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anti hsp heat shock protein antibody  (StressMarq)


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    Structured Review

    StressMarq anti hsp heat shock protein antibody
    Application of <t>anti-HSP</t> antibody (conjugated <t>with</t> <t>FITC)</t> with the sandwich method without delivery reagent. Arrows indicate a layer of FITC signals on top of the nuclear and mitochondrial signals. Optical cross sections are shown at the right and bottom of ( A , C ). Scale bars: 50 μm. ( A ) Merge of FITC and Hoechst 33342 without blocking. ( B ) Three-dimensional reconstruction of optical sections (apical side up) showing a merge of FITC and Hoechst 33342 without blocking. ( C ) Merge of FITC, MitoRed, and Hoechst 33342 with blocking. ( D ) Three-dimensional reconstruction of optical sections (apical side up) showing a merge of FITC, MitoRed, and Hoechst 33342 with blocking.
    Anti Hsp Heat Shock Protein Antibody, supplied by StressMarq, used in various techniques. Bioz Stars score: 91/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti hsp heat shock protein antibody/product/StressMarq
    Average 91 stars, based on 7 article reviews
    anti hsp heat shock protein antibody - by Bioz Stars, 2026-02
    91/100 stars

    Images

    1) Product Images from "Protein Delivery to Insect Epithelial Cells In Vivo: Potential Application to Functional Molecular Analysis of Proteins in Butterfly Wing Development"

    Article Title: Protein Delivery to Insect Epithelial Cells In Vivo: Potential Application to Functional Molecular Analysis of Proteins in Butterfly Wing Development

    Journal: BioTech

    doi: 10.3390/biotech12020028

    Application of anti-HSP antibody (conjugated with FITC) with the sandwich method without delivery reagent. Arrows indicate a layer of FITC signals on top of the nuclear and mitochondrial signals. Optical cross sections are shown at the right and bottom of ( A , C ). Scale bars: 50 μm. ( A ) Merge of FITC and Hoechst 33342 without blocking. ( B ) Three-dimensional reconstruction of optical sections (apical side up) showing a merge of FITC and Hoechst 33342 without blocking. ( C ) Merge of FITC, MitoRed, and Hoechst 33342 with blocking. ( D ) Three-dimensional reconstruction of optical sections (apical side up) showing a merge of FITC, MitoRed, and Hoechst 33342 with blocking.
    Figure Legend Snippet: Application of anti-HSP antibody (conjugated with FITC) with the sandwich method without delivery reagent. Arrows indicate a layer of FITC signals on top of the nuclear and mitochondrial signals. Optical cross sections are shown at the right and bottom of ( A , C ). Scale bars: 50 μm. ( A ) Merge of FITC and Hoechst 33342 without blocking. ( B ) Three-dimensional reconstruction of optical sections (apical side up) showing a merge of FITC and Hoechst 33342 without blocking. ( C ) Merge of FITC, MitoRed, and Hoechst 33342 with blocking. ( D ) Three-dimensional reconstruction of optical sections (apical side up) showing a merge of FITC, MitoRed, and Hoechst 33342 with blocking.

    Techniques Used: Blocking Assay

    Application of anti-HSP antibody (conjugated with FITC) using the sandwich method with L17E. Optical cross sections are shown at the right and bottom of ( A , C ). Scale bars: 50 μm. ( A ) Merge of FITC and Hoechst 33342 without blocking. ( B ) Three-dimensional reconstruction of optical sections (apical side up) showing a merge of FITC and Hoechst 33342 without blocking. The FITC-positive layer is indicated by arrows. ( C ) Merge of FITC, MitoRed, and Hoechst 33342 with blocking. ( D ) Three-dimensional reconstruction of optical sections (apical side up) showing a merge of FITC, MitoRed, and Hoechst 33342 with blocking. The FITC-positive layer is indicated by arrows.
    Figure Legend Snippet: Application of anti-HSP antibody (conjugated with FITC) using the sandwich method with L17E. Optical cross sections are shown at the right and bottom of ( A , C ). Scale bars: 50 μm. ( A ) Merge of FITC and Hoechst 33342 without blocking. ( B ) Three-dimensional reconstruction of optical sections (apical side up) showing a merge of FITC and Hoechst 33342 without blocking. The FITC-positive layer is indicated by arrows. ( C ) Merge of FITC, MitoRed, and Hoechst 33342 with blocking. ( D ) Three-dimensional reconstruction of optical sections (apical side up) showing a merge of FITC, MitoRed, and Hoechst 33342 with blocking. The FITC-positive layer is indicated by arrows.

