c terminal modified csg peptide  (Millipore)


Bioz Verified Symbol Millipore is a verified supplier  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 99
    Name:
    Custom Peptides
    Description:
    PEPscreen Custom Peptide LIbraries Suitable for robotic production of peptide microarrays Screen mulitple proteotyptic peptides and rapidly characterize and select mass spec compatible peptides Get results quick with delivery of your peptide library in less than 7 business days Sequence Length 6 to 20 amino acids Amount 0 5 2 mg or 2 5 mg Modifications Comprehensive offering including phosphorylation biotin fluorescein stable isotopes etc Format Supplied dry in a 96 well tube rack Options Normalization and aliquoting stock and copy libraries Minimum library size of 24 peptidesRequest more informationUse our free design tool to design your libraryAQUA Peptides Accurately quantitate low abundance proteins Measure site specific phosphorylation states Validate gene silencing at the protein level Custom peptides are available either without stable isotope labeling or with stable isotope labeling Stable isotope labeled AQUA TM Peptide seqeunces contain one isotopically labeled amino acid Sequence Length 5 to 30 amino acids Amount 5 x 1 nmole Purity 95 by RP HPLC Modifications phosphorylation Ser Thr Tyr carboxymethylated Cys carbamidomethylated Cys hydroxyproline N terminal biotin please inquire regarding other modifications Quantification by amino acid analysis AAA Format Supplied dryRequest more information
    Catalog Number:
    peptide
    Price:
    None
    Buy from Supplier


    Structured Review

    Millipore c terminal modified csg peptide
    Custom Peptides
    PEPscreen Custom Peptide LIbraries Suitable for robotic production of peptide microarrays Screen mulitple proteotyptic peptides and rapidly characterize and select mass spec compatible peptides Get results quick with delivery of your peptide library in less than 7 business days Sequence Length 6 to 20 amino acids Amount 0 5 2 mg or 2 5 mg Modifications Comprehensive offering including phosphorylation biotin fluorescein stable isotopes etc Format Supplied dry in a 96 well tube rack Options Normalization and aliquoting stock and copy libraries Minimum library size of 24 peptidesRequest more informationUse our free design tool to design your libraryAQUA Peptides Accurately quantitate low abundance proteins Measure site specific phosphorylation states Validate gene silencing at the protein level Custom peptides are available either without stable isotope labeling or with stable isotope labeling Stable isotope labeled AQUA TM Peptide seqeunces contain one isotopically labeled amino acid Sequence Length 5 to 30 amino acids Amount 5 x 1 nmole Purity 95 by RP HPLC Modifications phosphorylation Ser Thr Tyr carboxymethylated Cys carbamidomethylated Cys hydroxyproline N terminal biotin please inquire regarding other modifications Quantification by amino acid analysis AAA Format Supplied dryRequest more information
    https://www.bioz.com/result/c terminal modified csg peptide/product/Millipore
    Average 99 stars, based on 20563 article reviews
    Price from $9.99 to $1999.99
    c terminal modified csg peptide - by Bioz Stars, 2020-09
    99/100 stars

    Images

    1) Product Images from "Immune‐mediated ECM depletion improves tumour perfusion and payload delivery"

    Article Title: Immune‐mediated ECM depletion improves tumour perfusion and payload delivery

    Journal: EMBO Molecular Medicine

    doi: 10.15252/emmm.201910923

    The effects of TNFα‐CSG on tumour ECM and perfusion Comparison of CD8 + T‐cell (red) or ECM content (laminin, red) in tumour (T) and the surrounding normal pancreas (N Pan) for RIP1‐Tag5 mice treated with 5 daily doses on indicated compound. Scale bars: 100 μm. Stiffness analyses of the RIP1‐Tag5 tumours following treatment with 4 × daily i.v. injections of indicated compounds. Tumour stiffness was analysed on day 5. Left panel: En face quantitative micro‐elastograms showing tumour stiffness (red arrow: stiffest zones). Right panel: The corresponding micrograph of haematoxylin and eosin (HE) staining of the tumours (yellow arrow: ECM‐rich zone). Scale bars: 400 μm. Micrographs show lectin + vessels (green) in 4T1 tumours, after mice were treated with 5 daily injections of indicated compounds and perfused with fluorescein‐labelled lectin to visualise patent blood vessels. Data show average vessel width for individual tumours and mean ± SEM for each group ( n = 4; **P
    Figure Legend Snippet: The effects of TNFα‐CSG on tumour ECM and perfusion Comparison of CD8 + T‐cell (red) or ECM content (laminin, red) in tumour (T) and the surrounding normal pancreas (N Pan) for RIP1‐Tag5 mice treated with 5 daily doses on indicated compound. Scale bars: 100 μm. Stiffness analyses of the RIP1‐Tag5 tumours following treatment with 4 × daily i.v. injections of indicated compounds. Tumour stiffness was analysed on day 5. Left panel: En face quantitative micro‐elastograms showing tumour stiffness (red arrow: stiffest zones). Right panel: The corresponding micrograph of haematoxylin and eosin (HE) staining of the tumours (yellow arrow: ECM‐rich zone). Scale bars: 400 μm. Micrographs show lectin + vessels (green) in 4T1 tumours, after mice were treated with 5 daily injections of indicated compounds and perfused with fluorescein‐labelled lectin to visualise patent blood vessels. Data show average vessel width for individual tumours and mean ± SEM for each group ( n = 4; **P

