in vitro ). Expression drops during bradyzoite stages for all proteins. ( B ) PruΔ ku80 and PruΔ ku80 MYR1-HA parasites were induced under alkaline conditions for 7 days before fixation. MYR1-HA (αHA; white) in bradyzoites (pLDH2-eGFP; green) is localised to the PV space and co-localises to cyst wall marker CST1 (αCST1; magenta). Brightness and contrast was edited on single colour channels prior to merging. ( C ) (i) WT and Δ myr1 parasites were fixed after 7 days of differentiation under alkaline conditions. Both WT and Δ myr1 were able to form intact cysts (DBA; green) containing health bradyzoites (αSRS9; magenta) and showed the presence of amylopectin granules (black arrows). Scale bar = 10μM; MYR, Myc Regulationr; PV, parasitophorous vacuole; DAPI, 4’,6-diamidino-2-phenylindole; DBA, fluorescein conjugated Dolichos biflorus agglutinin. Brightness and contrast was edited on single colour channels prior to merging. (ii) The number of bradyzoite containing cells after 7 days of differentiation between WT (Pru) and Δ myr1 was analysed by FACS (mean ± SD, n = 3 experiments, unpaired, two-sided Student’s t-test with Welch’s correction; **p=0.0058). (iii). The size of PruΔ ku80 Δ myr1 cysts were compared to WT by quantification of from immuno-fluorescence images (mean ± SD, n = 3 experiments, each experiment analysed on average between 20-40 bradyzoite cysts, unpaired, two-sided Student’s t-test with Mann-Whitney correction; p=0.156) ( D ) WT (Pru) and Δ myr1 inoculated human foreskin fibroblast (HFF) cells were FACS sorted into infected and uninfected samples before RNA extraction and sequencing (as per Fig. 1A ). Heat map of log 2 RPKM expression for the top 100 differentially regulated genes between WT bradyzoite infected and Δ myr1 bradyzoite infected cells. Expression has been scaled to have mean 0 and standard deviation 1 for each gene. In the absence of MYR1, bradyzoite specific host expression appears to somewhat mimic the bystander cell population (from both WT and Δ myr1 ). See also Figure S2 and Table S4 for gene list. ( E ) Venn diagram of bradyzoite WT infected vs uninfected DEGs (grey) and bradyzoite Δ myr1 infected vs uninfected DEGs (green); the number of up-regulated genes are identified in red and down-regulated genes in blue. Dotted lines indicated shared DEGs deemed as independent of MYR1.

    Techniques Used: In Vitro, Expressing, Marker, FACS, Fluorescence, MANN-WHITNEY, Infection, RNA Extraction, Sequencing, Standard Deviation

    3) Product Images from "Examination of a Virulence Mutant Uncovers the Ribosome Biogenesis Regulatory Protein of Toxoplasma gondii"

    Article Title: Examination of a Virulence Mutant Uncovers the Ribosome Biogenesis Regulatory Protein of Toxoplasma gondii

    Journal: The Journal of parasitology

    doi: 10.1645/GE-2741.1

    ( A ) C3-infected mice have reduced brain cyst burdens compared to the parental strain, PruΔ HPT (WT). At 22 days post-infection, brains of infected mice were collected, and cysts were quantified based on reactivity to Dolichos biflorus agglutinin
    Figure Legend Snippet: ( A ) C3-infected mice have reduced brain cyst burdens compared to the parental strain, PruΔ HPT (WT). At 22 days post-infection, brains of infected mice were collected, and cysts were quantified based on reactivity to Dolichos biflorus agglutinin

    Techniques Used: Infection, Mouse Assay

    4) Product Images from "Inhibitors of eIF2? Dephosphorylation Slow Replication and Stabilize Latency in Toxoplasma gondii"

    Article Title: Inhibitors of eIF2? Dephosphorylation Slow Replication and Stabilize Latency in Toxoplasma gondii

    Journal: Antimicrobial Agents and Chemotherapy

    doi: 10.1128/AAC.01899-12

    SAL and GA impede reactivation of latent bradyzoites in vitro . (A) The diagram outlines the experimental setup. ME49 tachyzoites (Tz) were differentiated into bradyzoite cysts (Bz) using alkaline (pH 8.1) medium for 7 days. The alkaline stress medium was then removed and replaced with normal medium (pH 7.2) containing indicated concentrations of SAL, GA, or vehicle (DMSO) for 3 days. Alkaline medium was retained in some samples as a positive control to prevent reactivation. Reactivation was assessed by counting Dolichos lectin-stained cysts in at least 25 random fields (B) or by counting reactivated tachyzoites present in culture medium (C). (B) The histogram shows the results from a representative experiment performed in triplicate and normalized to the number of cysts counted in the vehicle control. This experiment was repeated a total of three times, each with similar results. (C) The average for three independent experiments was normalized to the number of tachyzoites present in the vehicle control. In panels A and B, error bars indicate standard deviations and asterisks indicate a statistically significant difference relative to results for the vehicle control ( P
    Figure Legend Snippet: SAL and GA impede reactivation of latent bradyzoites in vitro . (A) The diagram outlines the experimental setup. ME49 tachyzoites (Tz) were differentiated into bradyzoite cysts (Bz) using alkaline (pH 8.1) medium for 7 days. The alkaline stress medium was then removed and replaced with normal medium (pH 7.2) containing indicated concentrations of SAL, GA, or vehicle (DMSO) for 3 days. Alkaline medium was retained in some samples as a positive control to prevent reactivation. Reactivation was assessed by counting Dolichos lectin-stained cysts in at least 25 random fields (B) or by counting reactivated tachyzoites present in culture medium (C). (B) The histogram shows the results from a representative experiment performed in triplicate and normalized to the number of cysts counted in the vehicle control. This experiment was repeated a total of three times, each with similar results. (C) The average for three independent experiments was normalized to the number of tachyzoites present in the vehicle control. In panels A and B, error bars indicate standard deviations and asterisks indicate a statistically significant difference relative to results for the vehicle control ( P

    Techniques Used: In Vitro, Positive Control, Staining

    5) Product Images from "Repair of injured proximal tubule does not involve specialized progenitors"

    Article Title: Repair of injured proximal tubule does not involve specialized progenitors

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    doi: 10.1073/pnas.1100629108

    Chains of proliferating cells in the upper papilla do not derive from LRCs. ( A ) Forty-eight hours after IRI, tubules can be seen in which nearly all epithelial cell nuclei are Ki67-positive (red). These tubules are located in the base of the papilla,
    Figure Legend Snippet: Chains of proliferating cells in the upper papilla do not derive from LRCs. ( A ) Forty-eight hours after IRI, tubules can be seen in which nearly all epithelial cell nuclei are Ki67-positive (red). These tubules are located in the base of the papilla,

    Techniques Used:

    6) Product Images from "Imaging mass spectrometry reveals direct albumin fragmentation within the diabetic kidney"

    Article Title: Imaging mass spectrometry reveals direct albumin fragmentation within the diabetic kidney

    Journal: Kidney international

    doi: 10.1016/j.kint.2018.01.040

    Examples of albumin fragment localization in diabetic renal tubules. PAS staining (right) and IMS (left) were performed on the same section; immunostaining and IMS were performed on serial sections. The resulting immunofluorescence and IMS images were co-registered. (A) Albumin fragments are not detected in glomeruli (marked by white-dashed circles). (B) Albumin fragments are localized to renal tubules. An example IMS ion image of the albumin peptide 25-48 acquired at 10 μm spatial resolution with corresponding H E stain. After the tissue was imaged, the matrix was removed with a series of ethanol washes and the tissue was H E stained. A zoomed in region is displayed in the right panel for clarity. (C) Albumin fragments (Left) co-localize with Lotus tetragonolobus lectin (LTL), a proximal tubule marker (Right). (D) Dolichos biflorus agglutinin (DBA), a distal tubule and collecting duct marker (Right) co-localizes with albumin fragments (Left). Scale bars for panels A, C and D = 200 μm. Scale bars for panel B= 50 μm (top panel) and 20 μm (bottom panel).
    Figure Legend Snippet: Examples of albumin fragment localization in diabetic renal tubules. PAS staining (right) and IMS (left) were performed on the same section; immunostaining and IMS were performed on serial sections. The resulting immunofluorescence and IMS images were co-registered. (A) Albumin fragments are not detected in glomeruli (marked by white-dashed circles). (B) Albumin fragments are localized to renal tubules. An example IMS ion image of the albumin peptide 25-48 acquired at 10 μm spatial resolution with corresponding H E stain. After the tissue was imaged, the matrix was removed with a series of ethanol washes and the tissue was H E stained. A zoomed in region is displayed in the right panel for clarity. (C) Albumin fragments (Left) co-localize with Lotus tetragonolobus lectin (LTL), a proximal tubule marker (Right). (D) Dolichos biflorus agglutinin (DBA), a distal tubule and collecting duct marker (Right) co-localizes with albumin fragments (Left). Scale bars for panels A, C and D = 200 μm. Scale bars for panel B= 50 μm (top panel) and 20 μm (bottom panel).

    Techniques Used: Staining, Immunostaining, Immunofluorescence, Marker

    7) Product Images from "FGF10 maintains distal lung bud epithelium and excessive signaling leads to progenitor state arrest, distalization, and goblet cell metaplasia"

    Article Title: FGF10 maintains distal lung bud epithelium and excessive signaling leads to progenitor state arrest, distalization, and goblet cell metaplasia

    Journal: BMC Developmental Biology

    doi: 10.1186/1471-213X-8-2

    Goblet cell metaplasia in the alveolar epithelium . A-B: IHC with Rhodamine-conjugated Dolichos Biflorus Agglutinin (DBA) and Beta-catenin. Goblet cells detected by their DBA reactivity were present in the alveolar epithelium of the transgenic mice (B), while no goblet cells were detected anywhere in the wildtype lungs (A). C-D: ISH using a Trefoil factor 3 probe. No Tff3 was detected in wildtype lung. Goblet cells in the transgenic lung were positive (D). E-F: IHC for pro-Surfactant protein C and fluorescein conjugated Dolichos Biflorus Agglutinin (DBA). Goblet cells did not co-express pro-Surfactant protein C.
    Figure Legend Snippet: Goblet cell metaplasia in the alveolar epithelium . A-B: IHC with Rhodamine-conjugated Dolichos Biflorus Agglutinin (DBA) and Beta-catenin. Goblet cells detected by their DBA reactivity were present in the alveolar epithelium of the transgenic mice (B), while no goblet cells were detected anywhere in the wildtype lungs (A). C-D: ISH using a Trefoil factor 3 probe. No Tff3 was detected in wildtype lung. Goblet cells in the transgenic lung were positive (D). E-F: IHC for pro-Surfactant protein C and fluorescein conjugated Dolichos Biflorus Agglutinin (DBA). Goblet cells did not co-express pro-Surfactant protein C.