    Techniques Used: Blocking Assay

    Application of antibodies using the sandwich method with ProteoCarry. ProteoCarry and antibody were used in an 8:1 ratio. Optical cross sections are shown at the right and bottom of the major plane panel. Scale bars: 10 μm. ( A – C ) A treated individual. Three panels ( A – C ) are images of the same visual field. ( A ) Anti-tubulin antibody conjugated with DyLight 550. Arrows indicate diffuse DyLight 550 signals. ( B ) BODIPY FL C 5 -ceramide. ( C ) Merge of DyLight 550, BODIPY FL C 5 -ceramide, and Hoechst 33342. ( D – F ) Another treated individual. Three panels ( D – F ) are images of the same visual field. ( D ) Anti- Drosophila axons antibodies conjugated with Alexa Fluor 488. Arrows indicate diffuse Alexa Fluor 488 signals. ( E ) LysoTracker Red. ( F ) Merge of Alexa Fluor 488, LysoTracker Red, and Hoechst 33342. Arrows indicate spreading cytosolic staining of Alexa Fluor 488. ( G – I ) Another treated individual. Three panels ( G – I ) are images of the same visual field. ( G ) Anti-HSP antibody conjugated with FITC. ( H ) LysoTracker Red. ( I ) Merge of FITC, LysoTracker Red, and Hoechst 33342. Arrows indicate diffuse FITC signals.
    Figure Legend Snippet: Application of antibodies using the sandwich method with ProteoCarry. ProteoCarry and antibody were used in an 8:1 ratio. Optical cross sections are shown at the right and bottom of the major plane panel. Scale bars: 10 μm. ( A – C ) A treated individual. Three panels ( A – C ) are images of the same visual field. ( A ) Anti-tubulin antibody conjugated with DyLight 550. Arrows indicate diffuse DyLight 550 signals. ( B ) BODIPY FL C 5 -ceramide. ( C ) Merge of DyLight 550, BODIPY FL C 5 -ceramide, and Hoechst 33342. ( D – F ) Another treated individual. Three panels ( D – F ) are images of the same visual field. ( D ) Anti- Drosophila axons antibodies conjugated with Alexa Fluor 488. Arrows indicate diffuse Alexa Fluor 488 signals. ( E ) LysoTracker Red. ( F ) Merge of Alexa Fluor 488, LysoTracker Red, and Hoechst 33342. Arrows indicate spreading cytosolic staining of Alexa Fluor 488. ( G – I ) Another treated individual. Three panels ( G – I ) are images of the same visual field. ( G ) Anti-HSP antibody conjugated with FITC. ( H ) LysoTracker Red. ( I ) Merge of FITC, LysoTracker Red, and Hoechst 33342. Arrows indicate diffuse FITC signals.

    Techniques Used: Staining



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    Application of <t>anti-HSP</t> antibody (conjugated <t>with</t> <t>FITC)</t> with the sandwich method without delivery reagent. Arrows indicate a layer of FITC signals on top of the nuclear and mitochondrial signals. Optical cross sections are shown at the right and bottom of ( A , C ). Scale bars: 50 μm. ( A ) Merge of FITC and Hoechst 33342 without blocking. ( B ) Three-dimensional reconstruction of optical sections (apical side up) showing a merge of FITC and Hoechst 33342 without blocking. ( C ) Merge of FITC, MitoRed, and Hoechst 33342 with blocking. ( D ) Three-dimensional reconstruction of optical sections (apical side up) showing a merge of FITC, MitoRed, and Hoechst 33342 with blocking.
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    <t>MAPKAPK3</t> was significantly co-expressed with TSPO . (a) Co-expression genes of TSPO in glioma (including LGG and GBM) according to data from TCGA database were identified. (b-c) Biological function and KEGG analysis of TSPO co-expression genes were performed. (d-e) Correlation between TSPO and MAPKAPK3 expression was identified from LGG and GBM tissue samples, respectively, in TCGA database. (f) Correlation between TSPO and MAPKAPK3 expression was identified from glioma tissues in our cohort. (g–h) The expression of MAPKAPK3 in patients with glioma and its relationship with survival rates are shown according to TCGA database.
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    <t>MAPKAPK3</t> was significantly co-expressed with TSPO . (a) Co-expression genes of TSPO in glioma (including LGG and GBM) according to data from TCGA database were identified. (b-c) Biological function and KEGG analysis of TSPO co-expression genes were performed. (d-e) Correlation between TSPO and MAPKAPK3 expression was identified from LGG and GBM tissue samples, respectively, in TCGA database. (f) Correlation between TSPO and MAPKAPK3 expression was identified from glioma tissues in our cohort. (g–h) The expression of MAPKAPK3 in patients with glioma and its relationship with survival rates are shown according to TCGA database.
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    Image Search Results


