Structured Review

Becton Dickinson anti gapdh
Down-regulation of BACE1 protein in aged Mgat3 −/− mouse brain Immunostaining of 12-month-old brain sections (cerebral cortex) with anti-BACE1. Scale bar, 100 μm. Proteins from the membrane fractions of 12-month-old mouse brains ( n = 4–5) were immunoblotted for BACE1, and BACE1 intensity was quantified. * P = 0.044. Lysates from MEFs were immunoblotted for <t>APP,</t> BACE1, or <t>GAPDH</t> (loading control), and BACE1 intensity was quantified ( n = 4). Amount of Aβ40 in the culture medium of immortalized MEFs ( n = 3). * P = 0.045. MEFs were transfected with control siRNA or GGA3-siRNA and then immunoblotted for BACE1, GGA3, or GAPDH (loading control) ( n = 6). Data Information: All graphs show means ± SEM (* P
Anti Gapdh, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 92/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/anti gapdh/product/Becton Dickinson
Average 92 stars, based on 3 article reviews
Price from $9.99 to $1999.99
anti gapdh - by Bioz Stars, 2020-09
92/100 stars

Images

1) Product Images from "An aberrant sugar modification of BACE1 blocks its lysosomal targeting in Alzheimer's disease"

Article Title: An aberrant sugar modification of BACE1 blocks its lysosomal targeting in Alzheimer's disease

Journal: EMBO Molecular Medicine

doi: 10.15252/emmm.201404438

Down-regulation of BACE1 protein in aged Mgat3 −/− mouse brain Immunostaining of 12-month-old brain sections (cerebral cortex) with anti-BACE1. Scale bar, 100 μm. Proteins from the membrane fractions of 12-month-old mouse brains ( n = 4–5) were immunoblotted for BACE1, and BACE1 intensity was quantified. * P = 0.044. Lysates from MEFs were immunoblotted for APP, BACE1, or GAPDH (loading control), and BACE1 intensity was quantified ( n = 4). Amount of Aβ40 in the culture medium of immortalized MEFs ( n = 3). * P = 0.045. MEFs were transfected with control siRNA or GGA3-siRNA and then immunoblotted for BACE1, GGA3, or GAPDH (loading control) ( n = 6). Data Information: All graphs show means ± SEM (* P
Figure Legend Snippet: Down-regulation of BACE1 protein in aged Mgat3 −/− mouse brain Immunostaining of 12-month-old brain sections (cerebral cortex) with anti-BACE1. Scale bar, 100 μm. Proteins from the membrane fractions of 12-month-old mouse brains ( n = 4–5) were immunoblotted for BACE1, and BACE1 intensity was quantified. * P = 0.044. Lysates from MEFs were immunoblotted for APP, BACE1, or GAPDH (loading control), and BACE1 intensity was quantified ( n = 4). Amount of Aβ40 in the culture medium of immortalized MEFs ( n = 3). * P = 0.045. MEFs were transfected with control siRNA or GGA3-siRNA and then immunoblotted for BACE1, GGA3, or GAPDH (loading control) ( n = 6). Data Information: All graphs show means ± SEM (* P

Techniques Used: Immunostaining, Transfection

BACE1 is directed to late endosomes/lysosomes in Mgat3 −/− cells BACE1 from 2-week-old mouse brains was immunoprecipitated and immunoblotted (left). Immunoprecipitated BACE1 activity was measured in vitro (right, n = 3). The values of Bace1 −/− samples were subtracted as a background. N.S., P = 0.101. MEF homogenates were fractionated by sucrose density centrifugation and immunoblotted for BACE1, APP, rab5, or rab7. EE, early endosome; LE, late endosome. Brain homogenates were fractionated by sucrose density centrifugation and immunoblotted for BACE1, rab5, or rab9. EE, early endosome; LE, late endosome. Signal intensities were quantified and are shown in the right graphs. Immunostaining of 12-month-old mouse cerebral cortex for BACE1 and APP. A typical image in the vicinity of plaque-forming area is shown for hAPP/Mgat3 +/+ brain. The area of co-localization was quantified using random images of cerebral cortex ( n = 10). * P = 0.015. Immunoblot of BACE1 or GAPDH (loading control) from immortalized MEFs treated with a proteasome inhibitor (MG132) or a lysosome inhibitor (chloroquine; CQ). Immunostaining of 12-month-old mouse cerebral cortex for BACE1 (F), or nicastrin (G), and Lamp1. LE, late endosome. Scale bar, 10 μm. The area in which co-localized staining was observed was quantified as a percentage of the total BACE1-positive area (right, n = 10). ** P = 0.007. Data information: All graphs show means ± SEM (Student's t -test). Source data are available online for this figure.
Figure Legend Snippet: BACE1 is directed to late endosomes/lysosomes in Mgat3 −/− cells BACE1 from 2-week-old mouse brains was immunoprecipitated and immunoblotted (left). Immunoprecipitated BACE1 activity was measured in vitro (right, n = 3). The values of Bace1 −/− samples were subtracted as a background. N.S., P = 0.101. MEF homogenates were fractionated by sucrose density centrifugation and immunoblotted for BACE1, APP, rab5, or rab7. EE, early endosome; LE, late endosome. Brain homogenates were fractionated by sucrose density centrifugation and immunoblotted for BACE1, rab5, or rab9. EE, early endosome; LE, late endosome. Signal intensities were quantified and are shown in the right graphs. Immunostaining of 12-month-old mouse cerebral cortex for BACE1 and APP. A typical image in the vicinity of plaque-forming area is shown for hAPP/Mgat3 +/+ brain. The area of co-localization was quantified using random images of cerebral cortex ( n = 10). * P = 0.015. Immunoblot of BACE1 or GAPDH (loading control) from immortalized MEFs treated with a proteasome inhibitor (MG132) or a lysosome inhibitor (chloroquine; CQ). Immunostaining of 12-month-old mouse cerebral cortex for BACE1 (F), or nicastrin (G), and Lamp1. LE, late endosome. Scale bar, 10 μm. The area in which co-localized staining was observed was quantified as a percentage of the total BACE1-positive area (right, n = 10). ** P = 0.007. Data information: All graphs show means ± SEM (Student's t -test). Source data are available online for this figure.

