rabbit polyclonal anti dock7 (Bioss)
Bioss is a verified supplier 
Bioss manufactures this product 
90
Structured Review
Bioss
rabbit polyclonal anti dock7
Rabbit Polyclonal Anti Dock7, supplied by Bioss, used in various techniques. Bioz Stars score: 90/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/rabbit polyclonal anti dock7/product/Bioss
Average 90 stars, based on 3 article reviews
Rabbit Polyclonal Anti Dock7, supplied by Bioss, used in various techniques. Bioz Stars score: 90/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/rabbit polyclonal anti dock7/product/Bioss
Average 90 stars, based on 3 article reviews
rabbit polyclonal anti dock7 - by Bioz Stars,
2026-03
90/100 stars
Images
1) Product Images from "Dual role for DOCK7 in tangential migration of interneuron precursors in the postnatal forebrain"
Article Title: Dual role for DOCK7 in tangential migration of interneuron precursors in the postnatal forebrain
Journal: The Journal of Cell Biology
doi: 10.1083/jcb.201704157
Figure Legend Snippet: Expression of DOCK7 in the postnatal mouse forebrain. (A) A cartoon representation of the V-SVZ–RMS–OB pathway. (B) Coronal sections of forebrains of P10 mice at positions indicated in the cartoon in A immunostained with antibodies to DOCK7 and DCX and counterstained with DAPI. Boxed regions in III are enlarged and shown at the bottom. Bars: (top) 50 µm; (bottom) 10 µm. (C) Coronal sections of the V-SVZ region of P10 mice immunostained with antibodies to DOCK7 and GFAP, MASH1, or nestin and counterstained with DAPI. Boxed regions are enlarged and shown at the bottom. The yellow dashed line indicates the boundary region between the V-SVZ and the lateral ventricle. Bars: (top) 25 µm; (bottom) 10 µm. (D) Localization of DOCK7 in cultured V-SVZ–derived neuroblasts. Neuroblasts dissociated from V-SVZ tissue of P1–3 mice were fixed at 30 h in vitro, followed by immunostaining with indicated antibodies and counterstaining with DAPI. Bar, 10 µm.
Techniques Used: Expressing, Cell Culture, Derivative Assay, In Vitro, Immunostaining
Figure Legend Snippet: DOCK7 function is required for the migration of neuroblasts along the RMS. (A) Schematic drawing of postnatal in vivo electroporation. A virtual line (red) connecting the right eye to the craniometrical landmark λ serves as positional marker for plasmid injection into the lateral ventricle (LV). Lateral bars indicate position of electrodes. (B) Composite confocal images of forebrains of mice electroporated at P3 with plasmids expressing EGFP and nontargeting shRNA (scr#1), Dock7-targeting shRNAs (Dock7#1 and Dock7#2), or Dock7#2 shRNA together with DOCK7 cDNA (Dock7#2 + DOCK7) and sacrificed at P10 showing distribution of EGFP + transfected cells along the V-SVZ–RMS–OB pathway. Slices were counterstained with DAPI. Dotted lines outline borders of sagittal slices. Bar, 500 µm. (C) Quantification of the distribution of EGFP + transfected cells along the V-SVZ–RMS–OB pathway in the forebrains of mice electroporated at P3 and sacrificed at P10. n = 1,316–2,511 cells from at least three animals for each condition. (D) Quantification of the distribution of EGFP + transfected cells along the V-SVZ–RMS–OB pathway in the forebrains of mice electroporated at P3 and sacrificed at P17. n = 2,379–2,462 cells from at least three animals for each condition. (E) Enlarged images of neuroblasts in RMSp regions of mice electroporated with indicated constructs at P3 and sacrificed at P10. Arrowheads indicate branching of LP. Bar, 20 µm. (F) Quantification of the length of the LP of neuroblasts in the RMS of mice electroporated with indicated constructs at P3 and sacrificed at P10. n = 91–680 cells from at least three animals for each condition. Data are shown as means ± SEM. **, P < 0.01; ***, P < 0.001; ns, P > 0.05 compared with scr#1; one-way ANOVA with Dunnett’s post hoc test (C and F) or Student’s t test (D).