    Application of anti-HSP antibody (conjugated with FITC) with the sandwich method without delivery reagent. Arrows indicate a layer of FITC signals on top of the nuclear and mitochondrial signals. Optical cross sections are shown at the right and bottom of ( A , C ). Scale bars: 50 μm. ( A ) Merge of FITC and Hoechst 33342 without blocking. ( B ) Three-dimensional reconstruction of optical sections (apical side up) showing a merge of FITC and Hoechst 33342 without blocking. ( C ) Merge of FITC, MitoRed, and Hoechst 33342 with blocking. ( D ) Three-dimensional reconstruction of optical sections (apical side up) showing a merge of FITC, MitoRed, and Hoechst 33342 with blocking.

    Journal: BioTech

    Article Title: Protein Delivery to Insect Epithelial Cells In Vivo: Potential Application to Functional Molecular Analysis of Proteins in Butterfly Wing Development

    doi: 10.3390/biotech12020028

    Figure Lengend Snippet: Application of anti-HSP antibody (conjugated with FITC) with the sandwich method without delivery reagent. Arrows indicate a layer of FITC signals on top of the nuclear and mitochondrial signals. Optical cross sections are shown at the right and bottom of ( A , C ). Scale bars: 50 μm. ( A ) Merge of FITC and Hoechst 33342 without blocking. ( B ) Three-dimensional reconstruction of optical sections (apical side up) showing a merge of FITC and Hoechst 33342 without blocking. ( C ) Merge of FITC, MitoRed, and Hoechst 33342 with blocking. ( D ) Three-dimensional reconstruction of optical sections (apical side up) showing a merge of FITC, MitoRed, and Hoechst 33342 with blocking.

    Article Snippet: Anti-HSP (heat shock protein) antibody labeled with FITC (fluorescein isothiocyanate) (mouse monoclonal) against human HSP70 expressed in E. coli (product code: SMC-162D-FITC) was purchased from StressMarq Biosciences (Cadboro Bay Village, BC, Canada).

    Techniques: Blocking Assay

    Application of anti-HSP antibody (conjugated with FITC) using the sandwich method with L17E. Optical cross sections are shown at the right and bottom of ( A , C ). Scale bars: 50 μm. ( A ) Merge of FITC and Hoechst 33342 without blocking. ( B ) Three-dimensional reconstruction of optical sections (apical side up) showing a merge of FITC and Hoechst 33342 without blocking. The FITC-positive layer is indicated by arrows. ( C ) Merge of FITC, MitoRed, and Hoechst 33342 with blocking. ( D ) Three-dimensional reconstruction of optical sections (apical side up) showing a merge of FITC, MitoRed, and Hoechst 33342 with blocking. The FITC-positive layer is indicated by arrows.