    Techniques Used: Mouse Assay, Staining

    TNFα‐CSG therapy enhances survival, suppresses tumour growth and generates intratumoral effector T cells Per cent survival of mice bearing RIP1‐Tag5 and 4T1 tumours, either untreated or treated according to the schedule depicted ( n = 16–27 for RIP1‐Tag5 and n = 5 for 4T1; ** P
    Figure Legend Snippet: TNFα‐CSG therapy enhances survival, suppresses tumour growth and generates intratumoral effector T cells Per cent survival of mice bearing RIP1‐Tag5 and 4T1 tumours, either untreated or treated according to the schedule depicted ( n = 16–27 for RIP1‐Tag5 and n = 5 for 4T1; ** P

    Techniques Used: Mouse Assay

    CD8 + and CD4 + T cells mediate ECM degradation and anti‐tumour effects of TNFα‐CSG BALB/c nude mice bearing 4T1 tumours were treated with 5 daily i.v. injections of TNFα‐CSG in the absence or presence of naïve splenic CD4 + and CD8 + T cells, or both (triple treatment). The cells were injected i.p. on days 10 and 13. On day 16 post‐implantation, the tumours were analysed for weight and volume (B), immune infiltrates (C) and collagen IV content (D). Plots of individual tumour weights (g) and volumes (mm 3 ) and mean ± SEM on day 16 are shown for untreated (UT) and treated groups ( n = 5; * P
    Figure Legend Snippet: CD8 + and CD4 + T cells mediate ECM degradation and anti‐tumour effects of TNFα‐CSG BALB/c nude mice bearing 4T1 tumours were treated with 5 daily i.v. injections of TNFα‐CSG in the absence or presence of naïve splenic CD4 + and CD8 + T cells, or both (triple treatment). The cells were injected i.p. on days 10 and 13. On day 16 post‐implantation, the tumours were analysed for weight and volume (B), immune infiltrates (C) and collagen IV content (D). Plots of individual tumour weights (g) and volumes (mm 3 ) and mean ± SEM on day 16 are shown for untreated (UT) and treated groups ( n = 5; * P

    Techniques Used: Mouse Assay, Injection

    The effects of TNFα‐CSG on immune infiltrates and protease mRNA transcripts and ECM components Quantitative PCR analysis was performed on (top) macrophages (CD45 + /CD11b + cells) isolated from 4T1 tumours treated with 5 daily injections of indicated compounds and (bottom) cultured 4T1 cells incubated overnight with indicated compounds. Hypoxanthine‐guanine phosphoribosyltransferase (HPRT) was used as a standard (mean ± SEM are shown; n = 5; *** P
    Figure Legend Snippet: The effects of TNFα‐CSG on immune infiltrates and protease mRNA transcripts and ECM components Quantitative PCR analysis was performed on (top) macrophages (CD45 + /CD11b + cells) isolated from 4T1 tumours treated with 5 daily injections of indicated compounds and (bottom) cultured 4T1 cells incubated overnight with indicated compounds. Hypoxanthine‐guanine phosphoribosyltransferase (HPRT) was used as a standard (mean ± SEM are shown; n = 5; *** P

    Techniques Used: Real-time Polymerase Chain Reaction, Isolation, Cell Culture, Incubation