    Techniques Used: Immunohistochemistry, Transgenic Assay, Mouse Assay, In Situ Hybridization

    8) Product Images from "Aberrant Regulation of Planar Cell Polarity in Polycystic Kidney Disease"

    Article Title: Aberrant Regulation of Planar Cell Polarity in Polycystic Kidney Disease

    Journal: Journal of the American Society of Nephrology : JASN

    doi: 10.1681/ASN.2010010127

    Tubular cell circumference (TCC) distribution is altered in distal precystic Pkd1 -inactivated tubules. (A through D) Graphs represent the distribution of TCC in proximal tubules (LTL; A and C) and distal tubules (DBA; B and D) in 2-week-old developing Mx1 -Cre.Pkd1 F/null or Mx1 -Cre.Pkd1 F/F precystic (LTL n = 310, DBA n = 225, four mice) and Pkd1 F/+ or Pkd1 F/F control (LTL n = 169, DBA n = 458, three mice) kidneys (A and B) and in 8-week-old injured Mx1 -Cre.Pkd1 F/F precystic (LTL n = 459, DBA n = 470, three mice) and Pkd1 F/F control (LTL n = 359, DBA n = 511, three mice) kidneys (C and D). (A and C) Note that there is no difference in TCC distribution in normal versus precystic proximal tubules. The TCC distribution in precystic collecting tubules shifts to the right. Insets are shown to demonstrate that only perfect epithelial cross-sections were evaluated.
    Figure Legend Snippet: Tubular cell circumference (TCC) distribution is altered in distal precystic Pkd1 -inactivated tubules. (A through D) Graphs represent the distribution of TCC in proximal tubules (LTL; A and C) and distal tubules (DBA; B and D) in 2-week-old developing Mx1 -Cre.Pkd1 F/null or Mx1 -Cre.Pkd1 F/F precystic (LTL n = 310, DBA n = 225, four mice) and Pkd1 F/+ or Pkd1 F/F control (LTL n = 169, DBA n = 458, three mice) kidneys (A and B) and in 8-week-old injured Mx1 -Cre.Pkd1 F/F precystic (LTL n = 459, DBA n = 470, three mice) and Pkd1 F/F control (LTL n = 359, DBA n = 511, three mice) kidneys (C and D). (A and C) Note that there is no difference in TCC distribution in normal versus precystic proximal tubules. The TCC distribution in precystic collecting tubules shifts to the right. Insets are shown to demonstrate that only perfect epithelial cross-sections were evaluated.

    Techniques Used: Mouse Assay

    9) Product Images from "Toxoplasma gondii tissue cyst purification using Percoll gradients"

    Article Title: Toxoplasma gondii tissue cyst purification using Percoll gradients

    Journal: Current protocols in microbiology

    doi: 10.1002/cpmc.30

    Imaging of purified tissue cysts A–C Assembly of the Cytospin holders to pellet the purified tissue cysts onto the slide surface. A . A glass slide and hole punched filter card are placed into the stainless steel clip holder. B . A sample funnel is placed into the holder such that the base of funnel aligns with the lower hole punch on the filter card. C . Assembled Cytospin holders. D–E . Cytospin holders are placed in the centrifuge and the sample added to the funnels using a micropipettor. F . Following centrifugation and the disassembly of the holder the slides are placed in a Coplin jar with fixative. G–I Imaging of a tissue cyst with Dolichos biflorus lectin (DBA-green) ( G ) and Concanavalin A (ConA-Red) ( H ) acquired on a Zeiss Axiophot stand using a 100× 1.4NA objective. The merged image ( I ) clearly shows the differential distribution of the glycans recognized by these lectins within the tissue cyst.
    Figure Legend Snippet: Imaging of purified tissue cysts A–C Assembly of the Cytospin holders to pellet the purified tissue cysts onto the slide surface. A . A glass slide and hole punched filter card are placed into the stainless steel clip holder. B . A sample funnel is placed into the holder such that the base of funnel aligns with the lower hole punch on the filter card. C . Assembled Cytospin holders. D–E . Cytospin holders are placed in the centrifuge and the sample added to the funnels using a micropipettor. F . Following centrifugation and the disassembly of the holder the slides are placed in a Coplin jar with fixative. G–I Imaging of a tissue cyst with Dolichos biflorus lectin (DBA-green) ( G ) and Concanavalin A (ConA-Red) ( H ) acquired on a Zeiss Axiophot stand using a 100× 1.4NA objective. The merged image ( I ) clearly shows the differential distribution of the glycans recognized by these lectins within the tissue cyst.

    Techniques Used: Imaging, Purification, Cross-linking Immunoprecipitation, Transferring, Centrifugation

    10) Product Images from "Targeting of Receptor for Advanced Glycation End Products Suppresses Cyst Growth in Polycystic Kidney Disease *"

    Article Title: Targeting of Receptor for Advanced Glycation End Products Suppresses Cyst Growth in Polycystic Kidney Disease *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.514166

    Silencing RAGE reduced the cystic area originating from each nephron segment in PC2R mice. A , kidney sections stained with tubule-specific markers. Kidney sections were stained with tubule-specific antibodies to classify cyst origin. The antibodies used were anti-DBA ( green ) for collecting duct staining, anti-LTA ( green ) for the proximal tubule, and anti-THP antibody ( green ) for the distal tubule. The nuclei were stained with DAPI ( blue ). Representative data are presented (magnification, ×100). Scale bars , 200 μm. B , statistical analysis of cystic area in each case. The IMA module of MetaMorph software was utilized to calculate cystic area (each > 40 cysts). Data are mean ± S.D. ( error bars ). *, p
    Figure Legend Snippet: Silencing RAGE reduced the cystic area originating from each nephron segment in PC2R mice. A , kidney sections stained with tubule-specific markers. Kidney sections were stained with tubule-specific antibodies to classify cyst origin. The antibodies used were anti-DBA ( green ) for collecting duct staining, anti-LTA ( green ) for the proximal tubule, and anti-THP antibody ( green ) for the distal tubule. The nuclei were stained with DAPI ( blue ). Representative data are presented (magnification, ×100). Scale bars , 200 μm. B , statistical analysis of cystic area in each case. The IMA module of MetaMorph software was utilized to calculate cystic area (each > 40 cysts). Data are mean ± S.D. ( error bars ). *, p

    Techniques Used: Mouse Assay, Staining, Software

    11) Product Images from "Toxoplasma TgATG9 is critical for autophagy and long-term persistence in tissue cysts"

    Article Title: Toxoplasma TgATG9 is critical for autophagy and long-term persistence in tissue cysts

    Journal: bioRxiv

    doi: 10.1101/2020.05.13.093401

    TgATG8 is required for efficient autophagosome production in T. gondii bradyzoites. (A) Stage-specific expression and fluorescent tagging of TgATG8 was achieved by insertion of the tachyzoite-specific TgSAG1 promoter and a GFP coding sequence immediately upstream of the TgATG8 gene. Site-specific insertion of the DHFR-pSAG1-mGFP repair template was performed by homology-directed repair. (B) PCR analysis confirmed the repair template had been inserted at the correct locus to generate a T. gondii strain in which TgATG8 expression was driven by the TgSAG1 promoter ( S/ATG8 ). Stage-specific expression of GFP-TgATG8 in tachyzoites (Tz) but not bradyzoites (Bz) was confirmed by immunofluorescence microscopy (C) and western blotting (D). GFP-TgATG8 signal overlapped with the apicoplast marker TgCPN60, indicating correct localization to the apicoplast. Dashed lines outline individual parasites in the tachyzoite images and the limits of cysts on the bradyzoite images. (E) Fluorescent staining of in vitro differentiated cysts with the bradyzoite specific marker TgBAG1 and the autolysosome detection reagent CytoID. Phase contrast images indicate the development of dark puncta in LHVS treated bradyzoites. Scale bar, 10 µm. (F). Viability of WT and S/ATG8 bradyzoites isolated after 28 days of differentiation, as indicated by their application to fresh monolayers for plaque formation.
    Figure Legend Snippet: TgATG8 is required for efficient autophagosome production in T. gondii bradyzoites. (A) Stage-specific expression and fluorescent tagging of TgATG8 was achieved by insertion of the tachyzoite-specific TgSAG1 promoter and a GFP coding sequence immediately upstream of the TgATG8 gene. Site-specific insertion of the DHFR-pSAG1-mGFP repair template was performed by homology-directed repair. (B) PCR analysis confirmed the repair template had been inserted at the correct locus to generate a T. gondii strain in which TgATG8 expression was driven by the TgSAG1 promoter ( S/ATG8 ). Stage-specific expression of GFP-TgATG8 in tachyzoites (Tz) but not bradyzoites (Bz) was confirmed by immunofluorescence microscopy (C) and western blotting (D). GFP-TgATG8 signal overlapped with the apicoplast marker TgCPN60, indicating correct localization to the apicoplast. Dashed lines outline individual parasites in the tachyzoite images and the limits of cysts on the bradyzoite images. (E) Fluorescent staining of in vitro differentiated cysts with the bradyzoite specific marker TgBAG1 and the autolysosome detection reagent CytoID. Phase contrast images indicate the development of dark puncta in LHVS treated bradyzoites. Scale bar, 10 µm. (F). Viability of WT and S/ATG8 bradyzoites isolated after 28 days of differentiation, as indicated by their application to fresh monolayers for plaque formation.