Techniques Used: Migration, In Vivo, Electroporation, Marker, Plasmid Preparation, Injection, Expressing, shRNA, Transfection, Construct
Figure Legend Snippet: Knockdown of DOCK7 affects the migration distance, displacement, speed, and LP branching frequency of migrating neuroblasts. (A–F) P2–3 mouse pups were electroporated with plasmids expressing tdTomato and scr#1, Dock7#2 shRNA, or the rescue construct (Dock7#2 + DOCK7). After 5 d, acute sagittal brain slices were prepared, and tdTomato + transfected neuroblasts were imaged by spinning-disk confocal microscopy over a 4-h time period. (A) Time-lapse sequence of scr#1 or Dock7#2 shRNA-expressing cells migrating in the lower vertical arm of the RMSp. Five cells in each slice are labeled in the 0-min panel, and their tracks over time are indicated by lines of the same color. Bars, 70 µm. (B–D) Quantifications of the mean migrated distance (B), displacement (C), and velocity (D) of neuroblasts expressing indicated constructs. n = 50–61 cells from five to seven animals for each condition. (E) Examples of time-lapse series of scr#1 or Dock7#2 shRNA-expressing cells in the lower vertical arm of the RMSp (higher magnification). Arrowheads indicate branching of LP. Bars, 50 µm. (F) Quantification of the number of branching events per h for neuroblasts expressing indicated constructs. n = 50–61 cells from five to seven animals for each condition. Data are shown as means ± SEM. **, P < 0.01; ****, P < 0.0001; ns, P > 0.05 compared with scr#1; one-way ANOVA with Dunnett’s post hoc test.
Techniques Used: Migration, Expressing, shRNA, Construct, Transfection, Confocal Microscopy, Sequencing, Labeling
Figure Legend Snippet: DOCK7 controls different cellular aspects of neuroblast migration via DHR2/Rac-dependent and R2-dependent pathways. (A) DOCK7 domain structure and deletion and point mutant constructs. ΔR2 comprises the DHR1 domain (amino acids 561–727) and TACC3-binding domain (amino acids 933–1,164). The asterisk indicates the DOCK7(V2022A) mutation. (B) Composite confocal images of forebrains of mice electroporated at P3 with plasmids expressing EGFP and Dock7#2 shRNA + DOCK7, Dock7#2 shRNA + DOCK7ΔDHR2, Dock7#2 shRNA + DOCK7V2022A, or Dock7#2 shRNA + DOCK7ΔR2 and sacrificed at P10, showing distribution of EGFP + transfected neuroblasts along the V-SVZ–RMS–OB pathway. Slices were counterstained with DAPI. Dotted lines outline borders of sagittal slices. Bar, 500 µm. (C) Quantification of the distribution of EGFP + transfected cells along the V-SVZ–RMS–OB pathway. n = 1,316–1,870 cells from at least three animals for each condition. (D) Quantification of the length of the LP of neuroblasts expressing indicated constructs. n = 91–680 cells from at least three animals for each condition. (E–H) P2–3 mouse pups were electroporated with a tdTomato-expressing plasmid together with one of the indicated constructs. Acute sagittal brain slices were prepared 5 d later and subjected to confocal live-cell imaging. Quantifications of the mean migrated distance (E), displacement (F), velocity (G), and number of branching events per h (H) for the tdTomato + transfected neuroblasts. n = 42–61 cells from four to seven animals for each condition. Data are shown as means ± SEM. *, P < 0.05; **, P < 0.01; ***, P < 0.001; ****, P < 0.0001; ns, P > 0.05 compared with scr#1; one-way ANOVA with Dunnett’s post hoc test.