    The effects of TNFα‐CSG on immune infiltrates in tumours Co‐staining of RIP1‐Tag5 tumour sections treated with 5 daily doses of indicated compounds. Micrographs show CD8 + T‐cell (red) infiltration relative to collagen IV (A; green) and CD31 + blood vessels (B; green). Scale bars: 100 μm. Left panels show representative flow cytometry plots of quantification of immune cells in 4T1 tumours treated with 5 daily i.v. injections of 0.5 μg of unconjugated TNFα or TNFα‐CSG, or left untreated (UT). Bar charts show mean ± SEM of cell counts in each treatment group (data are shown for one of the two repeated experiments; n = 4; * P
    Figure Legend Snippet: The effects of TNFα‐CSG on immune infiltrates in tumours Co‐staining of RIP1‐Tag5 tumour sections treated with 5 daily doses of indicated compounds. Micrographs show CD8 + T‐cell (red) infiltration relative to collagen IV (A; green) and CD31 + blood vessels (B; green). Scale bars: 100 μm. Left panels show representative flow cytometry plots of quantification of immune cells in 4T1 tumours treated with 5 daily i.v. injections of 0.5 μg of unconjugated TNFα or TNFα‐CSG, or left untreated (UT). Bar charts show mean ± SEM of cell counts in each treatment group (data are shown for one of the two repeated experiments; n = 4; * P

    Techniques Used: Staining, Flow Cytometry, Cytometry

    ECM depletion in TNFα‐CSG‐treated tumours (T‐CSG) correlates with decompressed blood vessels, and enhanced perfusion and uptake of nanoparticles Lectin + vesse ls (green) in tumours after RIP1‐Tag5 mice were treated with 5 daily i.v. injections of indicated compounds (or untreated, UT) and perfused with fluorescein‐labelled lectin. Representative micrographs show lectin + vessel widths for each group, and quantification of mean vessel diameter/tumour area and mean ± SEM are shown (12–15 tumours from n = 5 mice; **** P
    Figure Legend Snippet: ECM depletion in TNFα‐CSG‐treated tumours (T‐CSG) correlates with decompressed blood vessels, and enhanced perfusion and uptake of nanoparticles Lectin + vesse ls (green) in tumours after RIP1‐Tag5 mice were treated with 5 daily i.v. injections of indicated compounds (or untreated, UT) and perfused with fluorescein‐labelled lectin. Representative micrographs show lectin + vessel widths for each group, and quantification of mean vessel diameter/tumour area and mean ± SEM are shown (12–15 tumours from n = 5 mice; **** P

    Techniques Used: Mouse Assay

    TNFα‐CSG treatment reduces tumour stiffness En face optical coherence tomography (OCT) images of tumours at a depth of ˜100 μm. Scale bars: 1 mm. The corresponding en face quantitative micro‐elastograms showing tumour elasticity. Scale bars: 1 mm. Plots of stiffness distribution in the tumours. Top: Stiffness variance (see Materials and Methods ). Bottom: Fractions of pixels between 100 and 1,000 kPa. For both plots, mean ± SEM is shown ( n = 3; * P
    Figure Legend Snippet: TNFα‐CSG treatment reduces tumour stiffness En face optical coherence tomography (OCT) images of tumours at a depth of ˜100 μm. Scale bars: 1 mm. The corresponding en face quantitative micro‐elastograms showing tumour elasticity. Scale bars: 1 mm. Plots of stiffness distribution in the tumours. Top: Stiffness variance (see Materials and Methods ). Bottom: Fractions of pixels between 100 and 1,000 kPa. For both plots, mean ± SEM is shown ( n = 3; * P

    Techniques Used:

    TNFα‐CSG (T‐CSG) treatment promotes immune cell infiltration and induces them to secrete proteases Left panels: Representative micrographs of immune cell infiltrates (red) in tumours from RIP1‐Tag5 mice untreated (UT) or treated with 5 daily i.v. injections of indicated compounds. Scale bars: 100 μm. Right panels: fraction of cells stained with the indicated antibodies/tumour and mean ± SEM (4–7 tumours from n = 3 mice; * P
    Figure Legend Snippet: TNFα‐CSG (T‐CSG) treatment promotes immune cell infiltration and induces them to secrete proteases Left panels: Representative micrographs of immune cell infiltrates (red) in tumours from RIP1‐Tag5 mice untreated (UT) or treated with 5 daily i.v. injections of indicated compounds. Scale bars: 100 μm. Right panels: fraction of cells stained with the indicated antibodies/tumour and mean ± SEM (4–7 tumours from n = 3 mice; * P