    Journal: BioTech

    Article Title: Protein Delivery to Insect Epithelial Cells In Vivo: Potential Application to Functional Molecular Analysis of Proteins in Butterfly Wing Development

    doi: 10.3390/biotech12020028

    Figure Lengend Snippet: Application of anti-HSP antibody (conjugated with FITC) using the sandwich method with L17E. Optical cross sections are shown at the right and bottom of ( A , C ). Scale bars: 50 μm. ( A ) Merge of FITC and Hoechst 33342 without blocking. ( B ) Three-dimensional reconstruction of optical sections (apical side up) showing a merge of FITC and Hoechst 33342 without blocking. The FITC-positive layer is indicated by arrows. ( C ) Merge of FITC, MitoRed, and Hoechst 33342 with blocking. ( D ) Three-dimensional reconstruction of optical sections (apical side up) showing a merge of FITC, MitoRed, and Hoechst 33342 with blocking. The FITC-positive layer is indicated by arrows.

    Article Snippet: Anti-HSP (heat shock protein) antibody labeled with FITC (fluorescein isothiocyanate) (mouse monoclonal) against human HSP70 expressed in E. coli (product code: SMC-162D-FITC) was purchased from StressMarq Biosciences (Cadboro Bay Village, BC, Canada).

    Techniques: Blocking Assay

    Application of antibodies using the sandwich method with ProteoCarry. ProteoCarry and antibody were used in an 8:1 ratio. Optical cross sections are shown at the right and bottom of the major plane panel. Scale bars: 10 μm. ( A – C ) A treated individual. Three panels ( A – C ) are images of the same visual field. ( A ) Anti-tubulin antibody conjugated with DyLight 550. Arrows indicate diffuse DyLight 550 signals. ( B ) BODIPY FL C 5 -ceramide. ( C ) Merge of DyLight 550, BODIPY FL C 5 -ceramide, and Hoechst 33342. ( D – F ) Another treated individual. Three panels ( D – F ) are images of the same visual field. ( D ) Anti- Drosophila axons antibodies conjugated with Alexa Fluor 488. Arrows indicate diffuse Alexa Fluor 488 signals. ( E ) LysoTracker Red. ( F ) Merge of Alexa Fluor 488, LysoTracker Red, and Hoechst 33342. Arrows indicate spreading cytosolic staining of Alexa Fluor 488. ( G – I ) Another treated individual. Three panels ( G – I ) are images of the same visual field. ( G ) Anti-HSP antibody conjugated with FITC. ( H ) LysoTracker Red. ( I ) Merge of FITC, LysoTracker Red, and Hoechst 33342. Arrows indicate diffuse FITC signals.

    Journal: BioTech

    Article Title: Protein Delivery to Insect Epithelial Cells In Vivo: Potential Application to Functional Molecular Analysis of Proteins in Butterfly Wing Development

    doi: 10.3390/biotech12020028

    Figure Lengend Snippet: Application of antibodies using the sandwich method with ProteoCarry. ProteoCarry and antibody were used in an 8:1 ratio. Optical cross sections are shown at the right and bottom of the major plane panel. Scale bars: 10 μm. ( A – C ) A treated individual. Three panels ( A – C ) are images of the same visual field. ( A ) Anti-tubulin antibody conjugated with DyLight 550. Arrows indicate diffuse DyLight 550 signals. ( B ) BODIPY FL C 5 -ceramide. ( C ) Merge of DyLight 550, BODIPY FL C 5 -ceramide, and Hoechst 33342. ( D – F ) Another treated individual. Three panels ( D – F ) are images of the same visual field. ( D ) Anti- Drosophila axons antibodies conjugated with Alexa Fluor 488. Arrows indicate diffuse Alexa Fluor 488 signals. ( E ) LysoTracker Red. ( F ) Merge of Alexa Fluor 488, LysoTracker Red, and Hoechst 33342. Arrows indicate spreading cytosolic staining of Alexa Fluor 488. ( G – I ) Another treated individual. Three panels ( G – I ) are images of the same visual field. ( G ) Anti-HSP antibody conjugated with FITC. ( H ) LysoTracker Red. ( I ) Merge of FITC, LysoTracker Red, and Hoechst 33342. Arrows indicate diffuse FITC signals.

    Article Snippet: Anti-HSP (heat shock protein) antibody labeled with FITC (fluorescein isothiocyanate) (mouse monoclonal) against human HSP70 expressed in E. coli (product code: SMC-162D-FITC) was purchased from StressMarq Biosciences (Cadboro Bay Village, BC, Canada).