Techniques Used: Immunoprecipitation, Activity Assay, In Vitro, Centrifugation, Immunostaining, Staining

2) Product Images from "USP9X destabilizes pVHL and promotes cell proliferation"

Article Title: USP9X destabilizes pVHL and promotes cell proliferation

Journal: Oncotarget

doi: 10.18632/oncotarget.11139

USP9X negatively regulates pVHL A. Western blot analysis of pVHL protein levels in USP9X knockdown cells. HEK293T cells were infected with scramble or shUSP9X lentivirus for 48 hours. After harvesting cells were immunoblotted with indicated antibodies. B. Relative VHL mRNA levels in USP9X knockdown cells. Either VHL or USP9X was knocked down in HEK293T cells and mRNA levels of VHL were determined by qPCR. The expression levels are normalized to the GAPDH mRNA level. The results represent the mean ± SEM of three independent experiments and were analyzed with the Student's t -test. * p
Figure Legend Snippet: USP9X negatively regulates pVHL A. Western blot analysis of pVHL protein levels in USP9X knockdown cells. HEK293T cells were infected with scramble or shUSP9X lentivirus for 48 hours. After harvesting cells were immunoblotted with indicated antibodies. B. Relative VHL mRNA levels in USP9X knockdown cells. Either VHL or USP9X was knocked down in HEK293T cells and mRNA levels of VHL were determined by qPCR. The expression levels are normalized to the GAPDH mRNA level. The results represent the mean ± SEM of three independent experiments and were analyzed with the Student's t -test. * p

Techniques Used: Western Blot, Infection, Real-time Polymerase Chain Reaction, Expressing

CP2005 induces pVHL through targeting USP9X to inhibit tumor cells growth A. and B. HepG2 and PC3 cells were treated with CP2005 (2.5 μM) for indicated periods of time. After harvesting cells were immunoblotted with indicated antibodies. C. and D. HepG2 and PC3 cells were treated with vehicle control or CP2005 (2.5 μM) for 1 hour, and GLUT1 mRNA levels were determined by qPCR. The expression levels are normalized to the GAPDH mRNA level. The results represent the mean ± SEM of three independent experiments and were analyzed with the Student's t -test. ** p
Figure Legend Snippet: CP2005 induces pVHL through targeting USP9X to inhibit tumor cells growth A. and B. HepG2 and PC3 cells were treated with CP2005 (2.5 μM) for indicated periods of time. After harvesting cells were immunoblotted with indicated antibodies. C. and D. HepG2 and PC3 cells were treated with vehicle control or CP2005 (2.5 μM) for 1 hour, and GLUT1 mRNA levels were determined by qPCR. The expression levels are normalized to the GAPDH mRNA level. The results represent the mean ± SEM of three independent experiments and were analyzed with the Student's t -test. ** p

Techniques Used: Real-time Polymerase Chain Reaction, Expressing

3) Product Images from "MicroRNA-21-5p promotes proliferation of gastric cancer cells through targeting SMAD7"

Article Title: MicroRNA-21-5p promotes proliferation of gastric cancer cells through targeting SMAD7

Journal: OncoTargets and therapy

doi: 10.2147/OTT.S163771

The over-expression of miR-21 enhances GC cells via SMAD signaling pathway. Notes: ( A ) Western blot for the expressions of SMAD2, SMAD3, SMAD7 in SGC-7901 cells transfected with miR-21-5p inhibitors and miR-21-5p mimics. GAPDH was used as the loading control. ( B ) Statistical results of Western blot analyzed on SPSS 16.0 (* P
Figure Legend Snippet: The over-expression of miR-21 enhances GC cells via SMAD signaling pathway. Notes: ( A ) Western blot for the expressions of SMAD2, SMAD3, SMAD7 in SGC-7901 cells transfected with miR-21-5p inhibitors and miR-21-5p mimics. GAPDH was used as the loading control. ( B ) Statistical results of Western blot analyzed on SPSS 16.0 (* P

Techniques Used: Over Expression, Western Blot, Transfection

4) Product Images from "Staufen1 Regulates Multiple Alternative Splicing Events either Positively or Negatively in DM1 Indicating Its Role as a Disease Modifier"

Article Title: Staufen1 Regulates Multiple Alternative Splicing Events either Positively or Negatively in DM1 Indicating Its Role as a Disease Modifier

