Structured Review

Cell Signaling Technology Inc rabbit anti actin
Rabbit Anti Actin, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/rabbit anti actin/product/Cell Signaling Technology Inc
Average 99 stars, based on 13 article reviews
Price from $9.99 to $1999.99
rabbit anti actin - by Bioz Stars, 2020-09
99/100 stars

Images

Related Articles

Produced:

Article Title: The ubiquitin ligase Cullin-1 associates with chromatin and regulates transcription of specific c-MYC target genes
Article Snippet: .. Western blot analysis against 3xFLAG was carried out using monoclonal anti-FLAG M2 antibody produced in mouse (Sigma-Aldrich, #F1804-1MG) with β-actin rabbit monoclonal antibody (Cell Signaling Technology, clone D6A8) as a loading control. .. Western blot against CUL1 was performed with recombinant anti-Cullin1/CUL-1 antibody (Abcam, ab75817).

Western Blot:

Article Title: The ubiquitin ligase Cullin-1 associates with chromatin and regulates transcription of specific c-MYC target genes
Article Snippet: .. Western blot analysis against 3xFLAG was carried out using monoclonal anti-FLAG M2 antibody produced in mouse (Sigma-Aldrich, #F1804-1MG) with β-actin rabbit monoclonal antibody (Cell Signaling Technology, clone D6A8) as a loading control. .. Western blot against CUL1 was performed with recombinant anti-Cullin1/CUL-1 antibody (Abcam, ab75817).

Article Title: Dissecting cell-type-specific metabolism in pancreatic ductal adenocarcinoma
Article Snippet: .. Western blots were performed using primary antibodies against PC (Santa Cruz sc-271493, 1:100 dilution), ME1 (Proteintech 16619–1-AP, 1:250 dilution), or β -actin (Cell Signaling Technologies 8457, 1:10,000 dilution). .. Quantification and statistical analysisGraphPad Prism software was used for statistical analysis.

Incubation:

Article Title: Endocrine sensitivity of estrogen receptor‐positive breast cancer is negatively correlated with aspartate‐β‐hydroxylase expression
Article Snippet: .. Membranes were incubated at 4°C overnight with primary monoclonal antibodies including mouse anti‐ASPH (FB‐50), rabbit anti‐β actin (D6A8; Cell Signaling Technology), rabbit anti‐ERK1/2 (137F5; Cell Signaling Technology), rabbit anti‐P‐ERK1/2 (Thr202/Tyr204; D13.14.4E; Cell Signaling Technology), rabbit anti‐Akt (C67E7; Cell Signaling Technology), and rabbit anti‐P‐Akt (Ser473; D9E; Cell Signaling Technology). .. Membranes were incubated with HRP‐conjugated anti‐mouse IgG antibody (Jackson ImmunoResearch, West Grove, PA, USA) or anti‐rabbit IgG antibody (Cell Signaling Technology), followed by chemiluminescence detection.

other:

Article Title: EZH2 inhibits autophagic cell death of aortic vascular smooth muscle cells to affect aortic dissection
Article Snippet: Antibodies The antibodies used in this study including EZH2 (#5246), H3K27me2 (#9728), H3K27me3 (#9733), p-MEK1/2 (#9154), ERK1/2 (#4695), p-ERK1/2 (#4370), P38 (#8690), p-P38 (#4511), mTOR (#2983), p-mTOR (#5536), S6 (#2317), p-S6 (#5364), p-AMPKα (#2535), AMPKα (#5831), LC3II/I (#12741), FLAG (#2368), ATG5 (#12994), ATG7 (#8558), GAPDH (#5174), and β-actin (#8457) were obtained from Cell Signaling Technology.

Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 90
    Cell Signaling Technology Inc rabbit anti human β actin antibody
    Ornithine transcarbamylase (OTC) is expressed in both hMSCs and T-ALL cells and BCT-10 treatment could suppress OTC expression significant in T-ALL cells but only modestly on MSCs. ( a ) Basal expression of OTC in hTertMSCs, hMSCs from 2 healthy donors, CCRF-CEM, Jurkat and MOLT-4. Cells were harvested and respective proteins were extracted from the corresponding cell lines. SDS-PAGE was performed to separate the proteins. OTC and <t>β-actin</t> (internal control) expression were probed by the corresponding antibodies and then visualized by enzyme coupled luminescence (ECL). ( b ) Expression of OTC in hMSCs after BCT-100 treatment. hTertMSCs or hMSCs from a healthy donor were cultured in different doses of BCT-100 (0 U/ml, 0.5 U/ml, 1 U/ml and 2 U/ml) for 36 hours and protein was extracted from the cell culture. SDS-PAGE followed by Western blotting was performed. The expression of OTC and β-actin (internal control) of hTertMSCs is presented in the figure. ( c ), ( d ) and ( e ) Expression of OTC in CCRF-CEM, Jurkat or MOLT-4 after BCT-100 treatment respectively. CCRF-CEM, Jurkat and MOLT-4 were cultured in different doses of BCT-100 (0 U/ml, 0.5 U/ml, 1 U/ml and 2 U/ml) for 36 hours and protein was extracted. SDS-PAGE followed by Western blotting was performed. The expression of OTC and β-actin (internal control) of CCRF-CEM, Jurkat or MOLT-4 is presented in the figures. The most representative results are presented.
    Rabbit Anti Human β Actin Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 90/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit anti human β actin antibody/product/Cell Signaling Technology Inc
    Average 90 stars, based on 4 article reviews
    Price from $9.99 to $1999.99
    rabbit anti human β actin antibody - by Bioz Stars, 2020-09
    90/100 stars
      Buy from Supplier

    93
    Cell Signaling Technology Inc rabbit anti β actin
    Immunofluorescence detection of iNOS in activated J774-A1 macrophages infected with T. gondii . (A) Detection of iNOS (green) in non-infected (Control) and in T. gondii (red) infected cells (DAPI - blue) at 2, 6, and 24 h post-infection. Scale bar = 10 μm. (B) Analysis of the proportion of iNOS positive or negative macrophages in non-infected (Control) and T. gondii infected cells at 2 and 24 h post-infection. Mean ± SEM ( n = 4 experiments, each with 8 replicates). (C) Western blot detection of iNOS expression in non-infected (Control) and T. gondii infected (Infected) cells. <t>β-actin</t> was used as loading control. (D) Densitometry of western blots normalized to β-actin at 2 h post-infection. Mean ± SD ( n = 3 experiments, each with 1 replicate). ∗ P ≤ 0.05, two-way ANOVA with Tukey post-test, n.s (not significant).
    Rabbit Anti β Actin, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit anti β actin/product/Cell Signaling Technology Inc
    Average 93 stars, based on 14 article reviews
    Price from $9.99 to $1999.99
    rabbit anti β actin - by Bioz Stars, 2020-09
    93/100 stars
      Buy from Supplier

    Image Search Results


    Ornithine transcarbamylase (OTC) is expressed in both hMSCs and T-ALL cells and BCT-10 treatment could suppress OTC expression significant in T-ALL cells but only modestly on MSCs. ( a ) Basal expression of OTC in hTertMSCs, hMSCs from 2 healthy donors, CCRF-CEM, Jurkat and MOLT-4. Cells were harvested and respective proteins were extracted from the corresponding cell lines. SDS-PAGE was performed to separate the proteins. OTC and β-actin (internal control) expression were probed by the corresponding antibodies and then visualized by enzyme coupled luminescence (ECL). ( b ) Expression of OTC in hMSCs after BCT-100 treatment. hTertMSCs or hMSCs from a healthy donor were cultured in different doses of BCT-100 (0 U/ml, 0.5 U/ml, 1 U/ml and 2 U/ml) for 36 hours and protein was extracted from the cell culture. SDS-PAGE followed by Western blotting was performed. The expression of OTC and β-actin (internal control) of hTertMSCs is presented in the figure. ( c ), ( d ) and ( e ) Expression of OTC in CCRF-CEM, Jurkat or MOLT-4 after BCT-100 treatment respectively. CCRF-CEM, Jurkat and MOLT-4 were cultured in different doses of BCT-100 (0 U/ml, 0.5 U/ml, 1 U/ml and 2 U/ml) for 36 hours and protein was extracted. SDS-PAGE followed by Western blotting was performed. The expression of OTC and β-actin (internal control) of CCRF-CEM, Jurkat or MOLT-4 is presented in the figures. The most representative results are presented.