    Techniques: Staining

    MAPKAPK3 was significantly co-expressed with TSPO . (a) Co-expression genes of TSPO in glioma (including LGG and GBM) according to data from TCGA database were identified. (b-c) Biological function and KEGG analysis of TSPO co-expression genes were performed. (d-e) Correlation between TSPO and MAPKAPK3 expression was identified from LGG and GBM tissue samples, respectively, in TCGA database. (f) Correlation between TSPO and MAPKAPK3 expression was identified from glioma tissues in our cohort. (g–h) The expression of MAPKAPK3 in patients with glioma and its relationship with survival rates are shown according to TCGA database.

    Journal: Bioengineered

    Article Title: Inhibition of translocator protein 18 kDa suppressed the progression of glioma via the ELAV-like RNA-binding protein 1/MAPK-activated protein kinase 3 axis

    doi: 10.1080/21655979.2022.2048992

    Figure Lengend Snippet: MAPKAPK3 was significantly co-expressed with TSPO . (a) Co-expression genes of TSPO in glioma (including LGG and GBM) according to data from TCGA database were identified. (b-c) Biological function and KEGG analysis of TSPO co-expression genes were performed. (d-e) Correlation between TSPO and MAPKAPK3 expression was identified from LGG and GBM tissue samples, respectively, in TCGA database. (f) Correlation between TSPO and MAPKAPK3 expression was identified from glioma tissues in our cohort. (g–h) The expression of MAPKAPK3 in patients with glioma and its relationship with survival rates are shown according to TCGA database.

    Article Snippet: After blocking the membranes with skimmed milk powder (Beyotime Biotechnology), they were incubated with primary antibodies, containing TSPO (1:1000, cat no. ab109497; Abcam), E-cadherin (1:1000, cat no. 20,874-1-AP; Proteintech Group, Wuhan, China), N-cadherin (1:1000, cat no. 22,018-1-AP; Proteintech Group), vimentin (1:1000, cat no. 10,366-1-AP; Proteintech Group), β-catenin (1:1000, cat no. 51,067-2-AP; Proteintech Group), Slug (1:1000, cat no. 12,129-1-AP; Proteintech Group), MAPKAPK3 (1:1000, cat no. 15,424-1-AP; Proteintech Group), p-MAPKAPK3 (1:250, cat no. SPC-1016; StressMarq Biosciences Inc., USA), CREB (1:1000, cat no. 12,208-1-AP; Proteintech Group), p-CREB (1:1000, cat no. #9198; Cell Signaling Technology, USA), HUR (1:1000, cat no. 11,910-1-AP; Proteintech Group), H3 (1:1000, cat no. 17,168-1-AP; Proteintech Group), and α-tubulin (1:2000, cat no. 11,224-1-AP; Proteintech Group), for 12 h at 4°C.

    Techniques: Expressing

    Inhibition of TSPO decreased the expression of MAPKAPK3 and increased its mRNA degradation . (a) qRT-PCR was used to detected the MAPKAPK3 mRNA levels in U87 and U251 cells with TSPO inhibition. (b) Co-immunostaining in U251 cells indicated that cells with TSPO knockdown had a lower MAPKAPK3 signal. (c-d) Western blotting showing the protein level of MAPKAPK3, p-MAPKAPK3, and p-CREB was decreased under TSPO inhibition. (e) Amanitin (0.1 µM) was used to inhibit mRNA synthesis at 0, 2, 4, 6, and 8 h, and qRT-PCR results indicated that inhibition of TSPO expression increased the degradation rate of the MAPKAPK3 mRNA. * P < 0.05; ** P < 0.01.

    Journal: Bioengineered

    Article Title: Inhibition of translocator protein 18 kDa suppressed the progression of glioma via the ELAV-like RNA-binding protein 1/MAPK-activated protein kinase 3 axis

    doi: 10.1080/21655979.2022.2048992

    Figure Lengend Snippet: Inhibition of TSPO decreased the expression of MAPKAPK3 and increased its mRNA degradation . (a) qRT-PCR was used to detected the MAPKAPK3 mRNA levels in U87 and U251 cells with TSPO inhibition. (b) Co-immunostaining in U251 cells indicated that cells with TSPO knockdown had a lower MAPKAPK3 signal. (c-d) Western blotting showing the protein level of MAPKAPK3, p-MAPKAPK3, and p-CREB was decreased under TSPO inhibition. (e) Amanitin (0.1 µM) was used to inhibit mRNA synthesis at 0, 2, 4, 6, and 8 h, and qRT-PCR results indicated that inhibition of TSPO expression increased the degradation rate of the MAPKAPK3 mRNA. * P < 0.05; ** P < 0.01.