Journal: PLoS Genetics

doi: 10.1371/journal.pgen.1005827

Stau1 regulates splicing of INSR exon 11 through an interaction with Alu elements in intron 10. (A) The genomic DNA sequence of the human INSR (NG_008852.1) was used to assess the Alu elements located in intron 10. Introns are not to scale, and this is indicated in intron 11 (//). The IR-minigene constructs used in this study are shown here. Previously deleted segments of genomic DNA determined not to influence exon 11 splicing are indicated in intron 11 (Δ symbol), and black dotted lines represent the deleted segment containing the three Alu elements. (B) HeLa cells were transiently transfected with Stau1-HA plasmid and either the WT or ΔAlus IR-minigene. Immunoprecipitation (IP) of Stau1-HA protein was carried out using HA-specific antibodies under RNase-free conditions. Western blot using HA-antibodies show equal amounts of Stau1-HA protein was immunoprecipitated in each condition. RNA was collected and DNase-treated prior to cDNA synthesis. RT-PCR was performed using GAPDH specific primers to demonstrate a lack of non-specific binding of RNA to the beads used for immunoprecipitation. Equal amounts of transfected minigenes were confirmed by performing RT-PCR on the cDNA synthesized from the 10% inputs lysates with primers specific to amplify a portion of the plasmid vector (pSG5) and the IR-minigene (Exon 10), corresponds to the pSG5-E10 labelled band. RT-qPCR was carried out using primers specific to an 115 bp region of intron 10 of the IR-minigene to determine the amount of IR-minigene RNA bound to immunoprecipitated Stau1-HA. Bar graphs show an average of four independent RIP experiments. (C-D) HeLa cells were transiently transfected with a CTRL, Stau1-HA plasmid or shStau1 and either the WT or ΔAlus IR-minigene. IR-minigene splicing was determined by RT-PCR. The average of ≥3 independent experiments was used. Error bars represent SEM * = p
Figure Legend Snippet: Stau1 regulates splicing of INSR exon 11 through an interaction with Alu elements in intron 10. (A) The genomic DNA sequence of the human INSR (NG_008852.1) was used to assess the Alu elements located in intron 10. Introns are not to scale, and this is indicated in intron 11 (//). The IR-minigene constructs used in this study are shown here. Previously deleted segments of genomic DNA determined not to influence exon 11 splicing are indicated in intron 11 (Δ symbol), and black dotted lines represent the deleted segment containing the three Alu elements. (B) HeLa cells were transiently transfected with Stau1-HA plasmid and either the WT or ΔAlus IR-minigene. Immunoprecipitation (IP) of Stau1-HA protein was carried out using HA-specific antibodies under RNase-free conditions. Western blot using HA-antibodies show equal amounts of Stau1-HA protein was immunoprecipitated in each condition. RNA was collected and DNase-treated prior to cDNA synthesis. RT-PCR was performed using GAPDH specific primers to demonstrate a lack of non-specific binding of RNA to the beads used for immunoprecipitation. Equal amounts of transfected minigenes were confirmed by performing RT-PCR on the cDNA synthesized from the 10% inputs lysates with primers specific to amplify a portion of the plasmid vector (pSG5) and the IR-minigene (Exon 10), corresponds to the pSG5-E10 labelled band. RT-qPCR was carried out using primers specific to an 115 bp region of intron 10 of the IR-minigene to determine the amount of IR-minigene RNA bound to immunoprecipitated Stau1-HA. Bar graphs show an average of four independent RIP experiments. (C-D) HeLa cells were transiently transfected with a CTRL, Stau1-HA plasmid or shStau1 and either the WT or ΔAlus IR-minigene. IR-minigene splicing was determined by RT-PCR. The average of ≥3 independent experiments was used. Error bars represent SEM * = p

Techniques Used: Sequencing, Construct, Transfection, Plasmid Preparation, Immunoprecipitation, Western Blot, Reverse Transcription Polymerase Chain Reaction, Binding Assay, Synthesized, Quantitative RT-PCR

Stau1 levels regulate the pre-mRNA splicing of the human INSR in HeLa cells. (A) pGIPZ (CTRL) or Stau1-HA (Stau1-HA) plasmids were transiently transfected into HeLa cell lines, and total RNA and protein lysate was collected after 48 hours. RT-PCR using primers specific to the human endogenous INSR were used on cDNA synthesized from total RNA to amplify the two isoforms (IR-A and IR-B) of the INSR . Stau1-HA protein levels were assessed by Western blot using HA-specific antibodies, and GAPDH was used as a loading control. (B) shCTRL or shStau1 were transiently transfected into HeLa cell lines and total RNA and protein lysate was collected after 48 hours. RT-PCR was performed to amplify the INSR isoforms. Stau1 protein levels were assessed by Western blot and quantified using GAPDH as a loading control. (C) Representative Western blots showing protein levels of CUGBP1, MBNL1 and hnRNP H in HeLa cells transfected with CTRL, shRNA or Stau1-HA plasmids. GAPDH was used as a loading control. (D) Quantification of Western blot analysis of splicing factors upon Stau1 level modulation. In all cases, bar graphs show an average of ≥3 independent experiments. Error bars represent SEM * = p
Figure Legend Snippet: Stau1 levels regulate the pre-mRNA splicing of the human INSR in HeLa cells. (A) pGIPZ (CTRL) or Stau1-HA (Stau1-HA) plasmids were transiently transfected into HeLa cell lines, and total RNA and protein lysate was collected after 48 hours. RT-PCR using primers specific to the human endogenous INSR were used on cDNA synthesized from total RNA to amplify the two isoforms (IR-A and IR-B) of the INSR . Stau1-HA protein levels were assessed by Western blot using HA-specific antibodies, and GAPDH was used as a loading control. (B) shCTRL or shStau1 were transiently transfected into HeLa cell lines and total RNA and protein lysate was collected after 48 hours. RT-PCR was performed to amplify the INSR isoforms. Stau1 protein levels were assessed by Western blot and quantified using GAPDH as a loading control. (C) Representative Western blots showing protein levels of CUGBP1, MBNL1 and hnRNP H in HeLa cells transfected with CTRL, shRNA or Stau1-HA plasmids. GAPDH was used as a loading control. (D) Quantification of Western blot analysis of splicing factors upon Stau1 level modulation. In all cases, bar graphs show an average of ≥3 independent experiments. Error bars represent SEM * = p