    Techniques Used: Mouse Assay, Staining

    TNFα‐CSG treatment induces specific tumour ECM degradation Staining with indicated antibodies (red) for tissues treated with 5 μg doses of TNFα‐CSG (T‐CSG) or TNFα‐RGR (T‐RGR), or 0.8 μg doses of CSG peptide. Scale bars: 50 μm. Quantitative analysis of ECM staining/field/tumour from panel (A) and mean ± SEM (3–8 tumours from n = 3 mice; * P
    Figure Legend Snippet: TNFα‐CSG treatment induces specific tumour ECM degradation Staining with indicated antibodies (red) for tissues treated with 5 μg doses of TNFα‐CSG (T‐CSG) or TNFα‐RGR (T‐RGR), or 0.8 μg doses of CSG peptide. Scale bars: 50 μm. Quantitative analysis of ECM staining/field/tumour from panel (A) and mean ± SEM (3–8 tumours from n = 3 mice; * P

    Techniques Used: Staining, Mouse Assay

    2) Product Images from "Effect and mechanism of the aβ2-GP I/rhβ2-GP I complex on JEG-3 cell proliferation, migration and invasion"

    Article Title: Effect and mechanism of the aβ2-GP I/rhβ2-GP I complex on JEG-3 cell proliferation, migration and invasion

    Journal: Molecular Medicine Reports

    doi: 10.3892/mmr.2018.8822

    Prokaryotic expression and purification of rhβ2-GP I. (A) The prokaryotic expression fusion protein rhβ2-GP I was identified following 2, 4, 6 h of extension incubation of transfected E. coli BL21 (DE3) cells with 0.1 mM IPTG and bacterium lysate was detected by SDS-PAGE and Coomassie staining, as indicated by the arrow. (B) The fusion protein with His-tag was successfully purified by Ni-NTA chelating agarose and detected by SDS-PAGE and Coomassie staining. Furthermore, the purified protein was detected by western blotting with anti-His antibody and was employed to detected the His-tagged protein (far right). IPTG, isopropyl β-D-1-thiogalactopyranoside; aβ2-GP I, anti-β2-glycoprotein; rh, human recombinant.
    Figure Legend Snippet: Prokaryotic expression and purification of rhβ2-GP I. (A) The prokaryotic expression fusion protein rhβ2-GP I was identified following 2, 4, 6 h of extension incubation of transfected E. coli BL21 (DE3) cells with 0.1 mM IPTG and bacterium lysate was detected by SDS-PAGE and Coomassie staining, as indicated by the arrow. (B) The fusion protein with His-tag was successfully purified by Ni-NTA chelating agarose and detected by SDS-PAGE and Coomassie staining. Furthermore, the purified protein was detected by western blotting with anti-His antibody and was employed to detected the His-tagged protein (far right). IPTG, isopropyl β-D-1-thiogalactopyranoside; aβ2-GP I, anti-β2-glycoprotein; rh, human recombinant.

    Techniques Used: Expressing, Purification, Incubation, Transfection, SDS Page, Staining, Western Blot, Recombinant

    3) Product Images from "Effect and mechanism of the aβ2-GP I/rhβ2-GP I complex on JEG-3 cell proliferation, migration and invasion"

    Article Title: Effect and mechanism of the aβ2-GP I/rhβ2-GP I complex on JEG-3 cell proliferation, migration and invasion

    Journal: Molecular Medicine Reports

    doi: 10.3892/mmr.2018.8822

    Effects of aβ2-GP I/rhβ2-GP I complexes on JEG-3 cell proliferation. (A) Cell proliferation was assessed by CCK-8 assay (n=3). (B) EdU staining for cell proliferation (magnification, ×100) (n=3). Red: EdU stained nuclei of proliferating cells; blue: All nuclei counterstained with Hoechst (all reagents were from EdU labeling kit). The statistical analysis of EdU staining was performed by Image-Pro Plus 6.0 software. (C) Cell cycle was analyzed by flow cytometry following 24-h incubations. Statistical analysis of % cell population in each stage of cell cycle was performed. IgG, rhβ2-GP I, aβ2-GP I and IgG/rhβ2-GP I were regarded as controls. *P
    Figure Legend Snippet: Effects of aβ2-GP I/rhβ2-GP I complexes on JEG-3 cell proliferation. (A) Cell proliferation was assessed by CCK-8 assay (n=3). (B) EdU staining for cell proliferation (magnification, ×100) (n=3). Red: EdU stained nuclei of proliferating cells; blue: All nuclei counterstained with Hoechst (all reagents were from EdU labeling kit). The statistical analysis of EdU staining was performed by Image-Pro Plus 6.0 software. (C) Cell cycle was analyzed by flow cytometry following 24-h incubations. Statistical analysis of % cell population in each stage of cell cycle was performed. IgG, rhβ2-GP I, aβ2-GP I and IgG/rhβ2-GP I were regarded as controls. *P