    Techniques Used: Expressing, Sequencing, Polymerase Chain Reaction, Immunofluorescence, Microscopy, Western Blot, Marker, Staining, In Vitro, Isolation

    Autophagy is required for bradyzoite viability and the persistence of tissue cysts. Quantification of bradyzoite viability by qPCR/plaque assay after differentiation media for one week followed by treatment with DMSO (vehicle control, blue) or LHVS (red) for a further one week (A) or two weeks (B). Data are from 3 biological replicates each with 3 technical replicates and are normalized to WT set at 100%. Bars represent mean ± S.E.M. (C) Viability of untreated bradyzoites after 2 weeks of differentiation in vitro . Each dot represents viability from one technical replicate. Data are merged from 4 biological replicates. Statistical comparisons were done using a Kruskal-Wallis test with Dunn’s multiple comparisons. Significance is indicated as ***, p
    Figure Legend Snippet: Autophagy is required for bradyzoite viability and the persistence of tissue cysts. Quantification of bradyzoite viability by qPCR/plaque assay after differentiation media for one week followed by treatment with DMSO (vehicle control, blue) or LHVS (red) for a further one week (A) or two weeks (B). Data are from 3 biological replicates each with 3 technical replicates and are normalized to WT set at 100%. Bars represent mean ± S.E.M. (C) Viability of untreated bradyzoites after 2 weeks of differentiation in vitro . Each dot represents viability from one technical replicate. Data are merged from 4 biological replicates. Statistical comparisons were done using a Kruskal-Wallis test with Dunn’s multiple comparisons. Significance is indicated as ***, p

    Techniques Used: Real-time Polymerase Chain Reaction, Plaque Assay, In Vitro

    TgATG9 is required for efficient autophagosome production in T. gondii bradyzoites. (A) Phase contrast images showing that the development of dark puncta in in vitro differentiated bradyzoites following LHVS treatment is dependent on the expression of TgATG9. Arrowheads indicate a subset of dark puncta. Scale bar, 10 µm. (B) Quantification of dark puncta size. Each dot represents the mean size of puncta within one cyst. Data are merged from 6 biological replicates, with a minimum of 22 cysts analyzed per sample type, per biological replicate and a minimum total of 242 cysts analyzed per sample type across all biological replicates. (C) CytoID staining of autolysosomes in in vitro differentiated bradyzoite cysts. Arrowheads indicate a subset of dark puncta and the corresponding CytoID positive structures. Scale bar, 5 µm. Quantification of the size (D) and number (E) of CytoID-positive structures in in vitro differentiated bradyzoites. Each dot represents the average puncta measurement within a single cyst. Data are merged from 3 biological replicates, with a minimum total of 81 cysts analyzed per sample type across 3 biological replicates. For panels B, D and E, bars represent mean ± S.D. Statistical comparisons were done using a Kruskal-Wallis test with Dunn’s multiple comparisons. Statistical significance is indicated as follows: **, p
    Figure Legend Snippet: TgATG9 is required for efficient autophagosome production in T. gondii bradyzoites. (A) Phase contrast images showing that the development of dark puncta in in vitro differentiated bradyzoites following LHVS treatment is dependent on the expression of TgATG9. Arrowheads indicate a subset of dark puncta. Scale bar, 10 µm. (B) Quantification of dark puncta size. Each dot represents the mean size of puncta within one cyst. Data are merged from 6 biological replicates, with a minimum of 22 cysts analyzed per sample type, per biological replicate and a minimum total of 242 cysts analyzed per sample type across all biological replicates. (C) CytoID staining of autolysosomes in in vitro differentiated bradyzoite cysts. Arrowheads indicate a subset of dark puncta and the corresponding CytoID positive structures. Scale bar, 5 µm. Quantification of the size (D) and number (E) of CytoID-positive structures in in vitro differentiated bradyzoites. Each dot represents the average puncta measurement within a single cyst. Data are merged from 3 biological replicates, with a minimum total of 81 cysts analyzed per sample type across 3 biological replicates. For panels B, D and E, bars represent mean ± S.D. Statistical comparisons were done using a Kruskal-Wallis test with Dunn’s multiple comparisons. Statistical significance is indicated as follows: **, p

    Techniques Used: In Vitro, Expressing, Staining

    Canonical autophagy is required for normal bradyzoite morphology and cell division. (A) Quantification of cyst size based on staining for the cyst wall with Dolichos lectin. Each dot represents the size of one cyst. Data are merged from 3 biological replicates, each with a minimum of 52 cysts analyzed per sample type, per biological replicate and a minimum total of 199 cysts analyzed per sample type across 3 biological replicates. Bars indicate mean ± S.D. Statistical comparisons were done using a Kruskal-Wallis test with Dunn’s multiple comparisons. Significance is indicated **, p
    Figure Legend Snippet: Canonical autophagy is required for normal bradyzoite morphology and cell division. (A) Quantification of cyst size based on staining for the cyst wall with Dolichos lectin. Each dot represents the size of one cyst. Data are merged from 3 biological replicates, each with a minimum of 52 cysts analyzed per sample type, per biological replicate and a minimum total of 199 cysts analyzed per sample type across 3 biological replicates. Bars indicate mean ± S.D. Statistical comparisons were done using a Kruskal-Wallis test with Dunn’s multiple comparisons. Significance is indicated **, p

    Techniques Used: Staining

    Autophagic structures and abnormal mitochondria in Δ atg9 bradyzoites. (A) TEM of Δ atg9 parasites showing a double membrane structure containing cytoplasmic components including ER. (B) Immunofluorescence imaging of bradyzoites stained with α-F 1 F 0 ATPase revealed an aberrant mitochondrial network in some Δ atg9 parasites. Scale bar, 10 µm. (C) TEM showing a normal mitochondrion in WT bradyzoites. (D) TEM of Δ atg9 bradyzoites presenting thin mitochondria (m) in a horseshoe conformation with bulbous ends, wherein cristae can be seen. Nucleus (n) is denoted. (E) TEM of Δ atg9 parasites revealing mitochondrial profiles (m) enveloping many organelles, including endoplasmic reticulum (ER), dense granules (DG), micronemes (mi), mitochondria (m) and lipid droplets (LD). (F) Examples of ER and mitochondrial section wrapped by the mitochondrion after bradyzoite treatment with LHVS. Inset of the lower panel illustrates the 4 membranes observed in such structures. All TEM scale bars are 500 nm.
    Figure Legend Snippet: Autophagic structures and abnormal mitochondria in Δ atg9 bradyzoites. (A) TEM of Δ atg9 parasites showing a double membrane structure containing cytoplasmic components including ER. (B) Immunofluorescence imaging of bradyzoites stained with α-F 1 F 0 ATPase revealed an aberrant mitochondrial network in some Δ atg9 parasites. Scale bar, 10 µm. (C) TEM showing a normal mitochondrion in WT bradyzoites. (D) TEM of Δ atg9 bradyzoites presenting thin mitochondria (m) in a horseshoe conformation with bulbous ends, wherein cristae can be seen. Nucleus (n) is denoted. (E) TEM of Δ atg9 parasites revealing mitochondrial profiles (m) enveloping many organelles, including endoplasmic reticulum (ER), dense granules (DG), micronemes (mi), mitochondria (m) and lipid droplets (LD). (F) Examples of ER and mitochondrial section wrapped by the mitochondrion after bradyzoite treatment with LHVS. Inset of the lower panel illustrates the 4 membranes observed in such structures. All TEM scale bars are 500 nm.

    Techniques Used: Transmission Electron Microscopy, Immunofluorescence, Imaging, Staining

    12) Product Images from "Toxoplasma gondii tissue cyst purification using Percoll gradients"

    Article Title: Toxoplasma gondii tissue cyst purification using Percoll gradients

    Journal: Current protocols in microbiology

    doi: 10.1002/cpmc.30

    Imaging of purified tissue cysts A–C Assembly of the Cytospin holders to pellet the purified tissue cysts onto the slide surface. A . A glass slide and hole punched filter card are placed into the stainless steel clip holder. B . A sample funnel is placed into the holder such that the base of funnel aligns with the lower hole punch on the filter card. C . Assembled Cytospin holders. D–E . Cytospin holders are placed in the centrifuge and the sample added to the funnels using a micropipettor. F . Following centrifugation and the disassembly of the holder the slides are placed in a Coplin jar with fixative. G–I Imaging of a tissue cyst with Dolichos biflorus lectin (DBA-green) ( G ) and Concanavalin A (ConA-Red) ( H ) acquired on a Zeiss Axiophot stand using a 100× 1.4NA objective. The merged image ( I ) clearly shows the differential distribution of the glycans recognized by these lectins within the tissue cyst.
    Figure Legend Snippet: Imaging of purified tissue cysts A–C Assembly of the Cytospin holders to pellet the purified tissue cysts onto the slide surface. A . A glass slide and hole punched filter card are placed into the stainless steel clip holder. B . A sample funnel is placed into the holder such that the base of funnel aligns with the lower hole punch on the filter card. C . Assembled Cytospin holders. D–E . Cytospin holders are placed in the centrifuge and the sample added to the funnels using a micropipettor. F . Following centrifugation and the disassembly of the holder the slides are placed in a Coplin jar with fixative. G–I Imaging of a tissue cyst with Dolichos biflorus lectin (DBA-green) ( G ) and Concanavalin A (ConA-Red) ( H ) acquired on a Zeiss Axiophot stand using a 100× 1.4NA objective. The merged image ( I ) clearly shows the differential distribution of the glycans recognized by these lectins within the tissue cyst.

    Techniques Used: Imaging, Purification, Cross-linking Immunoprecipitation, Transferring, Centrifugation

    13) Product Images from "Spliced XBP1 Rescues Renal Interstitial Inflammation Due to Loss of Sec63 in Collecting Ducts"

    Article Title: Spliced XBP1 Rescues Renal Interstitial Inflammation Due to Loss of Sec63 in Collecting Ducts