Techniques Used: Transfection, Reverse Transcription Polymerase Chain Reaction, Synthesized, Western Blot, shRNA

5) Product Images from "Cell-permeable iron inhibits vascular endothelial growth factor receptor-2 signaling and tumor angiogenesis"

Article Title: Cell-permeable iron inhibits vascular endothelial growth factor receptor-2 signaling and tumor angiogenesis

Journal: Oncotarget

doi: 10.18632/oncotarget.11689

Cell-permeable iron inhibits VEGFR-2 signaling through FAK and p38 MAPK affecting migration HUVEC-I cells were stimulated with VEGF-A (100 ng/ml) for 10 min to 60 min in the presence of 35 μM iron. ( A ) Cell lysates were then analyzed by Western blots to determine relative levels of phosphorylated FAK (pTyr-397 and pTyr-861). ( B ) Cumulative data showing relative levels of FAK phosphorylation and total FAK levels from two-four independent experiments. ( C ) Western blots showing phosphorylated p38-MAPK and total levels of PTP1B following VEGF-A stimulation of HUVEC-I cells in the presence of cell-permeable iron. ( D ) Densitometric analyses of Western blots from two independent experiments. Beta-Actin levels were used for normalization of phospho and total p38 MAPK levels. GAPDH levels were used to normalize PTP1B levels. * P
Figure Legend Snippet: Cell-permeable iron inhibits VEGFR-2 signaling through FAK and p38 MAPK affecting migration HUVEC-I cells were stimulated with VEGF-A (100 ng/ml) for 10 min to 60 min in the presence of 35 μM iron. ( A ) Cell lysates were then analyzed by Western blots to determine relative levels of phosphorylated FAK (pTyr-397 and pTyr-861). ( B ) Cumulative data showing relative levels of FAK phosphorylation and total FAK levels from two-four independent experiments. ( C ) Western blots showing phosphorylated p38-MAPK and total levels of PTP1B following VEGF-A stimulation of HUVEC-I cells in the presence of cell-permeable iron. ( D ) Densitometric analyses of Western blots from two independent experiments. Beta-Actin levels were used for normalization of phospho and total p38 MAPK levels. GAPDH levels were used to normalize PTP1B levels. * P

Techniques Used: Migration, Western Blot

Cell-permeable iron inhibits VEGFR-2 receptor phosphorylation and downstream signaling HUVEC-I cells were stimulated with VEGF-A (100 ng/ml) for 10 min to 60 min in the presence of 35 μM iron. ( A ) Cell lysates were probed for phosphorylated tyrosine residues (pTyr-1175 and pTyr-1214) by Western blots using site-specific antibodies. Representative blot from two-three independent experiments is shown. ( B ) Densitometry analyses were used to determine relative levels of phosphorylated VEGFR-2 and total VEGFR-2. GAPDH levels were used for normalization for pTyr-1175 and total receptor levels. Beta-Actin levels were used for normalizing pTyr-1214 VEGFR-2 levels. Data represent mean ± SD from two-three independent experiments. ( C ) Representative Western blot showing phosphorylated p44/p42 MAPK and phosphorylated AKT. ( D ) Densitometric analysis of relative levels of phosphorylated and total p44/p42 MAPK and p-AKT. GAPDH levels were used for normalization. Data represent mean ± SD from two-three independent experiments. * P
Figure Legend Snippet: Cell-permeable iron inhibits VEGFR-2 receptor phosphorylation and downstream signaling HUVEC-I cells were stimulated with VEGF-A (100 ng/ml) for 10 min to 60 min in the presence of 35 μM iron. ( A ) Cell lysates were probed for phosphorylated tyrosine residues (pTyr-1175 and pTyr-1214) by Western blots using site-specific antibodies. Representative blot from two-three independent experiments is shown. ( B ) Densitometry analyses were used to determine relative levels of phosphorylated VEGFR-2 and total VEGFR-2. GAPDH levels were used for normalization for pTyr-1175 and total receptor levels. Beta-Actin levels were used for normalizing pTyr-1214 VEGFR-2 levels. Data represent mean ± SD from two-three independent experiments. ( C ) Representative Western blot showing phosphorylated p44/p42 MAPK and phosphorylated AKT. ( D ) Densitometric analysis of relative levels of phosphorylated and total p44/p42 MAPK and p-AKT. GAPDH levels were used for normalization. Data represent mean ± SD from two-three independent experiments. * P