    Techniques Used: CCK-8 Assay, Staining, Labeling, Software, Flow Cytometry, Cytometry

    Prokaryotic expression and purification of rhβ2-GP I. (A) The prokaryotic expression fusion protein rhβ2-GP I was identified following 2, 4, 6 h of extension incubation of transfected E. coli BL21 (DE3) cells with 0.1 mM IPTG and bacterium lysate was detected by SDS-PAGE and Coomassie staining, as indicated by the arrow. (B) The fusion protein with His-tag was successfully purified by Ni-NTA chelating agarose and detected by SDS-PAGE and Coomassie staining. Furthermore, the purified protein was detected by western blotting with anti-His antibody and was employed to detected the His-tagged protein (far right). IPTG, isopropyl β-D-1-thiogalactopyranoside; aβ2-GP I, anti-β2-glycoprotein; rh, human recombinant.
    Figure Legend Snippet: Prokaryotic expression and purification of rhβ2-GP I. (A) The prokaryotic expression fusion protein rhβ2-GP I was identified following 2, 4, 6 h of extension incubation of transfected E. coli BL21 (DE3) cells with 0.1 mM IPTG and bacterium lysate was detected by SDS-PAGE and Coomassie staining, as indicated by the arrow. (B) The fusion protein with His-tag was successfully purified by Ni-NTA chelating agarose and detected by SDS-PAGE and Coomassie staining. Furthermore, the purified protein was detected by western blotting with anti-His antibody and was employed to detected the His-tagged protein (far right). IPTG, isopropyl β-D-1-thiogalactopyranoside; aβ2-GP I, anti-β2-glycoprotein; rh, human recombinant.

    Techniques Used: Expressing, Purification, Incubation, Transfection, SDS Page, Staining, Western Blot, Recombinant

    aβ2-GP I/rhβ2-GP I complex induces the activity of NF-κB in JEG-3 cells. (A) Relative mRNA expressions of MyD88, IKKβ, NF-κB and IκBα in JEG-3 cell line. (B) The protein level of MyD88, IκBα and p-IκBα in stimulated JEG-3 cells detected by western blotting. The data statistics of western blot test was performed by Image-Pro Plus 6.0 software. (C) Luciferase activity was measured to assess NF-κB expression. IgG, rhβ2-GP I, aβ2-GP I and IgG/rhβ2-GPI were regarded as controls. *P
    Figure Legend Snippet: aβ2-GP I/rhβ2-GP I complex induces the activity of NF-κB in JEG-3 cells. (A) Relative mRNA expressions of MyD88, IKKβ, NF-κB and IκBα in JEG-3 cell line. (B) The protein level of MyD88, IκBα and p-IκBα in stimulated JEG-3 cells detected by western blotting. The data statistics of western blot test was performed by Image-Pro Plus 6.0 software. (C) Luciferase activity was measured to assess NF-κB expression. IgG, rhβ2-GP I, aβ2-GP I and IgG/rhβ2-GPI were regarded as controls. *P

    Techniques Used: Activity Assay, Western Blot, Software, Luciferase, Expressing

    Effects of the aβ2-GP I/rhβ2-GP I complex on JEG-3 cell migration and invasion, and protein expression levels of tumor metastasis- and diffusion-associated factors. (A and B) Cell migration measured by transwell assay (magnification, ×200). Statistical analysis of the results of the transwell assay was performed using Image-Pro Plus 6.0 software. (C and D) Protein levels of N-cadherin, E-cadherin and γ-caterin were detected by western blotting. Statistical analysis was performed by Image-Pro Plus 6.0 software. IgG, rhβ2-GP I, aβ2-GPIand IgG/rhβ2-GP I were regarded as controls. *P
    Figure Legend Snippet: Effects of the aβ2-GP I/rhβ2-GP I complex on JEG-3 cell migration and invasion, and protein expression levels of tumor metastasis- and diffusion-associated factors. (A and B) Cell migration measured by transwell assay (magnification, ×200). Statistical analysis of the results of the transwell assay was performed using Image-Pro Plus 6.0 software. (C and D) Protein levels of N-cadherin, E-cadherin and γ-caterin were detected by western blotting. Statistical analysis was performed by Image-Pro Plus 6.0 software. IgG, rhβ2-GP I, aβ2-GPIand IgG/rhβ2-GP I were regarded as controls. *P