    Journal: Journal of the American Society of Nephrology : JASN

    doi: 10.1681/ASN.2018060614

    Macrophage infiltrates in kidneys with dual inactivation of Sec63 and Xbp1 . (A–I) Immunocytochemical analysis of (A–C) WT, (D–F) SKO, and (G–I) DKO kidneys at P35. (A, D, and G) show macrophages (F4/80; red) and proximal tubules (LTL; green); (B, E, and H) macrophages (red) and thick ascending limbs of the loop of Henle (Tamm–Horsfall protein [THP]; green); and (C, F, and I) macrophages (red) and collecting duct ( Dolichos biflorus agglutinin [DBA]; green) in the outer medulla. (G–I) The macrophage infiltrates are much more prominent in DKO kidneys. (H) The inflamed DKO mTAL contains urinary THP casts (arrows). (I) Macrophages are found infiltrating around the collecting duct tubules (“tubulitis”; arrowheads). Nuclei are labeled with Hoechst, blue. Scale bar, 50 µ m. (J) Gene transcript expression by quantitative RT-PCR for F4/80 and monocyte chemoattractant protein 1 (MCP1) indicates significantly increased mRNA levels in DKO kidneys compared with WT and SKO beginning at P35 (F4/80, n =3 and MCP1, n =6 at each time point for each genotype). Results are shown as mean ± SEM (ANOVA). *** P
    Figure Legend Snippet: Macrophage infiltrates in kidneys with dual inactivation of Sec63 and Xbp1 . (A–I) Immunocytochemical analysis of (A–C) WT, (D–F) SKO, and (G–I) DKO kidneys at P35. (A, D, and G) show macrophages (F4/80; red) and proximal tubules (LTL; green); (B, E, and H) macrophages (red) and thick ascending limbs of the loop of Henle (Tamm–Horsfall protein [THP]; green); and (C, F, and I) macrophages (red) and collecting duct ( Dolichos biflorus agglutinin [DBA]; green) in the outer medulla. (G–I) The macrophage infiltrates are much more prominent in DKO kidneys. (H) The inflamed DKO mTAL contains urinary THP casts (arrows). (I) Macrophages are found infiltrating around the collecting duct tubules (“tubulitis”; arrowheads). Nuclei are labeled with Hoechst, blue. Scale bar, 50 µ m. (J) Gene transcript expression by quantitative RT-PCR for F4/80 and monocyte chemoattractant protein 1 (MCP1) indicates significantly increased mRNA levels in DKO kidneys compared with WT and SKO beginning at P35 (F4/80, n =3 and MCP1, n =6 at each time point for each genotype). Results are shown as mean ± SEM (ANOVA). *** P

    Techniques Used: Labeling, Expressing, Quantitative RT-PCR

    14) Product Images from "Periostin overexpression in collecting ducts accelerates renal cyst growth and fibrosis in polycystic kidney disease"

    Article Title: Periostin overexpression in collecting ducts accelerates renal cyst growth and fibrosis in polycystic kidney disease

    Journal: American Journal of Physiology - Renal Physiology

    doi: 10.1152/ajprenal.00246.2018

    Collecting duct (CD)-specific expression of periostin increases renal type I collagen and interstitial fibrosis in pcy mice. Representative sections from pcy ( A ) and Postn CD pcy ( B ) mice stained with antibodies to type I collagen (red) and Dolichos biflorus agglutinin (DBA; green). C : bar graph (means ± SE) represents the percentage of entire tissue sections that stained for type I collagen ( n = 4), normalized to total surface area (SA). Representative sections from pcy ( D ) and Postn CD pcy ( E ). F : tissue sections were scored by a naïve observer assigning a percentage of fibrotic/edematous cortical area per total area of the cortex. Bar graph represents fibrosis as a percentage of total sectional area. * P
    Figure Legend Snippet: Collecting duct (CD)-specific expression of periostin increases renal type I collagen and interstitial fibrosis in pcy mice. Representative sections from pcy ( A ) and Postn CD pcy ( B ) mice stained with antibodies to type I collagen (red) and Dolichos biflorus agglutinin (DBA; green). C : bar graph (means ± SE) represents the percentage of entire tissue sections that stained for type I collagen ( n = 4), normalized to total surface area (SA). Representative sections from pcy ( D ) and Postn CD pcy ( E ). F : tissue sections were scored by a naïve observer assigning a percentage of fibrotic/edematous cortical area per total area of the cortex. Bar graph represents fibrosis as a percentage of total sectional area. * P

    Techniques Used: Expressing, Mouse Assay, Staining

    15) Product Images from "Developmental change in translation initiation alters the localization of a common microbial protein necessary for Toxoplasma chronic infection"

    Article Title: Developmental change in translation initiation alters the localization of a common microbial protein necessary for Toxoplasma chronic infection

    Journal: Molecular microbiology

    doi: 10.1111/mmi.13538

    TgBCP1 has punctate localization within tissue culture tachyzoite and bradyzoite parasites C3 and 38C3 parasites were grown for either 36 hours in tachyzoite or 5 days in bradyzoite conditions. Fixed and permeabilized cells were incubated with anti-TgBCP1 antibody (green) and for the red channel either dense granule protein 2 (GRA2) or Na(+)/H(+) exchanger (NHE3) for tachyzoites and Dolichos biflorus agglutinin (DBA) or bradyzoite heat-shock protein (BAG) for bradyzoites. Cells were mounted with DNA binding 4–6’diamidino-2-phenylindole (DAPI) to stain the nucleus of the parasites and host cells blue and imaged using differential interference contrast (DIC).
    Figure Legend Snippet: TgBCP1 has punctate localization within tissue culture tachyzoite and bradyzoite parasites C3 and 38C3 parasites were grown for either 36 hours in tachyzoite or 5 days in bradyzoite conditions. Fixed and permeabilized cells were incubated with anti-TgBCP1 antibody (green) and for the red channel either dense granule protein 2 (GRA2) or Na(+)/H(+) exchanger (NHE3) for tachyzoites and Dolichos biflorus agglutinin (DBA) or bradyzoite heat-shock protein (BAG) for bradyzoites. Cells were mounted with DNA binding 4–6’diamidino-2-phenylindole (DAPI) to stain the nucleus of the parasites and host cells blue and imaged using differential interference contrast (DIC).

    Techniques Used: Incubation, Binding Assay, Staining

    16) Product Images from "Targeting of Receptor for Advanced Glycation End Products Suppresses Cyst Growth in Polycystic Kidney Disease *"

    Article Title: Targeting of Receptor for Advanced Glycation End Products Suppresses Cyst Growth in Polycystic Kidney Disease *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.514166

    Silencing RAGE reduced the cystic area originating from each nephron segment in PC2R mice. A , kidney sections stained with tubule-specific markers. Kidney sections were stained with tubule-specific antibodies to classify cyst origin. The antibodies used were anti-DBA ( green ) for collecting duct staining, anti-LTA ( green ) for the proximal tubule, and anti-THP antibody ( green ) for the distal tubule. The nuclei were stained with DAPI ( blue ). Representative data are presented (magnification, ×100). Scale bars , 200 μm. B , statistical analysis of cystic area in each case. The IMA module of MetaMorph software was utilized to calculate cystic area (each > 40 cysts). Data are mean ± S.D. ( error bars ). *, p
    Figure Legend Snippet: Silencing RAGE reduced the cystic area originating from each nephron segment in PC2R mice. A , kidney sections stained with tubule-specific markers. Kidney sections were stained with tubule-specific antibodies to classify cyst origin. The antibodies used were anti-DBA ( green ) for collecting duct staining, anti-LTA ( green ) for the proximal tubule, and anti-THP antibody ( green ) for the distal tubule. The nuclei were stained with DAPI ( blue ). Representative data are presented (magnification, ×100). Scale bars , 200 μm. B , statistical analysis of cystic area in each case. The IMA module of MetaMorph software was utilized to calculate cystic area (each > 40 cysts). Data are mean ± S.D. ( error bars ). *, p

    Techniques Used: Mouse Assay, Staining, Software

    17) Product Images from "A novel model of autosomal recessive polycystic kidney questions the role of the Fibrocystin C-terminus in disease mechanism"

    Article Title: A novel model of autosomal recessive polycystic kidney questions the role of the Fibrocystin C-terminus in disease mechanism

    Journal: Kidney international

    doi: 10.1016/j.kint.2017.04.027

    Immunolocalization of endogenous FPC-HA in adult kidney, liver and pancreas ( a–h ) Adult kidney cryosections from Pkhd1 Flox67HA and Pkhd1 wt mice stained with anti-HA (red), Dolichos biflorus agglutinin (DBA) (green in panels a–d ) and anti-Na-K-Cl cotransporter 2 (NKCC2), (green in panels e–h ). ( i–p ) Cryosections from Pkhd1 Flox67HA and Pkhd1 wt Adult liver ( i–l ) and pancreas ( m–p ) stained with anti-HA (red) and ck19 (cytokeratin 19) (green). Arrows in c , g, k and o show accumulation of FPC-HA in sub-apical vesicle-like structures. Original magnification × 40 (scale bar 20 µm) in a , b , e , f , i , j , m , n . Original magnification × 63 (scale bar 2 µm) in c , g , k , o . The dotted lines and squares indicate corresponding enlarged areas. Dotted lines in i and j outline the portal vein.
    Figure Legend Snippet: Immunolocalization of endogenous FPC-HA in adult kidney, liver and pancreas ( a–h ) Adult kidney cryosections from Pkhd1 Flox67HA and Pkhd1 wt mice stained with anti-HA (red), Dolichos biflorus agglutinin (DBA) (green in panels a–d ) and anti-Na-K-Cl cotransporter 2 (NKCC2), (green in panels e–h ). ( i–p ) Cryosections from Pkhd1 Flox67HA and Pkhd1 wt Adult liver ( i–l ) and pancreas ( m–p ) stained with anti-HA (red) and ck19 (cytokeratin 19) (green). Arrows in c , g, k and o show accumulation of FPC-HA in sub-apical vesicle-like structures. Original magnification × 40 (scale bar 20 µm) in a , b , e , f , i , j , m , n . Original magnification × 63 (scale bar 2 µm) in c , g , k , o . The dotted lines and squares indicate corresponding enlarged areas. Dotted lines in i and j outline the portal vein.