Techniques Used: Migration, Mutagenesis, Construct, Binding Assay, Expressing, shRNA, Transfection, Plasmid Preparation, Live Cell Imaging
![DOCK7 interacts with p116 Rip . (A) DOCK7 and p116 Rip domain structure. (Top) DOCK7 fragments used in YTH screen/testing. CC, coiled-coil domain; PH, pleckstrin homology domain. (B) YTH interaction between DOCK7-R2 and p116 Rip . Yeast transformed with plasmids expressing DOCK7-R2 or DOCK7-R3 fused to GAL4 DNA–binding domain (GBD) and p116 Rip -C (amino acids 505–933) fused to the GAL4-activation domain (GAD) were grown on medium lacking histidine. Lamin served as negative and H-Ras and phosphatidylinositol 3-OH–kinase-δ (PI 3 KD) as positive controls. (C) Expression of p116 Rip in DCX-positive neuroblasts along the V-SVZ–RMS–OB pathway. Coronal sections of P10 mouse forebrain at positions indicated in the cartoon in immunostained with antibodies to p116 Rip and DCX and counterstained with DAPI. (D) DOCK7–p116 Rip interaction in mammalian cells. Lysates from HEK293 cells transiently expressing Flag-DOCK7 or empty control vector were immunoprecipitated (IP) with an antibody to Flag and analyzed by immunoblotting with antibodies to Flag and p116 Rip . TL, total lysate. (E) GST-p116 Rip -C (amino acids 505–1,024) fusion protein or GST alone (bottom, Coomassie brilliant blue [CBB] staining), immobilized on beads, was incubated with lysates from P5 mouse brains. Bound DOCK7 was detected by immunoblotting with an antibody to DOCK7. (F) Interaction of DOCK7 and p116 Rip in the brain. P10 mouse whole-brain extracts were immunoprecipitated with normal rabbit IgG, an anti-DOCK7 (DOCK7-Ab), or an anti-p116 Rip (p116 Rip -Ab) antibody and then were analyzed by immunoblotting with antibodies to DOCK7 and p116 Rip . Molecular masses are shown in kilodaltons. (G and H) Colocalization of DOCK7 and p116 Rip in V-SVZ–derived neuroblasts. (G) Coronal sections of P10 mouse forebrain at position III in the RMS as indicated in the cartoon in immunostained with antibodies to DOCK7 and p116 Rip and counterstained with DAPI. Boxed regions are enlarged and shown at the bottom. (H) Neuroblasts dissociated from V-SVZ tissue of P1–3 mice were fixed at 30 h in vitro, followed by immunostaining with indicated antibodies and counterstained with DAPI. Bars: (C and G, top) 50 µm; (G, bottom, and H) 10 µm.](https://pub-med-central-images-cdn.bioz.com/pub_med_central_ids_ending_with_6287/pmc05716287/pmc05716287__JCB_201704157_Fig5.jpg "DOCK7 interacts with p116 Rip . (A) DOCK7 and ...")
Figure Legend Snippet: DOCK7 interacts with p116 Rip . (A) DOCK7 and p116 Rip domain structure. (Top) DOCK7 fragments used in YTH screen/testing. CC, coiled-coil domain; PH, pleckstrin homology domain. (B) YTH interaction between DOCK7-R2 and p116 Rip . Yeast transformed with plasmids expressing DOCK7-R2 or DOCK7-R3 fused to GAL4 DNA–binding domain (GBD) and p116 Rip -C (amino acids 505–933) fused to the GAL4-activation domain (GAD) were grown on medium lacking histidine. Lamin served as negative and H-Ras and phosphatidylinositol 3-OH–kinase-δ (PI 3 KD) as positive controls. (C) Expression of p116 Rip in DCX-positive neuroblasts along the V-SVZ–RMS–OB pathway. Coronal sections of P10 mouse forebrain at positions indicated in the cartoon in immunostained with antibodies to p116 Rip and DCX and counterstained with DAPI. (D) DOCK7–p116 Rip interaction in mammalian cells. Lysates from HEK293 cells transiently expressing Flag-DOCK7 or empty control vector were immunoprecipitated (IP) with an antibody to Flag and analyzed by immunoblotting with antibodies to Flag and p116 Rip . TL, total lysate. (E) GST-p116 Rip -C (amino acids 505–1,024) fusion protein or GST alone (bottom, Coomassie brilliant blue [CBB] staining), immobilized on beads, was incubated with lysates from P5 mouse brains. Bound DOCK7 was detected by immunoblotting with an antibody to DOCK7. (F) Interaction of DOCK7 and p116 Rip in the brain. P10 mouse whole-brain extracts were immunoprecipitated with normal rabbit IgG, an anti-DOCK7 (DOCK7-Ab), or an anti-p116 Rip (p116 Rip -Ab) antibody and then were analyzed by immunoblotting with antibodies to DOCK7 and p116 Rip . Molecular masses are shown in kilodaltons. (G and H) Colocalization of DOCK7 and p116 Rip in V-SVZ–derived neuroblasts. (G) Coronal sections of P10 mouse forebrain at position III in the RMS as indicated in the cartoon in immunostained with antibodies to DOCK7 and p116 Rip and counterstained with DAPI. Boxed regions are enlarged and shown at the bottom. (H) Neuroblasts dissociated from V-SVZ tissue of P1–3 mice were fixed at 30 h in vitro, followed by immunostaining with indicated antibodies and counterstained with DAPI. Bars: (C and G, top) 50 µm; (G, bottom, and H) 10 µm.