    Techniques Used: Migration, Expressing, Diffusion-based Assay, Transwell Assay, Software, Western Blot

    4) Product Images from "Immune‐mediated ECM depletion improves tumour perfusion and payload delivery"

    Article Title: Immune‐mediated ECM depletion improves tumour perfusion and payload delivery

    Journal: EMBO Molecular Medicine

    doi: 10.15252/emmm.201910923

    The effects of TNFα‐CSG on tumour ECM and perfusion Comparison of CD8 + T‐cell (red) or ECM content (laminin, red) in tumour (T) and the surrounding normal pancreas (N Pan) for RIP1‐Tag5 mice treated with 5 daily doses on indicated compound. Scale bars: 100 μm. Stiffness analyses of the RIP1‐Tag5 tumours following treatment with 4 × daily i.v. injections of indicated compounds. Tumour stiffness was analysed on day 5. Left panel: En face quantitative micro‐elastograms showing tumour stiffness (red arrow: stiffest zones). Right panel: The corresponding micrograph of haematoxylin and eosin (HE) staining of the tumours (yellow arrow: ECM‐rich zone). Scale bars: 400 μm. Micrographs show lectin + vessels (green) in 4T1 tumours, after mice were treated with 5 daily injections of indicated compounds and perfused with fluorescein‐labelled lectin to visualise patent blood vessels. Data show average vessel width for individual tumours and mean ± SEM for each group ( n = 4; **P
    Figure Legend Snippet: The effects of TNFα‐CSG on tumour ECM and perfusion Comparison of CD8 + T‐cell (red) or ECM content (laminin, red) in tumour (T) and the surrounding normal pancreas (N Pan) for RIP1‐Tag5 mice treated with 5 daily doses on indicated compound. Scale bars: 100 μm. Stiffness analyses of the RIP1‐Tag5 tumours following treatment with 4 × daily i.v. injections of indicated compounds. Tumour stiffness was analysed on day 5. Left panel: En face quantitative micro‐elastograms showing tumour stiffness (red arrow: stiffest zones). Right panel: The corresponding micrograph of haematoxylin and eosin (HE) staining of the tumours (yellow arrow: ECM‐rich zone). Scale bars: 400 μm. Micrographs show lectin + vessels (green) in 4T1 tumours, after mice were treated with 5 daily injections of indicated compounds and perfused with fluorescein‐labelled lectin to visualise patent blood vessels. Data show average vessel width for individual tumours and mean ± SEM for each group ( n = 4; **P

    Techniques Used: Mouse Assay, Staining

    TNFα‐CSG therapy enhances survival, suppresses tumour growth and generates intratumoral effector T cells Per cent survival of mice bearing RIP1‐Tag5 and 4T1 tumours, either untreated or treated according to the schedule depicted ( n = 16–27 for RIP1‐Tag5 and n = 5 for 4T1; ** P
    Figure Legend Snippet: TNFα‐CSG therapy enhances survival, suppresses tumour growth and generates intratumoral effector T cells Per cent survival of mice bearing RIP1‐Tag5 and 4T1 tumours, either untreated or treated according to the schedule depicted ( n = 16–27 for RIP1‐Tag5 and n = 5 for 4T1; ** P

    Techniques Used: Mouse Assay

    CD8 + and CD4 + T cells mediate ECM degradation and anti‐tumour effects of TNFα‐CSG BALB/c nude mice bearing 4T1 tumours were treated with 5 daily i.v. injections of TNFα‐CSG in the absence or presence of naïve splenic CD4 + and CD8 + T cells, or both (triple treatment). The cells were injected i.p. on days 10 and 13. On day 16 post‐implantation, the tumours were analysed for weight and volume (B), immune infiltrates (C) and collagen IV content (D). Plots of individual tumour weights (g) and volumes (mm 3 ) and mean ± SEM on day 16 are shown for untreated (UT) and treated groups ( n = 5; * P
    Figure Legend Snippet: CD8 + and CD4 + T cells mediate ECM degradation and anti‐tumour effects of TNFα‐CSG BALB/c nude mice bearing 4T1 tumours were treated with 5 daily i.v. injections of TNFα‐CSG in the absence or presence of naïve splenic CD4 + and CD8 + T cells, or both (triple treatment). The cells were injected i.p. on days 10 and 13. On day 16 post‐implantation, the tumours were analysed for weight and volume (B), immune infiltrates (C) and collagen IV content (D). Plots of individual tumour weights (g) and volumes (mm 3 ) and mean ± SEM on day 16 are shown for untreated (UT) and treated groups ( n = 5; * P