Techniques Used: Western Blot

Related Articles

Western Blot:

Article Title: IFITM3 Inhibits Influenza A Virus Infection by Preventing Cytosolic Entry
Article Snippet: .. Antibodies The following antibodies were used in this study for either Western blotting (WB) or immunoflourescence (IF), or both as indicated, along with their respective source and catalogue number: Primary antibodies: Actin (Sigma A5316, WB), CD63 (Developmental Studies Hybridoma Bank (DSHB) clone H5C6, IF), Fragilis (mouse Ifitm3) (Abcam ab15592, WB, IF), GAPDH (BD Biosciences 610340, WB), HA (Wistar collection, Coriell Institute, clone H18-S210, WC00029, IF), IFITM3 (Abgent AP1153a, WB, IF), IFITM3 (Abgent AP1153c, IF), LAMP1 ((DSHB) clone H4A3, WB, IF), LC3 (Nanotools Mab LC3-5F10, WB, IF), MX1 (Proteintech 13750-1-AP, WB, IF), NP (Millipore clone H16-L10-4R5 MAB8800, IF), RAB7 (Abcam 50533, WB, IF). .. Secondary antibodies for IF (all from Invitrogen): Alexa Fluor 488 and 647 (goat anti-rabbit and goat anti-mouse).

Incubation:

Article Title: Caspase-3 dependent nitrergic neuronal apoptosis following cavernous nerve injury is mediated via RhoA and ROCK activation in major pelvic ganglion
Article Snippet: .. Proteins were transferred to polyvinylidene fluoride membranes and incubated with primary antibodies (ROCK1, ROCK2 (1:1000, Santa Cruz Biotechnology, Santa Cruz, CA), total casapse-3, activated caspase-3 (1:1000 Cell Signaling, Beverly, MA), nNOS (1:200 Santa Cruz), GAPDH (1:2500 BD Bioscience) and actin (1:500 (Sigma Aldrich, St. Louis, MO)) overnight at 4 °C. .. The membranes were incubated with a horseradish peroxidase-linked secondary antibody and visualized using an enhanced chemiluminescence kit (Amersham).

Article Title: Gelsolin-Cu/ZnSOD interaction alters intracellular reactive oxygen species levels to promote cancer cell invasion
Article Snippet: .. Membranes were blocked with 5% w/v milk (Blocking grade milk, Bio-Rad) for 1 h and incubated overnight at 4o C with primary antibodies against gelsolin (Abcam, UK), Cu/ZnSOD (Cell Signaling, MA, USA), MnSOD (BD), VDAC (Cell Signaling); GAPDH (BD Biosciences) and β-actin (Sigma-Aldrich). .. The membranes were washed and incubated with horse radish peroxidase-conjugated secondary antibodies.

Article Title: MicroRNA-21-5p promotes proliferation of gastric cancer cells through targeting SMAD7
Article Snippet: .. After that, the gels were transferred to polyvinylidene difluoride (PVDF) membranes, which were incubated with rabbit polyclonal anti-SMAD2 (dilution 1:800), anti-SMAD3 (1:1,000), anti-SMAD7 (1:1,200), and anti-GAPDH (1:600) antibodies (all BD, Franklin Lakes, NJ, USA) overnight at 4°C. .. After washing with PBS three times, the membranes were incubated with a secondary polyclonal peroxidase labeled antibody for 2 h, and detected using autoradiography films (Amersham HyperFilm ECL; GE Healthcare, Fairfield, Connecticut, USA).

other:

Article Title: An aberrant sugar modification of BACE1 blocks its lysosomal targeting in Alzheimer's disease
Article Snippet: Antibodies and lectin The commercially available antibodies used were as follows: rabbit anti-BACE1 (5606), anti-nicastrin (9447S), anti-GGA3 (8027), anti-rab5 (3547), anti-rab7 (9367), and anti-rab9 (5118) from Cell Signaling Technology; anti-APP C-term (recognizes C-terminal part of APP, 18961), anti-APP N-term (10D1), and anti-sAPPβ-sw (10321, clone 6A1) from Immuno-Biological Laboratories; anti-Aβ (SIG-39220, clone 4G8) and anti-sAPPα (SIG-39320, clone 6E10) from SIGNET; anti-Lamp1 (ab25630) and anti-PSD95 (ab2723) from Abcam; anti-actin (A4700) from Sigma; anti-syntaxin 6 (610635) from BD Biosciences; anti-GAPDH (MAB374), anti-APP (22C11), and anti-MBP (MAB386) from Millipore; anti-MAP2 (sc-20172) from Santa Cruz Biotechnology; anti-GFAP (13-0300) from Life Technologies; anti-CHL1 (AF2147) and anti-contactin-2 (AF4439) from R & D systems; and anti-Iba1 (019-197419) from Wako.