    Techniques Used: Mouse Assay, Staining

    18) Product Images from "Isolation, culture and genetic manipulation of mouse pancreatic ductal cells"

    Article Title: Isolation, culture and genetic manipulation of mouse pancreatic ductal cells

    Journal: Nature protocols

    doi: 10.1038/nprot.2013.079

    Cells in 2D culture. Phase-contrast photomicrograph of DBA lectin–separated cells cultured on a collagen layer (2D) for 7 d. ( a ) DBA lectin–positive cells form epithelial colonies. ( b ) Of all the cell types in the DBA lectin–negative
    Figure Legend Snippet: Cells in 2D culture. Phase-contrast photomicrograph of DBA lectin–separated cells cultured on a collagen layer (2D) for 7 d. ( a ) DBA lectin–positive cells form epithelial colonies. ( b ) Of all the cell types in the DBA lectin–negative

    Techniques Used: Cell Culture

    Ratio of relative gene expression in DBA lectin-positive and DBA lectin–negative cells. Ductal marker genes ( Krt19 , Sox9 and Hnf1b ) are enriched, whereas acinar ( Ptf1a , Cela1 , Amy2a , Bhlha15 ) and endocrine ( Ins1, Neurod1, Neurog3 ) marker transcripts
    Figure Legend Snippet: Ratio of relative gene expression in DBA lectin-positive and DBA lectin–negative cells. Ductal marker genes ( Krt19 , Sox9 and Hnf1b ) are enriched, whereas acinar ( Ptf1a , Cela1 , Amy2a , Bhlha15 ) and endocrine ( Ins1, Neurod1, Neurog3 ) marker transcripts

    Techniques Used: Expressing, Marker

    DBA lectin distribution in the normal pancreas and disease. ( a ) Immunofluorescence of DBA lectin-positive (green) structures in a normal adult pancreas. ( b , c ) Acute cerulein-induced pancreatitis (day 3) ( b ) and Kras -driven neoplasia ( Pdx1cre ; Kras G12D
    Figure Legend Snippet: DBA lectin distribution in the normal pancreas and disease. ( a ) Immunofluorescence of DBA lectin-positive (green) structures in a normal adult pancreas. ( b , c ) Acute cerulein-induced pancreatitis (day 3) ( b ) and Kras -driven neoplasia ( Pdx1cre ; Kras G12D

    Techniques Used: Immunofluorescence

    19) Product Images from "Characterization and Quenching of Autofluorescence in Piglet Testis Tissue and Cells"

    Article Title: Characterization and Quenching of Autofluorescence in Piglet Testis Tissue and Cells

    Journal: Anatomy Research International

    doi: 10.1155/2012/820120

    Identification of gonocytes with DBA staining, following the masking of autofluorescence by Sudan Black B in situ and in vitro . Piglet testis tissue sections (a, b) and dissociated cells (c, d) were stained with FITC-labeled lectin DBA and DAPI, followed by Sudan Black B staining and imaging with a confocal laser scanning microscope with brightfield overlay. Scale bars, 100 μ m.
    Figure Legend Snippet: Identification of gonocytes with DBA staining, following the masking of autofluorescence by Sudan Black B in situ and in vitro . Piglet testis tissue sections (a, b) and dissociated cells (c, d) were stained with FITC-labeled lectin DBA and DAPI, followed by Sudan Black B staining and imaging with a confocal laser scanning microscope with brightfield overlay. Scale bars, 100 μ m.

    Techniques Used: Staining, In Situ, In Vitro, Labeling, Imaging, Laser-Scanning Microscopy

    20) Product Images from "Spliced XBP1 Rescues Renal Interstitial Inflammation Due to Loss of Sec63 in Collecting Ducts"

    Article Title: Spliced XBP1 Rescues Renal Interstitial Inflammation Due to Loss of Sec63 in Collecting Ducts

    Journal: Journal of the American Society of Nephrology : JASN

    doi: 10.1681/ASN.2018060614

    Macrophage infiltrates in kidneys with dual inactivation of Sec63 and Xbp1 . (A–I) Immunocytochemical analysis of (A–C) WT, (D–F) SKO, and (G–I) DKO kidneys at P35. (A, D, and G) show macrophages (F4/80; red) and proximal tubules (LTL; green); (B, E, and H) macrophages (red) and thick ascending limbs of the loop of Henle (Tamm–Horsfall protein [THP]; green); and (C, F, and I) macrophages (red) and collecting duct ( Dolichos biflorus agglutinin [DBA]; green) in the outer medulla. (G–I) The macrophage infiltrates are much more prominent in DKO kidneys. (H) The inflamed DKO mTAL contains urinary THP casts (arrows). (I) Macrophages are found infiltrating around the collecting duct tubules (“tubulitis”; arrowheads). Nuclei are labeled with Hoechst, blue. Scale bar, 50 µ m. (J) Gene transcript expression by quantitative RT-PCR for F4/80 and monocyte chemoattractant protein 1 (MCP1) indicates significantly increased mRNA levels in DKO kidneys compared with WT and SKO beginning at P35 (F4/80, n =3 and MCP1, n =6 at each time point for each genotype). Results are shown as mean ± SEM (ANOVA). *** P
    Figure Legend Snippet: Macrophage infiltrates in kidneys with dual inactivation of Sec63 and Xbp1 . (A–I) Immunocytochemical analysis of (A–C) WT, (D–F) SKO, and (G–I) DKO kidneys at P35. (A, D, and G) show macrophages (F4/80; red) and proximal tubules (LTL; green); (B, E, and H) macrophages (red) and thick ascending limbs of the loop of Henle (Tamm–Horsfall protein [THP]; green); and (C, F, and I) macrophages (red) and collecting duct ( Dolichos biflorus agglutinin [DBA]; green) in the outer medulla. (G–I) The macrophage infiltrates are much more prominent in DKO kidneys. (H) The inflamed DKO mTAL contains urinary THP casts (arrows). (I) Macrophages are found infiltrating around the collecting duct tubules (“tubulitis”; arrowheads). Nuclei are labeled with Hoechst, blue. Scale bar, 50 µ m. (J) Gene transcript expression by quantitative RT-PCR for F4/80 and monocyte chemoattractant protein 1 (MCP1) indicates significantly increased mRNA levels in DKO kidneys compared with WT and SKO beginning at P35 (F4/80, n =3 and MCP1, n =6 at each time point for each genotype). Results are shown as mean ± SEM (ANOVA). *** P

    Techniques Used: Labeling, Expressing, Quantitative RT-PCR

    Myofibroblasts coexist with macrophages in the kidneys of mice of double inactivation with Sec63 and Xbp1 . (A–I) Immunocytochemical analysis of F4/80 (green) and (A, D, and G) α -smooth muscle actin ( α SMA; red), (B, E, and H) FSP1 (red), and (C, F, and I) PDGFR β (red) in kidneys with the indicated genotypes at P49. (G) α SMA-positive, (H) FSP1-positive, and (I) PDGFR β -positive fibroblasts coexist with macrophages in DKO kidneys. Nuclei are labeled with Hoechst, blue. Scale bar, 50 µ m. (J) Representative immunoblots (top) and aggregate densitometric quantification from kidney lysates (bottom) show that levels of α SMA, FSP1, and PDGFR β are significantly increased in DKO compared with WT and SKO kidneys at P49. Densitometry is normalized to HSP90, which serves as loading control. n =3 per genotype; results are shown as mean ± SEM (ANOVA). *** P
    Figure Legend Snippet: Myofibroblasts coexist with macrophages in the kidneys of mice of double inactivation with Sec63 and Xbp1 . (A–I) Immunocytochemical analysis of F4/80 (green) and (A, D, and G) α -smooth muscle actin ( α SMA; red), (B, E, and H) FSP1 (red), and (C, F, and I) PDGFR β (red) in kidneys with the indicated genotypes at P49. (G) α SMA-positive, (H) FSP1-positive, and (I) PDGFR β -positive fibroblasts coexist with macrophages in DKO kidneys. Nuclei are labeled with Hoechst, blue. Scale bar, 50 µ m. (J) Representative immunoblots (top) and aggregate densitometric quantification from kidney lysates (bottom) show that levels of α SMA, FSP1, and PDGFR β are significantly increased in DKO compared with WT and SKO kidneys at P49. Densitometry is normalized to HSP90, which serves as loading control. n =3 per genotype; results are shown as mean ± SEM (ANOVA). *** P

    Techniques Used: Mouse Assay, Labeling, Western Blot

    21) Product Images from "RNA helicase p68 inhibits the transcription and post-transcription of Pkd1 in ADPKD"

    Article Title: RNA helicase p68 inhibits the transcription and post-transcription of Pkd1 in ADPKD

    Journal: Theranostics

    doi: 10.7150/thno.47315

    p68 regulates Pkd1 expression by miR-182-5p mediated post-transcriptional repression. ( A ) The interaction between Drosha and p53 (top panel) and between Drosha and p68 (middle panel) was detected in mIMCD3 cells with anti-Drosha antibody followed by blotting with p68 and p53. IgG was used as a negative control. ( B to D ) The expression of miR-182-5p, miR-17 and miR-200c, pre-miR-182-5p, pre-miR-17 and pre-miR-200c, and pri-miR-182-5p, pri-miR-17 and pri-miR-200c in mIMCD3 cells transfected with p68 or control siRNA examined by qRT-PCR analysis. ( E , F ) The levels of Pkd1 mRNA and PC1 protein in mIMCD3 cells treated with a miR-182-5p inhibitor examined by qRT-PCR and Western blot analysis. ( G, H ) The levels of Pkd1 mRNA and protein were examined by qRT-PCR ( G ) and Western blot analysis ( H ) in mIMCD3 cells treated with a miR-182-5p mimics.
    Figure Legend Snippet: p68 regulates Pkd1 expression by miR-182-5p mediated post-transcriptional repression. ( A ) The interaction between Drosha and p53 (top panel) and between Drosha and p68 (middle panel) was detected in mIMCD3 cells with anti-Drosha antibody followed by blotting with p68 and p53. IgG was used as a negative control. ( B to D ) The expression of miR-182-5p, miR-17 and miR-200c, pre-miR-182-5p, pre-miR-17 and pre-miR-200c, and pri-miR-182-5p, pri-miR-17 and pri-miR-200c in mIMCD3 cells transfected with p68 or control siRNA examined by qRT-PCR analysis. ( E , F ) The levels of Pkd1 mRNA and PC1 protein in mIMCD3 cells treated with a miR-182-5p inhibitor examined by qRT-PCR and Western blot analysis. ( G, H ) The levels of Pkd1 mRNA and protein were examined by qRT-PCR ( G ) and Western blot analysis ( H ) in mIMCD3 cells treated with a miR-182-5p mimics.