Techniques Used: Transformation Assay, Expressing, Binding Assay, Activation Assay, Plasmid Preparation, Immunoprecipitation, Western Blot, Staining, Incubation, Derivative Assay, In Vitro, Immunostaining
Figure Legend Snippet: DOCK7 interaction with p116 Rip is essential for neuroblast migration along the RMS. (A) Composite confocal images of forebrains of mice electroporated at P3 with plasmids expressing EGFP and Dock7#2, Dock7#2 + DOCK7, or Dock7#2 + DOCK7Δp116 Rip and sacrificed at P10, showing distribution of EGFP + transfected neuroblasts along the V-SVZ–RMS–OB pathway. Slices were counterstained with DAPI. Dotted lines outline borders of sagittal slices. Bar, 500 µm. (B) Quantification of the distribution of EGFP + transfected cells along the V-SVZ–RMS–OB pathway. n = 1,316–1,791 cells from at least three animals for each condition. (C) Quantification of the length of the LP of neuroblasts expressing indicated constructs. n = 91–680 cells from at least three animals for each condition. (D–G) P2–3 mouse pups were electroporated with a tdTomato-expressing plasmid together with one of the indicated constructs. Acute sagittal brain slices were prepared 5 d later and subjected to confocal live-cell imaging. Graphs show quantifications of the mean migrated distance (D), displacement (E), velocity (F), and number of branching events per h (G) for the tdTomato + transfected neuroblasts. n = 50–61 cells from five to seven animals for each condition. Data are shown as means ± SEM. *, P < 0.05; **, P < 0.01; ***, P < 0.001; ****, P < 0.0001; ns, P > 0.05 compared with scr#1; one-way ANOVA with Dunnett’s post hoc test.
Techniques Used: Migration, Expressing, Transfection, Construct, Plasmid Preparation, Live Cell Imaging
Figure Legend Snippet: DOCK7/p116 Rip signaling controls somal translocation. (A–F) Neuroblasts dissociated from the V-SVZ of P1–3 mice were coelectroporated with one of the indicated constructs and a plasmid coexpressing EGFP and PACT-mKO1, a marker for the centrosome. Cells were reaggregated, embedded in Matrigel, and subjected to confocal live-cell imaging. (A) Examples of time-lapse series showing centrosome and cell soma movements during migration in neuroblasts transfected with indicated constructs. Images are taken from Videos 8–12. Signals of EGFP and PACT-mKO1 are shown in green and red, respectively. White dashed lines indicate advancement of the rear edge of each cell. Arrowheads indicate centrosome position. Bars, 10 µm. (B and C) Temporal changes in the distance between the nucleus and the centrosome (N–C distance; B) and velocity of the cell body (green lines) and the centrosome (red lines; C) in migrating neuroblasts expressing indicated constructs. (D–F) Quantification of velocity (D), somal translocation events (E), and maximum nucleus–centrosome distance (F) for neuroblasts expressing indicated constructs. n = 6 cells (scr#2); n = 5 cells (p116 Rip #1); n = 7 cells (Dock7#2); n = 12 cells (Dock7#2 + DOCK7); and n = 8 cells (Dock7#2 + DOCK7Δp116 Rip ); from 5–12 animals for each condition. Data are shown as means ± SEM. *, P < 0.05; **, P < 0.01; ***, P < 0.001; ns, P > 0.05; one-way ANOVA with Dunnett’s post hoc test.