Blocking Assay:

Article Title: Gelsolin-Cu/ZnSOD interaction alters intracellular reactive oxygen species levels to promote cancer cell invasion
Article Snippet: .. Membranes were blocked with 5% w/v milk (Blocking grade milk, Bio-Rad) for 1 h and incubated overnight at 4o C with primary antibodies against gelsolin (Abcam, UK), Cu/ZnSOD (Cell Signaling, MA, USA), MnSOD (BD), VDAC (Cell Signaling); GAPDH (BD Biosciences) and β-actin (Sigma-Aldrich). .. The membranes were washed and incubated with horse radish peroxidase-conjugated secondary antibodies.

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    Becton Dickinson gapdh antibody
    “Endothelial nitric oxide synthase knockdown” HAECs were transduced with adenovirus (MOI of 20) encoding either RFP (control), S17-eNOS (Golgi targeted), or CAAX–eNOS (PM targeted) . Twenty-four hours later, cells were treated with L-NAME (1 mM) for 30 min, and TNFα (1 ng/ml) was added for an additional 24 h. Cell lysates were immunoblotted with <t>anti-ICAM-1,</t> anti-eNOS, and <t>anti-GAPDH</t> antibodies.
    Gapdh Antibody, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 92/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/gapdh antibody/product/Becton Dickinson
    Average 92 stars, based on 6 article reviews
    Price from $9.99 to $1999.99
    gapdh antibody - by Bioz Stars, 2020-09
    92/100 stars
      Buy from Supplier

    90
    Becton Dickinson mouse anti gapdh monoclonal antibody
    Assessment of autophagic flux in HC04 cells. ( A ) Human liver HC04 cells were mock infected or infected with B. pseudomallei or its rpoS mutant at MOI 10 in the presence or absence of bafilomycin A1 and at 2, 4 and 8 h.p.i. expression of <t>LC3-I</t> (14kDa) and II (16kDa) determined by western blotting. <t>GAPDH</t> were used as a loading control for each condition. The intensity of LC3-II and GAPDH were determined using ImageJ software and the numbers below the blots show the ratio between LC3-II and GAPDH. ( B ) The plot of autophagic flux in HC04 cells as determined from A. Statistical analyses were undertaken using SigmaPlot 11.0 one-way ANOVA. Lower case letters indicate a significant difference from the corresponding upper case letters ( P -value
    Mouse Anti Gapdh Monoclonal Antibody, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 90/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mouse anti gapdh monoclonal antibody/product/Becton Dickinson
    Average 90 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    mouse anti gapdh monoclonal antibody - by Bioz Stars, 2020-09
    90/100 stars
      Buy from Supplier

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    “Endothelial nitric oxide synthase knockdown” HAECs were transduced with adenovirus (MOI of 20) encoding either RFP (control), S17-eNOS (Golgi targeted), or CAAX–eNOS (PM targeted) . Twenty-four hours later, cells were treated with L-NAME (1 mM) for 30 min, and TNFα (1 ng/ml) was added for an additional 24 h. Cell lysates were immunoblotted with anti-ICAM-1, anti-eNOS, and anti-GAPDH antibodies.

    Journal: Frontiers in Physiology

    Article Title: Exogenous, but not Endogenous Nitric Oxide Inhibits Adhesion Molecule Expression in Human Endothelial Cells

    doi: 10.3389/fphys.2012.00003

    Figure Lengend Snippet: “Endothelial nitric oxide synthase knockdown” HAECs were transduced with adenovirus (MOI of 20) encoding either RFP (control), S17-eNOS (Golgi targeted), or CAAX–eNOS (PM targeted) . Twenty-four hours later, cells were treated with L-NAME (1 mM) for 30 min, and TNFα (1 ng/ml) was added for an additional 24 h. Cell lysates were immunoblotted with anti-ICAM-1, anti-eNOS, and anti-GAPDH antibodies.

    Article Snippet: ICAM-1 antibody was purchased from Santa Cruz. eNOS and GAPDH antibody were purchased from BD.

    Techniques: Transduction

    (A) Human aortic endothelial cells were incubated with TNFα (1 ng/ml) for 4, 8, and 24 h, in the presence and absence of L-NAME (1 mM, 30 min pre-treatment). Cell lysates were immunoblotted using an anti-ICAM-1 antibody and GAPDH was used as a loading control. (B) HAECs were pre-treated with L-NAME for 30 min, and stimulated with different concentrations of TNFα (0.5, 0.1, 1 ng/ml) for 24 h. (C) HAECs were treated with different concentrations of L-NAME (1 or 2 mM) for 30 min, and then exposed to TNFα (1 ng/ml) for another 24 h. (D) HAECs were pre-treated with L-NAME (1 mM) for different times (30 min or 24 h) prior to exposure to TNFα (1 ng/ml) for an additional 24 h. Cell lysates were immunoblotted using an anti-ICAM-1 or anti-VCAM-1 antibody and GAPDH was used as a loading control.