    Journal: Experimental Hematology & Oncology

    Article Title: Vincristine could partly suppress stromal support to T-ALL blasts during pegylated arginase I treatment

    doi: 10.1186/2162-3619-2-11

    Figure Lengend Snippet: Ornithine transcarbamylase (OTC) is expressed in both hMSCs and T-ALL cells and BCT-10 treatment could suppress OTC expression significant in T-ALL cells but only modestly on MSCs. ( a ) Basal expression of OTC in hTertMSCs, hMSCs from 2 healthy donors, CCRF-CEM, Jurkat and MOLT-4. Cells were harvested and respective proteins were extracted from the corresponding cell lines. SDS-PAGE was performed to separate the proteins. OTC and β-actin (internal control) expression were probed by the corresponding antibodies and then visualized by enzyme coupled luminescence (ECL). ( b ) Expression of OTC in hMSCs after BCT-100 treatment. hTertMSCs or hMSCs from a healthy donor were cultured in different doses of BCT-100 (0 U/ml, 0.5 U/ml, 1 U/ml and 2 U/ml) for 36 hours and protein was extracted from the cell culture. SDS-PAGE followed by Western blotting was performed. The expression of OTC and β-actin (internal control) of hTertMSCs is presented in the figure. ( c ), ( d ) and ( e ) Expression of OTC in CCRF-CEM, Jurkat or MOLT-4 after BCT-100 treatment respectively. CCRF-CEM, Jurkat and MOLT-4 were cultured in different doses of BCT-100 (0 U/ml, 0.5 U/ml, 1 U/ml and 2 U/ml) for 36 hours and protein was extracted. SDS-PAGE followed by Western blotting was performed. The expression of OTC and β-actin (internal control) of CCRF-CEM, Jurkat or MOLT-4 is presented in the figures. The most representative results are presented.

    Article Snippet: Rabbit anti-human β-actin antibody was purchased from Cell Signaling Technology (Danvers, MA).

    Techniques: Expressing, SDS Page, Cell Culture, Western Blot

    Immunofluorescence detection of iNOS in activated J774-A1 macrophages infected with T. gondii . (A) Detection of iNOS (green) in non-infected (Control) and in T. gondii (red) infected cells (DAPI - blue) at 2, 6, and 24 h post-infection. Scale bar = 10 μm. (B) Analysis of the proportion of iNOS positive or negative macrophages in non-infected (Control) and T. gondii infected cells at 2 and 24 h post-infection. Mean ± SEM ( n = 4 experiments, each with 8 replicates). (C) Western blot detection of iNOS expression in non-infected (Control) and T. gondii infected (Infected) cells. β-actin was used as loading control. (D) Densitometry of western blots normalized to β-actin at 2 h post-infection. Mean ± SD ( n = 3 experiments, each with 1 replicate). ∗ P ≤ 0.05, two-way ANOVA with Tukey post-test, n.s (not significant).

    Journal: Frontiers in Microbiology

    Article Title: Inhibition of Nitric Oxide Production in Activated Macrophages Caused by Toxoplasma gondii Infection Occurs by Distinct Mechanisms in Different Mouse Macrophage Cell Lines

    doi: 10.3389/fmicb.2018.01936

    Figure Lengend Snippet: Immunofluorescence detection of iNOS in activated J774-A1 macrophages infected with T. gondii . (A) Detection of iNOS (green) in non-infected (Control) and in T. gondii (red) infected cells (DAPI - blue) at 2, 6, and 24 h post-infection. Scale bar = 10 μm. (B) Analysis of the proportion of iNOS positive or negative macrophages in non-infected (Control) and T. gondii infected cells at 2 and 24 h post-infection. Mean ± SEM ( n = 4 experiments, each with 8 replicates). (C) Western blot detection of iNOS expression in non-infected (Control) and T. gondii infected (Infected) cells. β-actin was used as loading control. (D) Densitometry of western blots normalized to β-actin at 2 h post-infection. Mean ± SD ( n = 3 experiments, each with 1 replicate). ∗ P ≤ 0.05, two-way ANOVA with Tukey post-test, n.s (not significant).