Techniques Used: Translocation Assay, Construct, Plasmid Preparation, Marker, Live Cell Imaging, Migration, Transfection, Expressing
Figure Legend Snippet: DOCK7/p116 Rip signaling controls somal translocation through F-actin remodeling at the cell rear. (A) Neuroblasts dissociated from the V-SVZ of P1–3 mice were coelectroporated with one of the indicated constructs and a plasmid coexpressing Lifeact-EGFP, a marker for F-actin, and PACT-mKO1. Cells were reaggregated, embedded in Matrigel, and subjected to confocal live-cell imaging. Examples of time-lapse series showing F-actin remodeling during migration in neuroblasts transfected with indicated constructs. Signals of Lifeact-EGFP and PACT-mKO1 are shown in green and red, respectively. White dashed lines indicate advancement of the rear edge (RE) of each cell. White and yellow arrowheads indicate position of centrosome ahead of the nucleus and formation of F-actin condensation at the cell rear, respectively. Linescan profiles to the left of each image show the signal intensities of Lifeact-EGFP (green lines) and PACT-mKO1 (red lines) from the rear edge of the cell soma to the tip of the LP in the corresponding images. Representative images of a total of 5–12 independent experiments/condition are shown. (B) Enrichment of DOCK7 and p116 Rip signals at the cell rear during somal translocation. Reaggregated neuroblasts isolated from V-SVZ tissue of P1–3 mice were embedded in Matrigel and allowed to migrate for 30 h before immunostaining for DOCK7 and p116 Rip . Representative images of neuroblasts captured before (top two rows) and during somal translocation (bottom row) are shown. Enrichment of DOCK7 and p116 Rip signals at the cell rear just before and during somal translocation is indicated by arrowheads. Bars, 10 µm.
Techniques Used: Translocation Assay, Construct, Plasmid Preparation, Marker, Live Cell Imaging, Migration, Transfection, Isolation, Immunostaining
![RPA1 phosphorylated by PAK1 at Ser-135 and Thr-180 is critical for its role in replication stress response. ( A–C ) Control or DOCK7-depleted HEK293T cells were transfected with indicated FLAG-RPA1 constructs for 24 h. Cells were then pretreated with or without inhibitors (R-ketorolac or PAK1 inhibitor) before or after HU treatment. FLAG-RPA1 was coimmunoprecipitated from cell lysates and loaded on both normal and Phospho-tag gel, thereafter blotted with indicated antibodies. ( D ) Purified WT and ST/A mutant of RPA1 were incubated with or without constitutively active PAK1 (50 aa-150 aa) and incubated with γ- [32P] ATP for 30 min at 30°C before subjected to autoradiography. ( E–G ) Control or RPA1-depleted U2OS cells were transfected with WT or ST/A mutant of FLAG-RPA1 for 24 h before treatment with 10 mM HU for 1 h, and then the distribution of RPA1 and RPA2 in the chromatin and soluble fractions of cells were determined by immunoblotting (E). Representative images (F) and quantification (G) of RPA2 foci were analyzed by immunofluorescence. More than 200 cells were counted in each experiment. Error bars represent SEM from three independent experiments. ***p<0.001. ( H–J ) RPA1-depleted cells were transfected with WT or ST/A mutant of FLAG-RPA1 for 24 h before HU treatment, and then IPOND assay in HEK293T cells was performed to detect the distribution of the WT or ST/A mutant of RPA1 on the replication fork (H). DNA fiber assay in U2OS cells was performed to detect the length of CIdU track after HU was removed (J), and the representative pictures are shown in panel (I). The graphs represent mean ± S.D., two-tailed, unpaired t -test. ***p<0.001. ( K ) Control or RPA1-depleted U2OS cells were transfected with vector control, WT or ST/A mutant of FLAG-RPA1 for 24 h, treated with the indicated concentrations of HU and survival was measured using the colony formation assay. Error bars represent SEM from three independent experiments. ( L ) The protein stability of WT or ST/A mutant of RPA1 in the chromatin and soluble fraction of RPA1-depleted HEK293T cells under CHX treatment were analyzed by immunoblotting assay. ( M ) RPA1-depleted HEK293T cells were transfected with WT or ST/A mutant of FLAG-RPA1 and His-Ub for 24 h before HU treatment. Chromatin and soluble fractions derived from harvested cells were immunoprecipitated with nickel (His) beads and then blotted with indicated antibodies](https://pub-med-central-images-cdn.bioz.com/pub_med_central_ids_ending_with_4614/pmc08034614/pmc08034614__gkab134fig5.jpg)