    Journal: Frontiers in Physiology

    Article Title: Exogenous, but not Endogenous Nitric Oxide Inhibits Adhesion Molecule Expression in Human Endothelial Cells

    doi: 10.3389/fphys.2012.00003

    Figure Lengend Snippet: (A) Human aortic endothelial cells were incubated with TNFα (1 ng/ml) for 4, 8, and 24 h, in the presence and absence of L-NAME (1 mM, 30 min pre-treatment). Cell lysates were immunoblotted using an anti-ICAM-1 antibody and GAPDH was used as a loading control. (B) HAECs were pre-treated with L-NAME for 30 min, and stimulated with different concentrations of TNFα (0.5, 0.1, 1 ng/ml) for 24 h. (C) HAECs were treated with different concentrations of L-NAME (1 or 2 mM) for 30 min, and then exposed to TNFα (1 ng/ml) for another 24 h. (D) HAECs were pre-treated with L-NAME (1 mM) for different times (30 min or 24 h) prior to exposure to TNFα (1 ng/ml) for an additional 24 h. Cell lysates were immunoblotted using an anti-ICAM-1 or anti-VCAM-1 antibody and GAPDH was used as a loading control.

    Article Snippet: ICAM-1 antibody was purchased from Santa Cruz. eNOS and GAPDH antibody were purchased from BD.

    Techniques: Incubation

    (A) Human aortic endothelial cells were treated with L-NAME (1 mM) or DETA NONOate (1 mM) for 30 min, and then TNFα (1 ng/ml) was added for 24 h. Activation of NF-κB was detected by anti-ICAM-1 or anti-VCAM-1 antibodies. GAPDH was used as a loading control. (B) HAECs were plated into 96-well plate and cells were treated with the same condition as above, cell viability was detected by MTT assay 24 h after treatment. (C) Nitric oxide release from cells expressing RFP, S17-eNOS, CAAX–eNOS, or iNOS or from different concentrations (10, 30, 50, 100 μM) of DETA NONOate over 24 h. Results are presented as mean ± SEM ( n = 5). * p

    Journal: Frontiers in Physiology

    Article Title: Exogenous, but not Endogenous Nitric Oxide Inhibits Adhesion Molecule Expression in Human Endothelial Cells

    doi: 10.3389/fphys.2012.00003

    Figure Lengend Snippet: (A) Human aortic endothelial cells were treated with L-NAME (1 mM) or DETA NONOate (1 mM) for 30 min, and then TNFα (1 ng/ml) was added for 24 h. Activation of NF-κB was detected by anti-ICAM-1 or anti-VCAM-1 antibodies. GAPDH was used as a loading control. (B) HAECs were plated into 96-well plate and cells were treated with the same condition as above, cell viability was detected by MTT assay 24 h after treatment. (C) Nitric oxide release from cells expressing RFP, S17-eNOS, CAAX–eNOS, or iNOS or from different concentrations (10, 30, 50, 100 μM) of DETA NONOate over 24 h. Results are presented as mean ± SEM ( n = 5). * p

    Article Snippet: ICAM-1 antibody was purchased from Santa Cruz. eNOS and GAPDH antibody were purchased from BD.

    Techniques: Activation Assay, MTT Assay, Expressing

    The over-expression of miR-21 enhances GC cells via SMAD signaling pathway. Notes: ( A ) Western blot for the expressions of SMAD2, SMAD3, SMAD7 in SGC-7901 cells transfected with miR-21-5p inhibitors and miR-21-5p mimics. GAPDH was used as the loading control. ( B ) Statistical results of Western blot analyzed on SPSS 16.0 (* P

    Journal: OncoTargets and therapy

    Article Title: MicroRNA-21-5p promotes proliferation of gastric cancer cells through targeting SMAD7

    doi: 10.2147/OTT.S163771

    Figure Lengend Snippet: The over-expression of miR-21 enhances GC cells via SMAD signaling pathway. Notes: ( A ) Western blot for the expressions of SMAD2, SMAD3, SMAD7 in SGC-7901 cells transfected with miR-21-5p inhibitors and miR-21-5p mimics. GAPDH was used as the loading control. ( B ) Statistical results of Western blot analyzed on SPSS 16.0 (* P

    Article Snippet: After that, the gels were transferred to polyvinylidene difluoride (PVDF) membranes, which were incubated with rabbit polyclonal anti-SMAD2 (dilution 1:800), anti-SMAD3 (1:1,000), anti-SMAD7 (1:1,200), and anti-GAPDH (1:600) antibodies (all BD, Franklin Lakes, NJ, USA) overnight at 4°C.

    Techniques: Over Expression, Western Blot, Transfection

    Assessment of autophagic flux in HC04 cells. ( A ) Human liver HC04 cells were mock infected or infected with B. pseudomallei or its rpoS mutant at MOI 10 in the presence or absence of bafilomycin A1 and at 2, 4 and 8 h.p.i. expression of LC3-I (14kDa) and II (16kDa) determined by western blotting. GAPDH were used as a loading control for each condition. The intensity of LC3-II and GAPDH were determined using ImageJ software and the numbers below the blots show the ratio between LC3-II and GAPDH. ( B ) The plot of autophagic flux in HC04 cells as determined from A. Statistical analyses were undertaken using SigmaPlot 11.0 one-way ANOVA. Lower case letters indicate a significant difference from the corresponding upper case letters ( P -value