    Techniques Used: Expressing, Negative Control, Transfection, Quantitative RT-PCR, Western Blot

    22) Product Images from "Periostin overexpression in collecting ducts accelerates renal cyst growth and fibrosis in polycystic kidney disease"

    Article Title: Periostin overexpression in collecting ducts accelerates renal cyst growth and fibrosis in polycystic kidney disease

    Journal: American Journal of Physiology - Renal Physiology

    doi: 10.1152/ajprenal.00246.2018

    Collecting duct (CD)-specific expression of periostin increases renal type I collagen and interstitial fibrosis in pcy mice. Representative sections from pcy ( A ) and Postn CD pcy ( B ) mice stained with antibodies to type I collagen (red) and Dolichos biflorus agglutinin (DBA; green). C : bar graph (means ± SE) represents the percentage of entire tissue sections that stained for type I collagen ( n = 4), normalized to total surface area (SA). Representative sections from pcy ( D ) and Postn CD pcy ( E ). F : tissue sections were scored by a naïve observer assigning a percentage of fibrotic/edematous cortical area per total area of the cortex. Bar graph represents fibrosis as a percentage of total sectional area. * P
    Figure Legend Snippet: Collecting duct (CD)-specific expression of periostin increases renal type I collagen and interstitial fibrosis in pcy mice. Representative sections from pcy ( A ) and Postn CD pcy ( B ) mice stained with antibodies to type I collagen (red) and Dolichos biflorus agglutinin (DBA; green). C : bar graph (means ± SE) represents the percentage of entire tissue sections that stained for type I collagen ( n = 4), normalized to total surface area (SA). Representative sections from pcy ( D ) and Postn CD pcy ( E ). F : tissue sections were scored by a naïve observer assigning a percentage of fibrotic/edematous cortical area per total area of the cortex. Bar graph represents fibrosis as a percentage of total sectional area. * P

    Techniques Used: Expressing, Mouse Assay, Staining

    23) Product Images from "Tubular cell dedifferentiation and peritubular inflammation are coupled by the transcription regulator Id1 in renal fibrogenesis"

    Article Title: Tubular cell dedifferentiation and peritubular inflammation are coupled by the transcription regulator Id1 in renal fibrogenesis

    Journal: Kidney International

    doi: 10.1038/ki.2011.469

    Id1 is induced in a tubular segment-specific fashion after injury Immunofluorescence staining demonstrated Id1 (red) and various tubular markers (green) in the obstructed kidneys at 7 days after UUO. No or little Id1 expression was detected in the sham-operated normal kidneys (data not shown). Segment-specific tubular markers used are as follows: proximal tubule, aquaporin-1 (AQP1); cortical thick ascending limb, Tamm-Horsfall glycoprotein (THP); distal tubule, thiazide-sensitive NaCl cotransporter (TSC)/NCC; and collecting duct, fluorescein-labeled Dolichos Biflorus agglutinin (DBA). Boxed areas are enlarged. Arrowheads indicate Id1-positive tubules. Scale bar, 50 μm.
    Figure Legend Snippet: Id1 is induced in a tubular segment-specific fashion after injury Immunofluorescence staining demonstrated Id1 (red) and various tubular markers (green) in the obstructed kidneys at 7 days after UUO. No or little Id1 expression was detected in the sham-operated normal kidneys (data not shown). Segment-specific tubular markers used are as follows: proximal tubule, aquaporin-1 (AQP1); cortical thick ascending limb, Tamm-Horsfall glycoprotein (THP); distal tubule, thiazide-sensitive NaCl cotransporter (TSC)/NCC; and collecting duct, fluorescein-labeled Dolichos Biflorus agglutinin (DBA). Boxed areas are enlarged. Arrowheads indicate Id1-positive tubules. Scale bar, 50 μm.

    Techniques Used: Immunofluorescence, Staining, Expressing, Labeling

    24) Product Images from "Aberrant expression of laminin-332 promotes cell proliferation and cyst growth in ARPKD"

    Article Title: Aberrant expression of laminin-332 promotes cell proliferation and cyst growth in ARPKD

    Journal: American Journal of Physiology - Renal Physiology

    doi: 10.1152/ajprenal.00104.2013

    Laminin-332 is aberrantly expressed in human autosomal recessive polycystic kidney disease (ARPKD) kidney epithelia. A : relative expression levels of laminin α 3 -, β 3 -, and γ 2 -chains in human ARPKD cells compared with those of normal human kidney (NHK) cells. There was a significant 2-fold increase in mRNA levels of laminin-γ 2 in ARPKD cells compared with NHK cells. B : frozen kidney sections of a human subject with no kidney disease stained with a monoclonal laminin-332 antibody (red) and Dolichos biflorus agglutinin (DBA; green) demonstrated no red (laminin-332) staining in collecting ducts. C : laminin-332 (red) and DBA (green) staining in cystic structures (arrows) and precystic tubules of a typical kidney section procured from an ARPKD/congestive heart failure patient. D : laminin-332 staining alone of the image in C for clarity.
    Figure Legend Snippet: Laminin-332 is aberrantly expressed in human autosomal recessive polycystic kidney disease (ARPKD) kidney epithelia. A : relative expression levels of laminin α 3 -, β 3 -, and γ 2 -chains in human ARPKD cells compared with those of normal human kidney (NHK) cells. There was a significant 2-fold increase in mRNA levels of laminin-γ 2 in ARPKD cells compared with NHK cells. B : frozen kidney sections of a human subject with no kidney disease stained with a monoclonal laminin-332 antibody (red) and Dolichos biflorus agglutinin (DBA; green) demonstrated no red (laminin-332) staining in collecting ducts. C : laminin-332 (red) and DBA (green) staining in cystic structures (arrows) and precystic tubules of a typical kidney section procured from an ARPKD/congestive heart failure patient. D : laminin-332 staining alone of the image in C for clarity.

    Techniques Used: Expressing, Staining

    25) Product Images from "Repair after nephron ablation reveals limitations of neonatal neonephrogenesis"

    Article Title: Repair after nephron ablation reveals limitations of neonatal neonephrogenesis

    Journal: JCI Insight

    doi: 10.1172/jci.insight.88848

    Expression of developmentally regulated genes is unaltered in response to cryoinjury. ( A ) Immunofluorescence staining for Pax2 and ( B ) in situ hybridization for Lhx1 were used to determine expression patterns around the injury area compared with contralateral control kidneys. ( A ) Pax2 expression is not different around injured areas compared with controls (red, Pax2; green, DBA; white, LTL) Original magnification, ×20. ( B ) Lhx1 is not differentially expressed after injury, as determined by in situ hybridization. Original magnification, ×3. Asterisks indicate site of injury. DBA, Dolichos Biflorus Agglutinin; LTL, Lotus Tetragonolobus Agglutinin.
    Figure Legend Snippet: Expression of developmentally regulated genes is unaltered in response to cryoinjury. ( A ) Immunofluorescence staining for Pax2 and ( B ) in situ hybridization for Lhx1 were used to determine expression patterns around the injury area compared with contralateral control kidneys. ( A ) Pax2 expression is not different around injured areas compared with controls (red, Pax2; green, DBA; white, LTL) Original magnification, ×20. ( B ) Lhx1 is not differentially expressed after injury, as determined by in situ hybridization. Original magnification, ×3. Asterisks indicate site of injury. DBA, Dolichos Biflorus Agglutinin; LTL, Lotus Tetragonolobus Agglutinin.

    Techniques Used: Expressing, Immunofluorescence, Staining, In Situ Hybridization

    26) Product Images from "Expression of Glutamate Transporters in Mouse Liver, Kidney, and Intestine"

    Article Title: Expression of Glutamate Transporters in Mouse Liver, Kidney, and Intestine

    Journal: Journal of Histochemistry and Cytochemistry

    doi: 10.1369/0022155417749828

    EAAT3 was detected in the brush boarder of proximal tubules in mouse kidneys. Panel A–B: The section was labeled with rabbit anti-EAAC1 antibody (Ab#371; red, 1μg/ml) and fluorescein-conjugated LTL (green, 1:150, a marker for proximal tubules). The EAAT3 knockout (–/–) kidney was used as a control for antibody specificity (D and F). Panel C: EAAT3 is not present in collecting ducts. The section was double-labeled with anti-EAAT3 antibody Ab#371 (red, 3μg/ml) and fluorescein-conjugated DBAL (green, 1:150, a marker for collecting ducts). Panel E: EAAT3 is not expressed in thick ascending limb of Henle’s loop. The section was double-labeled with sheep anti-EAAT3 antibody (Ab#340; red, 3μg/ml) and fluorescein-conjugated THG (green, 1:500, a marker for thick ascending limb of Henle’s loop). Panel G–J: Higher magnification images showing that EAAT3 was localized at the brush border membrane of proximal tubule in the renal cortex. Scale bar = 100 μm in A–F, 20 μm in G–J. Abbreviations: EAAT, excitatory amino acid transporter; LTL, Lotus Tetragonolobus lectin; DBAL, Dolichos Biflorus Agglutinin Lectin; THG, Tamm Horsfall glycoprotein; Co, cortex; OM, outer medulla; G, glomerulus; DT, distal tubule; PT, proximal tubule; CD, collecting duct; TAL, thick ascending limb of Henle’s loop.
    Figure Legend Snippet: EAAT3 was detected in the brush boarder of proximal tubules in mouse kidneys. Panel A–B: The section was labeled with rabbit anti-EAAC1 antibody (Ab#371; red, 1μg/ml) and fluorescein-conjugated LTL (green, 1:150, a marker for proximal tubules). The EAAT3 knockout (–/–) kidney was used as a control for antibody specificity (D and F). Panel C: EAAT3 is not present in collecting ducts. The section was double-labeled with anti-EAAT3 antibody Ab#371 (red, 3μg/ml) and fluorescein-conjugated DBAL (green, 1:150, a marker for collecting ducts). Panel E: EAAT3 is not expressed in thick ascending limb of Henle’s loop. The section was double-labeled with sheep anti-EAAT3 antibody (Ab#340; red, 3μg/ml) and fluorescein-conjugated THG (green, 1:500, a marker for thick ascending limb of Henle’s loop). Panel G–J: Higher magnification images showing that EAAT3 was localized at the brush border membrane of proximal tubule in the renal cortex. Scale bar = 100 μm in A–F, 20 μm in G–J. Abbreviations: EAAT, excitatory amino acid transporter; LTL, Lotus Tetragonolobus lectin; DBAL, Dolichos Biflorus Agglutinin Lectin; THG, Tamm Horsfall glycoprotein; Co, cortex; OM, outer medulla; G, glomerulus; DT, distal tubule; PT, proximal tubule; CD, collecting duct; TAL, thick ascending limb of Henle’s loop.