    Techniques Used: Mouse Assay, Injection

    The effects of TNFα‐CSG on immune infiltrates and protease mRNA transcripts and ECM components Quantitative PCR analysis was performed on (top) macrophages (CD45 + /CD11b + cells) isolated from 4T1 tumours treated with 5 daily injections of indicated compounds and (bottom) cultured 4T1 cells incubated overnight with indicated compounds. Hypoxanthine‐guanine phosphoribosyltransferase (HPRT) was used as a standard (mean ± SEM are shown; n = 5; *** P
    Figure Legend Snippet: The effects of TNFα‐CSG on immune infiltrates and protease mRNA transcripts and ECM components Quantitative PCR analysis was performed on (top) macrophages (CD45 + /CD11b + cells) isolated from 4T1 tumours treated with 5 daily injections of indicated compounds and (bottom) cultured 4T1 cells incubated overnight with indicated compounds. Hypoxanthine‐guanine phosphoribosyltransferase (HPRT) was used as a standard (mean ± SEM are shown; n = 5; *** P

    Techniques Used: Real-time Polymerase Chain Reaction, Isolation, Cell Culture, Incubation

    The effects of TNFα‐CSG on immune infiltrates in tumours Co‐staining of RIP1‐Tag5 tumour sections treated with 5 daily doses of indicated compounds. Micrographs show CD8 + T‐cell (red) infiltration relative to collagen IV (A; green) and CD31 + blood vessels (B; green). Scale bars: 100 μm. Left panels show representative flow cytometry plots of quantification of immune cells in 4T1 tumours treated with 5 daily i.v. injections of 0.5 μg of unconjugated TNFα or TNFα‐CSG, or left untreated (UT). Bar charts show mean ± SEM of cell counts in each treatment group (data are shown for one of the two repeated experiments; n = 4; * P
    Figure Legend Snippet: The effects of TNFα‐CSG on immune infiltrates in tumours Co‐staining of RIP1‐Tag5 tumour sections treated with 5 daily doses of indicated compounds. Micrographs show CD8 + T‐cell (red) infiltration relative to collagen IV (A; green) and CD31 + blood vessels (B; green). Scale bars: 100 μm. Left panels show representative flow cytometry plots of quantification of immune cells in 4T1 tumours treated with 5 daily i.v. injections of 0.5 μg of unconjugated TNFα or TNFα‐CSG, or left untreated (UT). Bar charts show mean ± SEM of cell counts in each treatment group (data are shown for one of the two repeated experiments; n = 4; * P

    Techniques Used: Staining, Flow Cytometry, Cytometry

    ECM depletion in TNFα‐CSG‐treated tumours (T‐CSG) correlates with decompressed blood vessels, and enhanced perfusion and uptake of nanoparticles Lectin + vesse ls (green) in tumours after RIP1‐Tag5 mice were treated with 5 daily i.v. injections of indicated compounds (or untreated, UT) and perfused with fluorescein‐labelled lectin. Representative micrographs show lectin + vessel widths for each group, and quantification of mean vessel diameter/tumour area and mean ± SEM are shown (12–15 tumours from n = 5 mice; **** P
    Figure Legend Snippet: ECM depletion in TNFα‐CSG‐treated tumours (T‐CSG) correlates with decompressed blood vessels, and enhanced perfusion and uptake of nanoparticles Lectin + vesse ls (green) in tumours after RIP1‐Tag5 mice were treated with 5 daily i.v. injections of indicated compounds (or untreated, UT) and perfused with fluorescein‐labelled lectin. Representative micrographs show lectin + vessel widths for each group, and quantification of mean vessel diameter/tumour area and mean ± SEM are shown (12–15 tumours from n = 5 mice; **** P

    Techniques Used: Mouse Assay

    TNFα‐CSG treatment reduces tumour stiffness En face optical coherence tomography (OCT) images of tumours at a depth of ˜100 μm. Scale bars: 1 mm. The corresponding en face quantitative micro‐elastograms showing tumour elasticity. Scale bars: 1 mm. Plots of stiffness distribution in the tumours. Top: Stiffness variance (see Materials and Methods ). Bottom: Fractions of pixels between 100 and 1,000 kPa. For both plots, mean ± SEM is shown ( n = 3; * P
    Figure Legend Snippet: TNFα‐CSG treatment reduces tumour stiffness En face optical coherence tomography (OCT) images of tumours at a depth of ˜100 μm. Scale bars: 1 mm. The corresponding en face quantitative micro‐elastograms showing tumour elasticity. Scale bars: 1 mm. Plots of stiffness distribution in the tumours. Top: Stiffness variance (see Materials and Methods ). Bottom: Fractions of pixels between 100 and 1,000 kPa. For both plots, mean ± SEM is shown ( n = 3; * P