    Article Snippet: Samples were diluted 4:1 in 5× Laemmli buffer containing 10 mM of dithiothreitol (Sigma-Aldrich, United States), boiled for 5 min, resolved in 8% polyacrylamide gels (Bio-Rad Laboratories, Inc., United States) by SDS–PAGE, and transferred to nitrocellulose membranes Amersham Protran 0.45 NC (GE Healthcare Life Sciences, United States) for 1 h. Membranes were blocked overnight at 4°C with 5% fat-free milk in PBS 0.1% Tween 20 (Sigma-Aldrich, United States), probed for 1 h with anti-iNOS mouse monoclonal antibody (Santa Cruz Biotechnology, United States) dilute 1:1000 and rabbit anti-β-actin (Cell Signaling Technology, United States) diluted 1:1000 in 5% fat-free milk in PBS 0.1% Tween 20.

    Techniques: Immunofluorescence, Infection, Western Blot, Expressing

    Immunofluorescence detection of iNOS in activated RAW 264.7 macrophages infected with T. gondii . (A) Detection of iNOS (green) in non-infected (Control) and in T. gondii (red) infected cells (DAPI - blue) at 2, 6, and 24 h post-infection. Scale bar - 10 μm. (B) Analysis of the proportion of iNOS positive or negative macrophages in non-infected (Control) and T. gondii infected cells at 2 and 24 h post-infection. Mean ± SEM ( n = 4 experiments, each with 8 replicates). (C) Western blot detection of iNOS expression in non-infected (Control) and T. gondii - infected (Infected) cells at different time intervals post-infection. β-actin was used as loading control. (D) Densitometry of western bolts normalized to β-actin at 2 h post-infection. Mean ± SD ( n = 3 experiments, each with 1 replicate), n.s (not significant).

    Journal: Frontiers in Microbiology

    Article Title: Inhibition of Nitric Oxide Production in Activated Macrophages Caused by Toxoplasma gondii Infection Occurs by Distinct Mechanisms in Different Mouse Macrophage Cell Lines

    doi: 10.3389/fmicb.2018.01936

    Figure Lengend Snippet: Immunofluorescence detection of iNOS in activated RAW 264.7 macrophages infected with T. gondii . (A) Detection of iNOS (green) in non-infected (Control) and in T. gondii (red) infected cells (DAPI - blue) at 2, 6, and 24 h post-infection. Scale bar - 10 μm. (B) Analysis of the proportion of iNOS positive or negative macrophages in non-infected (Control) and T. gondii infected cells at 2 and 24 h post-infection. Mean ± SEM ( n = 4 experiments, each with 8 replicates). (C) Western blot detection of iNOS expression in non-infected (Control) and T. gondii - infected (Infected) cells at different time intervals post-infection. β-actin was used as loading control. (D) Densitometry of western bolts normalized to β-actin at 2 h post-infection. Mean ± SD ( n = 3 experiments, each with 1 replicate), n.s (not significant).

    Article Snippet: Samples were diluted 4:1 in 5× Laemmli buffer containing 10 mM of dithiothreitol (Sigma-Aldrich, United States), boiled for 5 min, resolved in 8% polyacrylamide gels (Bio-Rad Laboratories, Inc., United States) by SDS–PAGE, and transferred to nitrocellulose membranes Amersham Protran 0.45 NC (GE Healthcare Life Sciences, United States) for 1 h. Membranes were blocked overnight at 4°C with 5% fat-free milk in PBS 0.1% Tween 20 (Sigma-Aldrich, United States), probed for 1 h with anti-iNOS mouse monoclonal antibody (Santa Cruz Biotechnology, United States) dilute 1:1000 and rabbit anti-β-actin (Cell Signaling Technology, United States) diluted 1:1000 in 5% fat-free milk in PBS 0.1% Tween 20.

    Techniques: Immunofluorescence, Infection, Western Blot, Expressing

    NQDI 1 effectively inhibits phosphorylation of ASK1 and downstream MAPK cascades. A Bioinformatics analysis: protein-protein interaction network in STRING v.10. A screenshot from STRING shows a network associated with 4-1BB (Tnfrsf9). The upper right (red circle) shows cell signaling proteins in cells associated with 4-1BB. The lower left (blue circle) shows chemokines and chemokine receptors. Each node represents a protein and each line represents an interaction, color coded by evidence type. Gene and protein names are listed in the table. B Experimental protocol for the induction of silicosis and treatment scheme of 4-1BBIg. C Western blot analysis of lung from different treated mice (n=3-4) Figure shows the representative images of three independent experiments. D The levels of p-ASK1 were normalized to those of β-actin. Data are the mean of three independent experiments. Error bars indicate the mean ± S.D. # P