    Journal: FEMS Microbiology Letters

    Article Title: Burkholderia pseudomallei rpoS mediates iNOS suppression in human hepatocyte (HC04) cells

    doi: 10.1093/femsle/fnw161

    Figure Lengend Snippet: Assessment of autophagic flux in HC04 cells. ( A ) Human liver HC04 cells were mock infected or infected with B. pseudomallei or its rpoS mutant at MOI 10 in the presence or absence of bafilomycin A1 and at 2, 4 and 8 h.p.i. expression of LC3-I (14kDa) and II (16kDa) determined by western blotting. GAPDH were used as a loading control for each condition. The intensity of LC3-II and GAPDH were determined using ImageJ software and the numbers below the blots show the ratio between LC3-II and GAPDH. ( B ) The plot of autophagic flux in HC04 cells as determined from A. Statistical analyses were undertaken using SigmaPlot 11.0 one-way ANOVA. Lower case letters indicate a significant difference from the corresponding upper case letters ( P -value

    Article Snippet: The expression levels of LC3-II and Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH) were determined by western blotting using a rabbit anti-LC3 polyclonal antibody (2775S; Cell Signaling Technology) and a mouse anti-GAPDH monoclonal antibody (611463; BD Pharmacia, San Jose, CA, USA) followed by a Horseradish peroxidase (HRP)-conjugated goat anti-rabbit IgG antibody (sc2004; Santa Cruz Biotechnology, Inc.) and a HRP-conjugated goat anti-mouse IgG antibody (sc2005; Santa Cruz Biotechnology, Inc.).

    Techniques: Infection, Mutagenesis, Expressing, Western Blot, Software

    Transgenic expression of Ronin induces Atxn1. Representative Western blots of protein fractions collected by size exclusion chromatography of ( A ) cerebellar extracts or ( B ) mouse embryonic stem cell (mES) cell lysates. The size exclusion standards thyroglobulin (669 kDa) and ADH (150 kDa) are indicated. In the cerebellum, Ronin is part of a large protein complex that only partially overlaps with Hcf1. In ES cells, Atxn 1 expression is induced by transgenic expression of Ronin. Ronin and Hcf1 are eluting in similar fractions, indicating that they are part of the same protein complex. ( C ) Western blot analyses of equal protein amounts of ES cell lysates (left) or cerebellar extracts from 10-week-old animals (right) of indicated genotypes. While Atxn1 protein is not expressed in control ES cells overexpressing Luciferase (Ctrl), it is induced in Ronin overexpressing ES cells (R wt ) but not in cells overexpressing a Ronin mutant incapable of binding to Hcf1 (R mut ). Atxn1 levels are also elevated in vivo in transgenic (R tg ) animals when compared to wt controls. ( D ) Quantification of transgenic Ronin, Atxn1 and Gapdh protein levels as detected by Western blot in cerebellar extracts at 5 and 10 weeks of age. At 5 weeks, a ~1.5-fold induction of Atxn1 is observed in transgenic Ronin animals when compared with wildtype littermates. Reflective of the decrease in Purkinje cells, at 10 weeks of age the expression of transgenic Ronin and Atxn1 induction were drastically reduced in comparison to the earlier time point. n=3; **p

    Journal: bioRxiv

    Article Title: SCA4 locus-associated gene Ronin (Thap11) increases Ataxin-1 protein levels and induces cerebellar degeneration in a mouse model of ataxia

    doi: 10.1101/2020.03.04.977405

    Figure Lengend Snippet: Transgenic expression of Ronin induces Atxn1. Representative Western blots of protein fractions collected by size exclusion chromatography of ( A ) cerebellar extracts or ( B ) mouse embryonic stem cell (mES) cell lysates. The size exclusion standards thyroglobulin (669 kDa) and ADH (150 kDa) are indicated. In the cerebellum, Ronin is part of a large protein complex that only partially overlaps with Hcf1. In ES cells, Atxn 1 expression is induced by transgenic expression of Ronin. Ronin and Hcf1 are eluting in similar fractions, indicating that they are part of the same protein complex. ( C ) Western blot analyses of equal protein amounts of ES cell lysates (left) or cerebellar extracts from 10-week-old animals (right) of indicated genotypes. While Atxn1 protein is not expressed in control ES cells overexpressing Luciferase (Ctrl), it is induced in Ronin overexpressing ES cells (R wt ) but not in cells overexpressing a Ronin mutant incapable of binding to Hcf1 (R mut ). Atxn1 levels are also elevated in vivo in transgenic (R tg ) animals when compared to wt controls. ( D ) Quantification of transgenic Ronin, Atxn1 and Gapdh protein levels as detected by Western blot in cerebellar extracts at 5 and 10 weeks of age. At 5 weeks, a ~1.5-fold induction of Atxn1 is observed in transgenic Ronin animals when compared with wildtype littermates. Reflective of the decrease in Purkinje cells, at 10 weeks of age the expression of transgenic Ronin and Atxn1 induction were drastically reduced in comparison to the earlier time point. n=3; **p

    Article Snippet: Following antibodies were used: guinea pig polyclonal anti-Cic serum , mouse monoclonal anti-FLAG M2 (F7425; Sigma), rabbit polyclonal anti-Atxn1 (11750VII) , mouse monoclonal anti-GAPDH (2-RGM2; Advanced Immunochemical), mouse monoclonal Ronin (Becton Dickinson), rabbit polyclonal Hcf1 (A301-400A, Bethyl Laboratories).

    Techniques: Transgenic Assay, Expressing, Western Blot, Size-exclusion Chromatography, Luciferase, Mutagenesis, Binding Assay, In Vivo