    Article Snippet: After blocking the membranes with skimmed milk powder (Beyotime Biotechnology), they were incubated with primary antibodies, containing TSPO (1:1000, cat no. ab109497; Abcam), E-cadherin (1:1000, cat no. 20,874-1-AP; Proteintech Group, Wuhan, China), N-cadherin (1:1000, cat no. 22,018-1-AP; Proteintech Group), vimentin (1:1000, cat no. 10,366-1-AP; Proteintech Group), β-catenin (1:1000, cat no. 51,067-2-AP; Proteintech Group), Slug (1:1000, cat no. 12,129-1-AP; Proteintech Group), MAPKAPK3 (1:1000, cat no. 15,424-1-AP; Proteintech Group), p-MAPKAPK3 (1:250, cat no. SPC-1016; StressMarq Biosciences Inc., USA), CREB (1:1000, cat no. 12,208-1-AP; Proteintech Group), p-CREB (1:1000, cat no. #9198; Cell Signaling Technology, USA), HUR (1:1000, cat no. 11,910-1-AP; Proteintech Group), H3 (1:1000, cat no. 17,168-1-AP; Proteintech Group), and α-tubulin (1:2000, cat no. 11,224-1-AP; Proteintech Group), for 12 h at 4°C.

    Techniques: Inhibition, Expressing, Quantitative RT-PCR, Immunostaining, Western Blot

    HUR regulated MAPKAPK3 expression and cell proliferation and mobility . U251 and U87 cells were treated with the NC siRNA + vector, HUR siRNA + vector, and HUR siRNA + MAPKAPK3 overexpression plasmid (MAPKAPK3-OE). (a–b) Western blotting was used to detect the protein expression of HUR, MAPKAPK3, p-MAPKAPK3, and p-CREB in each group. (c) The CCK-8 assay was used to detect the cell viability in each group in 48 h. (d-e) Transwell assays were used to detect the invasive cell numbers in each field in each group. (f–g) Western blotting was used to detect the expression of MAPKAPK3 in TSPO knockdown cells with HUR overexpression. (h) Amanitin (0.1 µM) was used to inhibit the mRNA synthesis for 0, 2, 4, 6, and 8 h, and qRT-PCR results indicated that overexpression of HUR increased the mRNA stability of MAPKAPK3 in U87 and U251 cells with TSPO inhibition. * P < 0.05; ** P < 0.01.

    Journal: Bioengineered

    Article Title: Inhibition of translocator protein 18 kDa suppressed the progression of glioma via the ELAV-like RNA-binding protein 1/MAPK-activated protein kinase 3 axis

    doi: 10.1080/21655979.2022.2048992

    Figure Lengend Snippet: HUR regulated MAPKAPK3 expression and cell proliferation and mobility . U251 and U87 cells were treated with the NC siRNA + vector, HUR siRNA + vector, and HUR siRNA + MAPKAPK3 overexpression plasmid (MAPKAPK3-OE). (a–b) Western blotting was used to detect the protein expression of HUR, MAPKAPK3, p-MAPKAPK3, and p-CREB in each group. (c) The CCK-8 assay was used to detect the cell viability in each group in 48 h. (d-e) Transwell assays were used to detect the invasive cell numbers in each field in each group. (f–g) Western blotting was used to detect the expression of MAPKAPK3 in TSPO knockdown cells with HUR overexpression. (h) Amanitin (0.1 µM) was used to inhibit the mRNA synthesis for 0, 2, 4, 6, and 8 h, and qRT-PCR results indicated that overexpression of HUR increased the mRNA stability of MAPKAPK3 in U87 and U251 cells with TSPO inhibition. * P < 0.05; ** P < 0.01.