    Techniques Used: Labeling, Marker, Knock-Out

    27) Product Images from "Repair after nephron ablation reveals limitations of neonatal neonephrogenesis"

    Article Title: Repair after nephron ablation reveals limitations of neonatal neonephrogenesis

    Journal: JCI Insight

    doi: 10.1172/jci.insight.88848

    Expression of developmentally regulated genes is unaltered in response to cryoinjury. ( A ) Immunofluorescence staining for Pax2 and ( B ) in situ hybridization for Lhx1 were used to determine expression patterns around the injury area compared with contralateral control kidneys. ( A ) Pax2 expression is not different around injured areas compared with controls (red, Pax2; green, DBA; white, LTL) Original magnification, ×20. ( B ) Lhx1 is not differentially expressed after injury, as determined by in situ hybridization. Original magnification, ×3. Asterisks indicate site of injury. DBA, Dolichos Biflorus Agglutinin; LTL, Lotus Tetragonolobus Agglutinin.
    Figure Legend Snippet: Expression of developmentally regulated genes is unaltered in response to cryoinjury. ( A ) Immunofluorescence staining for Pax2 and ( B ) in situ hybridization for Lhx1 were used to determine expression patterns around the injury area compared with contralateral control kidneys. ( A ) Pax2 expression is not different around injured areas compared with controls (red, Pax2; green, DBA; white, LTL) Original magnification, ×20. ( B ) Lhx1 is not differentially expressed after injury, as determined by in situ hybridization. Original magnification, ×3. Asterisks indicate site of injury. DBA, Dolichos Biflorus Agglutinin; LTL, Lotus Tetragonolobus Agglutinin.

    Techniques Used: Expressing, Immunofluorescence, Staining, In Situ Hybridization

    Related Articles

    Fluorescence:

    Article Title: Developmental change in translation initiation alters the localization of a common microbial protein necessary for Toxoplasma chronic infection
    Article Snippet: .. 250 µl of the homogenized brain was fixed with 3.0% formaldehyde for 20 min, quenched with 1 mM glycine for 5 min, and permeabilized and blocked in 0.2% Triton X-100 with 3.0% bovine serum albumin (BSA) for at least 30 min. Tissue cysts were then stained with fluorescein-labeled Dolichos biflorus agglutinin (Vector Labs, Burlingame, CA, USA) for 1 hour, and 3–5 µL samples were mounted and cyst numbers counted by fluorescence microscopy. ..

    Microscopy:

    Article Title: Examination of a Virulence Mutant Uncovers the Ribosome Biogenesis Regulatory Protein of Toxoplasma gondii
    Article Snippet: .. At 22 days post-infection, brain cyst loads were quantified by immunofluorescence microscopy using fluorescein-conjugated Dolichos biflorus agglutinin (DbA; Vector Laboratories, Inc., Burlingame, California) as previously described ( ). ..

    Article Title: Developmental change in translation initiation alters the localization of a common microbial protein necessary for Toxoplasma chronic infection
    Article Snippet: .. 250 µl of the homogenized brain was fixed with 3.0% formaldehyde for 20 min, quenched with 1 mM glycine for 5 min, and permeabilized and blocked in 0.2% Triton X-100 with 3.0% bovine serum albumin (BSA) for at least 30 min. Tissue cysts were then stained with fluorescein-labeled Dolichos biflorus agglutinin (Vector Labs, Burlingame, CA, USA) for 1 hour, and 3–5 µL samples were mounted and cyst numbers counted by fluorescence microscopy. ..

    Purification:

    Article Title: Spliced XBP1 Rescues Renal Interstitial Inflammation Due to Loss of Sec63 in Collecting Ducts
    Article Snippet: .. The following antibodies and lectins were used at the indicated dilutions: polyclonal antiserum raised to the COOH terminus of anti-megalin (anti-MC220; 1:300) ; anti-Tamm–Horsfall protein (AB733, 1:200; Millipore); anti-aquaporin 2 (AQP2; sc-9882, 1:100; Santa Cruz Biotechnology); fluorescein-labeled Lotus tetragonolobus lectin (LTL; FL-1321, 1:200; Vector Laboratories); fluorescein-labeled Dolichos biflorus agglutinin (FL-1031, 1:50; Vector Laboratories); anti-mouse F4/80 purified antigen (14–4801–81, 1:200; eBiosience); anti– α− smooth muscle actin antibody (ab5694, 1:300; Abcam); anti-S100A4 antibody (fibroblast-specific protein 1 [FSP1], ab27957, 1:500; Abcam); anti- PDGF receptor- β (PDGFR β , ab32570, 1:400; Abcam), anti–H+-ATPase (1:100; gift from SueAnn Mentone, Yale University), and anti-pendrin (1:100; gift from Peter Aronson, Yale University). .. Rat anti-L1CAM (L1; clone S10.33, 5 μ g/ml; gift from Ugo Cavallaro, Instituto Europeo di Oncologia) was conjugated using Alexa Fluor 647 antibody labeling kit (Invitrogen).

    Blocking Assay:

    Article Title: Toxoplasma gondii tissue cyst purification using Percoll gradients
    Article Snippet: .. Shandon Cytospin 4 Centrifuge Cytospin funnels (TPX Sample Chamber) (Thermo #A78710018) Cytoclip stainless steel slide holders (Thermo Fisher #59-910-052) Cytospin filter cards (Fisher #22-030-410) Frosted Glass Slides (Fisher #12-544-2) Cardboard slide holder (Fisher #12-587-10) Wax pencil (Fisher #NC9072020) Copin jars with screw on cap (Fisher 08-816) 70% Ethanol for decontamination Absolute Methanol (at −20°C) Paraformaldehyde stock (EMS #RT15710) Triton X-100 (0.2% in PBS) (Sigma #X100) Carbo-Free Blocking Solution (Vector Laboratories #SP5040) Dolichos biflorus Lectin (FITC-conjugated) (Vector Laboratories #FL-1031) Concanavalin A Lectin (Rhodamine conjugated) Vector Laboratories #FL-1001) Hoescht Dye (10mg/ml) (ThermoFisher #H3569) .. Aspirate the diluted Percoll as above (Basic Protocol 2) and resuspend the pellet in 500µl of PBS using a 1ml micropipettor.

    Staining:

    Article Title: Developmental change in translation initiation alters the localization of a common microbial protein necessary for Toxoplasma chronic infection
    Article Snippet: .. 250 µl of the homogenized brain was fixed with 3.0% formaldehyde for 20 min, quenched with 1 mM glycine for 5 min, and permeabilized and blocked in 0.2% Triton X-100 with 3.0% bovine serum albumin (BSA) for at least 30 min. Tissue cysts were then stained with fluorescein-labeled Dolichos biflorus agglutinin (Vector Labs, Burlingame, CA, USA) for 1 hour, and 3–5 µL samples were mounted and cyst numbers counted by fluorescence microscopy. ..

    Article Title: FGF10 maintains distal lung bud epithelium and excessive signaling leads to progenitor state arrest, distalization, and goblet cell metaplasia
    Article Snippet: .. Mature goblet cells were detected by an overnight staining using rhodamine or fluorescein conjugated Dolichos Biflorus Agglutinin (DBA) (Vector Laboratories). .. In situ probes where synthesized from mouse Fgf10 and Bmp4 previously isolated in our lab and cloned in pCR4 plasmids and Tff1 , Tff3 , Cryptdin3 and Fabp2 plasmids (Open Biosystems, Huntsville, AL, USA).

    Immunofluorescence:

    Article Title: Examination of a Virulence Mutant Uncovers the Ribosome Biogenesis Regulatory Protein of Toxoplasma gondii
    Article Snippet: .. At 22 days post-infection, brain cyst loads were quantified by immunofluorescence microscopy using fluorescein-conjugated Dolichos biflorus agglutinin (DbA; Vector Laboratories, Inc., Burlingame, California) as previously described ( ). ..

    Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 95
    Vector Laboratories fluorescent dolichos biflorus agglutinin
    AQP11 protein expression in Tg AQP11 mouse kidney and the segmental origin of cysts in AQP11(−/−) mouse kidney. Immunofluorescence with HA antibody of 3-week-old Tg AQP11 and WT mouse kidneys: (A) cortex and (B) medulla. The immunostaining, image capture, and image processing were carried out under the same conditions. AQP11 was present only at the cortex. Scale bar, 20 μ m. (C) Double immunofluorescence with HA antibody and AQP1 antibody (proximal tubule marker), NCC antibody (distal tubule marker), or dolichos <t>biflorus</t> agglutinin (DBA; collecting tubule and collecting duct marker) in the kidney of a 3-week-old Tg AQP11 mouse. AQP11 was localized in the cytoplasm of the proximal tubule cells. Scale bar, 10 μ m. (D) Fluorescent staining with lotus tetragonolobus lectin (LTL; proximal tubule marker) and DBA in 3-week-old AQP11(−/−) mouse kidney. Segmental origin of cysts in AQP11(−/−) kidney was mainly proximal tubules. Scale bar, 50 μ m.
    Fluorescent Dolichos Biflorus Agglutinin, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 95/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/fluorescent dolichos biflorus agglutinin/product/Vector Laboratories
    Average 95 stars, based on 13 article reviews
    Price from $9.99 to $1999.99
    fluorescent dolichos biflorus agglutinin - by Bioz Stars, 2020-08
    95/100 stars
      Buy from Supplier

    Image Search Results


    AQP11 protein expression in Tg AQP11 mouse kidney and the segmental origin of cysts in AQP11(−/−) mouse kidney. Immunofluorescence with HA antibody of 3-week-old Tg AQP11 and WT mouse kidneys: (A) cortex and (B) medulla. The immunostaining, image capture, and image processing were carried out under the same conditions. AQP11 was present only at the cortex. Scale bar, 20 μ m. (C) Double immunofluorescence with HA antibody and AQP1 antibody (proximal tubule marker), NCC antibody (distal tubule marker), or dolichos biflorus agglutinin (DBA; collecting tubule and collecting duct marker) in the kidney of a 3-week-old Tg AQP11 mouse. AQP11 was localized in the cytoplasm of the proximal tubule cells. Scale bar, 10 μ m. (D) Fluorescent staining with lotus tetragonolobus lectin (LTL; proximal tubule marker) and DBA in 3-week-old AQP11(−/−) mouse kidney. Segmental origin of cysts in AQP11(−/−) kidney was mainly proximal tubules. Scale bar, 50 μ m.

    Journal: Journal of the American Society of Nephrology : JASN

    Article Title: Aberrant Glycosylation and Localization of Polycystin-1 Cause Polycystic Kidney in an AQP11 Knockout Model

    doi: 10.1681/ASN.2013060614

    Figure Lengend Snippet: AQP11 protein expression in Tg AQP11 mouse kidney and the segmental origin of cysts in AQP11(−/−) mouse kidney. Immunofluorescence with HA antibody of 3-week-old Tg AQP11 and WT mouse kidneys: (A) cortex and (B) medulla. The immunostaining, image capture, and image processing were carried out under the same conditions. AQP11 was present only at the cortex. Scale bar, 20 μ m. (C) Double immunofluorescence with HA antibody and AQP1 antibody (proximal tubule marker), NCC antibody (distal tubule marker), or dolichos biflorus agglutinin (DBA; collecting tubule and collecting duct marker) in the kidney of a 3-week-old Tg AQP11 mouse. AQP11 was localized in the cytoplasm of the proximal tubule cells. Scale bar, 10 μ m. (D) Fluorescent staining with lotus tetragonolobus lectin (LTL; proximal tubule marker) and DBA in 3-week-old AQP11(−/−) mouse kidney. Segmental origin of cysts in AQP11(−/−) kidney was mainly proximal tubules. Scale bar, 50 μ m.