    Journal: Theranostics

    Article Title: Blocking the 4-1BB Pathway Ameliorates Crystalline Silica-induced Lung Inflammation and Fibrosis in Mice

    doi: 10.7150/thno.16180

    Figure Lengend Snippet: NQDI 1 effectively inhibits phosphorylation of ASK1 and downstream MAPK cascades. A Bioinformatics analysis: protein-protein interaction network in STRING v.10. A screenshot from STRING shows a network associated with 4-1BB (Tnfrsf9). The upper right (red circle) shows cell signaling proteins in cells associated with 4-1BB. The lower left (blue circle) shows chemokines and chemokine receptors. Each node represents a protein and each line represents an interaction, color coded by evidence type. Gene and protein names are listed in the table. B Experimental protocol for the induction of silicosis and treatment scheme of 4-1BBIg. C Western blot analysis of lung from different treated mice (n=3-4) Figure shows the representative images of three independent experiments. D The levels of p-ASK1 were normalized to those of β-actin. Data are the mean of three independent experiments. Error bars indicate the mean ± S.D. # P

    Article Snippet: Proteins were separated by application of a constant voltage of 100 V for 1.5 h and then transferred onto PVDF membranes at a constant voltage of 100 V for 1 h. After blocking nonspecific sites with TBS containing 0.1% Tween20 (TBST) and 5% defatted dried milk, membranes were washed and incubated with primary antibodies: rat anti-4-1BB (Abcam, 1:500), rat anti-4-1BBL (Santa, 1:200), rabbit anti-ASK1 (Abcam, 1:1000), rabbit anti-phospho-ASK1 (Cell Signaling Technology, 1:1000), rabbit anti-p38 (Cell Signaling Technology, 1:1000), rabbit anti-phospho-p38 (Cell Signaling Technology, 1:1000), rabbit anti-JNK (Cell Signaling Technology, 1:1000), rabbit anti-phospho-JNK (Cell Signaling Technology, 1:1000) and rabbit anti-β-Actin (Cell Signaling Technology, 1:1000) overnight at 4°C.

    Techniques: Western Blot, Mouse Assay

    TUG1 enhanced the activation of Wnt/β-catenin signaling pathway. (A and B) Representative images showing the nuclear localization of β-catenin in SW620 and LoVo cells transfected with TUG1 shRNA or scramble shRNA. The magnification level is indicated on the figure. (C and D) Western blot analysis of the β-catenin levels in the nuclear fraction from CRC cells transfected with TUG1 shRNA or scramble shRNA. β-actin was the internal reference. (E and F) TCF/LEF reporter assay for detecting the activation of Wnt/β-catenin signaling in SW620 and LoVo cells transfected with TUG1 or NC scramble shRNA. **P

    Journal: Oncology Letters

    Article Title: Long non-coding RNA TUG1 promotes the proliferation of colorectal cancer cells through regulating Wnt/β-catenin pathway

    doi: 10.3892/ol.2018.9259

    Figure Lengend Snippet: TUG1 enhanced the activation of Wnt/β-catenin signaling pathway. (A and B) Representative images showing the nuclear localization of β-catenin in SW620 and LoVo cells transfected with TUG1 shRNA or scramble shRNA. The magnification level is indicated on the figure. (C and D) Western blot analysis of the β-catenin levels in the nuclear fraction from CRC cells transfected with TUG1 shRNA or scramble shRNA. β-actin was the internal reference. (E and F) TCF/LEF reporter assay for detecting the activation of Wnt/β-catenin signaling in SW620 and LoVo cells transfected with TUG1 or NC scramble shRNA. **P

    Article Snippet: Membranes were blocked with 5% non-fat dry milk in TBS-0.05% Tween-20 (TBST) buffer for 2 h at room temperature and incubated with primary antibodies rabbit anti-β-catenin (cat no. #9562; Cell Signaling Technology, Inc.) and rabbit anti-β-actin (cat no. #4970; Cell Signaling Technology, Inc.), each diluted to 1:1,000] at 4°C overnight.

    Techniques: Activation Assay, Transfection, shRNA, Western Blot, Reporter Assay