    Article Snippet: After blocking the membranes with skimmed milk powder (Beyotime Biotechnology), they were incubated with primary antibodies, containing TSPO (1:1000, cat no. ab109497; Abcam), E-cadherin (1:1000, cat no. 20,874-1-AP; Proteintech Group, Wuhan, China), N-cadherin (1:1000, cat no. 22,018-1-AP; Proteintech Group), vimentin (1:1000, cat no. 10,366-1-AP; Proteintech Group), β-catenin (1:1000, cat no. 51,067-2-AP; Proteintech Group), Slug (1:1000, cat no. 12,129-1-AP; Proteintech Group), MAPKAPK3 (1:1000, cat no. 15,424-1-AP; Proteintech Group), p-MAPKAPK3 (1:250, cat no. SPC-1016; StressMarq Biosciences Inc., USA), CREB (1:1000, cat no. 12,208-1-AP; Proteintech Group), p-CREB (1:1000, cat no. #9198; Cell Signaling Technology, USA), HUR (1:1000, cat no. 11,910-1-AP; Proteintech Group), H3 (1:1000, cat no. 17,168-1-AP; Proteintech Group), and α-tubulin (1:2000, cat no. 11,224-1-AP; Proteintech Group), for 12 h at 4°C.

    Techniques: Expressing, Plasmid Preparation, Over Expression, Western Blot, CCK-8 Assay, Quantitative RT-PCR, Inhibition

    Overexpression of HUR or MAPKAPK3 reversed the inhibitory effects of TSPO inhibition of glioma cells . U251 and U87 cells were treated with NC siRNA, TSPO siRNA, TSPO siRNA + HUR-OE, and TSPO siRNA + MAPKAPK3-OE. (a) The CCK-8 assay was used to detect the proliferative rate of U87 and U251 cells in each group treated with the aforementioned conditions in 24 and 48 h. (b) EDU assays were used to detect the EDU-positive rate in each group. (c) Transwell assay was performed to detect the number of invasive cells in each field in each group. * P < 0.05; ** P < 0.01.

    Journal: Bioengineered

    Article Title: Inhibition of translocator protein 18 kDa suppressed the progression of glioma via the ELAV-like RNA-binding protein 1/MAPK-activated protein kinase 3 axis

    doi: 10.1080/21655979.2022.2048992

    Figure Lengend Snippet: Overexpression of HUR or MAPKAPK3 reversed the inhibitory effects of TSPO inhibition of glioma cells . U251 and U87 cells were treated with NC siRNA, TSPO siRNA, TSPO siRNA + HUR-OE, and TSPO siRNA + MAPKAPK3-OE. (a) The CCK-8 assay was used to detect the proliferative rate of U87 and U251 cells in each group treated with the aforementioned conditions in 24 and 48 h. (b) EDU assays were used to detect the EDU-positive rate in each group. (c) Transwell assay was performed to detect the number of invasive cells in each field in each group. * P < 0.05; ** P < 0.01.

    Article Snippet: After blocking the membranes with skimmed milk powder (Beyotime Biotechnology), they were incubated with primary antibodies, containing TSPO (1:1000, cat no. ab109497; Abcam), E-cadherin (1:1000, cat no. 20,874-1-AP; Proteintech Group, Wuhan, China), N-cadherin (1:1000, cat no. 22,018-1-AP; Proteintech Group), vimentin (1:1000, cat no. 10,366-1-AP; Proteintech Group), β-catenin (1:1000, cat no. 51,067-2-AP; Proteintech Group), Slug (1:1000, cat no. 12,129-1-AP; Proteintech Group), MAPKAPK3 (1:1000, cat no. 15,424-1-AP; Proteintech Group), p-MAPKAPK3 (1:250, cat no. SPC-1016; StressMarq Biosciences Inc., USA), CREB (1:1000, cat no. 12,208-1-AP; Proteintech Group), p-CREB (1:1000, cat no. #9198; Cell Signaling Technology, USA), HUR (1:1000, cat no. 11,910-1-AP; Proteintech Group), H3 (1:1000, cat no. 17,168-1-AP; Proteintech Group), and α-tubulin (1:2000, cat no. 11,224-1-AP; Proteintech Group), for 12 h at 4°C.

    Techniques: Over Expression, Inhibition, CCK-8 Assay, Transwell Assay