    Article Snippet: Fluorescent dolichos biflorus agglutinin and lotus tetragonolobus lectin were purchased from Vector Laboratories (Burlingame, CA).

    Techniques: Expressing, Immunofluorescence, Immunostaining, Marker, Staining

    MYR1 plays a role regulating host cell transcriptional changes in bradyzoites containing cells. ( A ) Differences in the expressional profile (Log 2 CPM) of MYR1, MYR2, and MYR3 between tachyzoites (24 hours) and bradyzoites (7 days in vitro ). Expression drops during bradyzoite stages for all proteins. ( B ) PruΔ ku80 and PruΔ ku80 MYR1-HA parasites were induced under alkaline conditions for 7 days before fixation. MYR1-HA (αHA; white) in bradyzoites (pLDH2-eGFP; green) is localised to the PV space and co-localises to cyst wall marker CST1 (αCST1; magenta). Brightness and contrast was edited on single colour channels prior to merging. ( C ) (i) WT and Δ myr1 parasites were fixed after 7 days of differentiation under alkaline conditions. Both WT and Δ myr1 were able to form intact cysts (DBA; green) containing health bradyzoites (αSRS9; magenta) and showed the presence of amylopectin granules (black arrows). Scale bar = 10μM; MYR, Myc Regulationr; PV, parasitophorous vacuole; DAPI, 4’,6-diamidino-2-phenylindole; DBA, fluorescein conjugated Dolichos biflorus agglutinin. Brightness and contrast was edited on single colour channels prior to merging. (ii) The number of bradyzoite containing cells after 7 days of differentiation between WT (Pru) and Δ myr1 was analysed by FACS (mean ± SD, n = 3 experiments, unpaired, two-sided Student’s t-test with Welch’s correction; **p=0.0058). (iii). The size of PruΔ ku80 Δ myr1 cysts were compared to WT by quantification of from immuno-fluorescence images (mean ± SD, n = 3 experiments, each experiment analysed on average between 20-40 bradyzoite cysts, unpaired, two-sided Student’s t-test with Mann-Whitney correction; p=0.156) ( D ) WT (Pru) and Δ myr1 inoculated human foreskin fibroblast (HFF) cells were FACS sorted into infected and uninfected samples before RNA extraction and sequencing (as per Fig. 1A ). Heat map of log 2 RPKM expression for the top 100 differentially regulated genes between WT bradyzoite infected and Δ myr1 bradyzoite infected cells. Expression has been scaled to have mean 0 and standard deviation 1 for each gene. In the absence of MYR1, bradyzoite specific host expression appears to somewhat mimic the bystander cell population (from both WT and Δ myr1 ). See also Figure S2 and Table S4 for gene list. ( E ) Venn diagram of bradyzoite WT infected vs uninfected DEGs (grey) and bradyzoite Δ myr1 infected vs uninfected DEGs (green); the number of up-regulated genes are identified in red and down-regulated genes in blue. Dotted lines indicated shared DEGs deemed as independent of MYR1.

    Journal: bioRxiv

    Article Title: Toxoplasma gondii bradyzoites induce transcriptional changes to host cells and prevent IFNγ-mediated cell death

    doi: 10.1101/669689

    Figure Lengend Snippet: MYR1 plays a role regulating host cell transcriptional changes in bradyzoites containing cells. ( A ) Differences in the expressional profile (Log 2 CPM) of MYR1, MYR2, and MYR3 between tachyzoites (24 hours) and bradyzoites (7 days in vitro ). Expression drops during bradyzoite stages for all proteins. ( B ) PruΔ ku80 and PruΔ ku80 MYR1-HA parasites were induced under alkaline conditions for 7 days before fixation. MYR1-HA (αHA; white) in bradyzoites (pLDH2-eGFP; green) is localised to the PV space and co-localises to cyst wall marker CST1 (αCST1; magenta). Brightness and contrast was edited on single colour channels prior to merging. ( C ) (i) WT and Δ myr1 parasites were fixed after 7 days of differentiation under alkaline conditions. Both WT and Δ myr1 were able to form intact cysts (DBA; green) containing health bradyzoites (αSRS9; magenta) and showed the presence of amylopectin granules (black arrows). Scale bar = 10μM; MYR, Myc Regulationr; PV, parasitophorous vacuole; DAPI, 4’,6-diamidino-2-phenylindole; DBA, fluorescein conjugated Dolichos biflorus agglutinin. Brightness and contrast was edited on single colour channels prior to merging. (ii) The number of bradyzoite containing cells after 7 days of differentiation between WT (Pru) and Δ myr1 was analysed by FACS (mean ± SD, n = 3 experiments, unpaired, two-sided Student’s t-test with Welch’s correction; **p=0.0058). (iii). The size of PruΔ ku80 Δ myr1 cysts were compared to WT by quantification of from immuno-fluorescence images (mean ± SD, n = 3 experiments, each experiment analysed on average between 20-40 bradyzoite cysts, unpaired, two-sided Student’s t-test with Mann-Whitney correction; p=0.156) ( D ) WT (Pru) and Δ myr1 inoculated human foreskin fibroblast (HFF) cells were FACS sorted into infected and uninfected samples before RNA extraction and sequencing (as per Fig. 1A ). Heat map of log 2 RPKM expression for the top 100 differentially regulated genes between WT bradyzoite infected and Δ myr1 bradyzoite infected cells. Expression has been scaled to have mean 0 and standard deviation 1 for each gene. In the absence of MYR1, bradyzoite specific host expression appears to somewhat mimic the bystander cell population (from both WT and Δ myr1 ). See also Figure S2 and Table S4 for gene list. ( E ) Venn diagram of bradyzoite WT infected vs uninfected DEGs (grey) and bradyzoite Δ myr1 infected vs uninfected DEGs (green); the number of up-regulated genes are identified in red and down-regulated genes in blue. Dotted lines indicated shared DEGs deemed as independent of MYR1.

    Article Snippet: The following antibodies were used in this study: αGAP45 , αSAG1 DG52 , αHA 3F10 (Roche), αSRS9 , αCST1 , Fluorescein-Dolichos Biflorus Agglutinin (DBA; Vector Labs), αIRF1 D5E4 (Cell Signalling Technologies) and αMyc 9E10 (Sigma).

    Techniques: In Vitro, Expressing, Marker, FACS, Fluorescence, MANN-WHITNEY, Infection, RNA Extraction, Sequencing, Standard Deviation

    ( A ) C3-infected mice have reduced brain cyst burdens compared to the parental strain, PruΔ HPT (WT). At 22 days post-infection, brains of infected mice were collected, and cysts were quantified based on reactivity to Dolichos biflorus agglutinin

    Journal: The Journal of parasitology

    Article Title: Examination of a Virulence Mutant Uncovers the Ribosome Biogenesis Regulatory Protein of Toxoplasma gondii

    doi: 10.1645/GE-2741.1

    Figure Lengend Snippet: ( A ) C3-infected mice have reduced brain cyst burdens compared to the parental strain, PruΔ HPT (WT). At 22 days post-infection, brains of infected mice were collected, and cysts were quantified based on reactivity to Dolichos biflorus agglutinin

    Article Snippet: At 22 days post-infection, brain cyst loads were quantified by immunofluorescence microscopy using fluorescein-conjugated Dolichos biflorus agglutinin (DbA; Vector Laboratories, Inc., Burlingame, California) as previously described ( ).

    Techniques: Infection, Mouse Assay

    Examples of albumin fragment localization in diabetic renal tubules. PAS staining (right) and IMS (left) were performed on the same section; immunostaining and IMS were performed on serial sections. The resulting immunofluorescence and IMS images were co-registered. (A) Albumin fragments are not detected in glomeruli (marked by white-dashed circles). (B) Albumin fragments are localized to renal tubules. An example IMS ion image of the albumin peptide 25-48 acquired at 10 μm spatial resolution with corresponding H E stain. After the tissue was imaged, the matrix was removed with a series of ethanol washes and the tissue was H E stained. A zoomed in region is displayed in the right panel for clarity. (C) Albumin fragments (Left) co-localize with Lotus tetragonolobus lectin (LTL), a proximal tubule marker (Right). (D) Dolichos biflorus agglutinin (DBA), a distal tubule and collecting duct marker (Right) co-localizes with albumin fragments (Left). Scale bars for panels A, C and D = 200 μm. Scale bars for panel B= 50 μm (top panel) and 20 μm (bottom panel).

    Journal: Kidney international

    Article Title: Imaging mass spectrometry reveals direct albumin fragmentation within the diabetic kidney

    doi: 10.1016/j.kint.2018.01.040

    Figure Lengend Snippet: Examples of albumin fragment localization in diabetic renal tubules. PAS staining (right) and IMS (left) were performed on the same section; immunostaining and IMS were performed on serial sections. The resulting immunofluorescence and IMS images were co-registered. (A) Albumin fragments are not detected in glomeruli (marked by white-dashed circles). (B) Albumin fragments are localized to renal tubules. An example IMS ion image of the albumin peptide 25-48 acquired at 10 μm spatial resolution with corresponding H E stain. After the tissue was imaged, the matrix was removed with a series of ethanol washes and the tissue was H E stained. A zoomed in region is displayed in the right panel for clarity. (C) Albumin fragments (Left) co-localize with Lotus tetragonolobus lectin (LTL), a proximal tubule marker (Right). (D) Dolichos biflorus agglutinin (DBA), a distal tubule and collecting duct marker (Right) co-localizes with albumin fragments (Left). Scale bars for panels A, C and D = 200 μm. Scale bars for panel B= 50 μm (top panel) and 20 μm (bottom panel).

    Article Snippet: Fluorescein-labeled lotus tetragonolobus lectin (LTL) and fluorescein-labeled dolichos biflorus agglutinin (DBA) kits were from VectorLabs (Burlingame, CA).

    Techniques: Staining, Immunostaining, Immunofluorescence, Marker