    Techniques Used:

    TNFα‐CSG (T‐CSG) treatment promotes immune cell infiltration and induces them to secrete proteases Left panels: Representative micrographs of immune cell infiltrates (red) in tumours from RIP1‐Tag5 mice untreated (UT) or treated with 5 daily i.v. injections of indicated compounds. Scale bars: 100 μm. Right panels: fraction of cells stained with the indicated antibodies/tumour and mean ± SEM (4–7 tumours from n = 3 mice; * P
    Figure Legend Snippet: TNFα‐CSG (T‐CSG) treatment promotes immune cell infiltration and induces them to secrete proteases Left panels: Representative micrographs of immune cell infiltrates (red) in tumours from RIP1‐Tag5 mice untreated (UT) or treated with 5 daily i.v. injections of indicated compounds. Scale bars: 100 μm. Right panels: fraction of cells stained with the indicated antibodies/tumour and mean ± SEM (4–7 tumours from n = 3 mice; * P

    Techniques Used: Mouse Assay, Staining

    TNFα‐CSG treatment induces specific tumour ECM degradation Staining with indicated antibodies (red) for tissues treated with 5 μg doses of TNFα‐CSG (T‐CSG) or TNFα‐RGR (T‐RGR), or 0.8 μg doses of CSG peptide. Scale bars: 50 μm. Quantitative analysis of ECM staining/field/tumour from panel (A) and mean ± SEM (3–8 tumours from n = 3 mice; * P
    Figure Legend Snippet: TNFα‐CSG treatment induces specific tumour ECM degradation Staining with indicated antibodies (red) for tissues treated with 5 μg doses of TNFα‐CSG (T‐CSG) or TNFα‐RGR (T‐RGR), or 0.8 μg doses of CSG peptide. Scale bars: 50 μm. Quantitative analysis of ECM staining/field/tumour from panel (A) and mean ± SEM (3–8 tumours from n = 3 mice; * P

    Techniques Used: Staining, Mouse Assay

    5) Product Images from "Functional Importance of the Anaphase-Promoting Complex-Cdh1-Mediated Degradation of TMAP/CKAP2 in Regulation of Spindle Function and Cytokinesis ▿Functional Importance of the Anaphase-Promoting Complex-Cdh1-Mediated Degradation of TMAP/CKAP2 in Regulation of Spindle Function and Cytokinesis ▿ †"

    Article Title: Functional Importance of the Anaphase-Promoting Complex-Cdh1-Mediated Degradation of TMAP/CKAP2 in Regulation of Spindle Function and Cytokinesis ▿Functional Importance of the Anaphase-Promoting Complex-Cdh1-Mediated Degradation of TMAP/CKAP2 in Regulation of Spindle Function and Cytokinesis ▿ †

    Journal:

    doi: 10.1128/MCB.01386-06

    Degradation of TMAP/CKAP2 during mitotic exit is mediated by APC-Cdh1. (A) Ectopic overexpression of Cdh1 induces cell cycle-independent degradation of TMAP/CKAP2. HeLa cells were cotransfected with GFP-CKAP2 and various amounts of myc-Cdh1 or myc-Cdc20
    Figure Legend Snippet: Degradation of TMAP/CKAP2 during mitotic exit is mediated by APC-Cdh1. (A) Ectopic overexpression of Cdh1 induces cell cycle-independent degradation of TMAP/CKAP2. HeLa cells were cotransfected with GFP-CKAP2 and various amounts of myc-Cdh1 or myc-Cdc20

    Techniques Used: Over Expression

    TMAP/CKAP2 is rapidly degraded during mitotic exit via the ubiquitin-proteasome pathway. (A) TMAP/CKAP2 is degraded during mitotic exit. HeLa cells arrested at mitosis by nocodazole treatment (0 h) were released into nocodazole-free medium and analyzed
    Figure Legend Snippet: TMAP/CKAP2 is rapidly degraded during mitotic exit via the ubiquitin-proteasome pathway. (A) TMAP/CKAP2 is degraded during mitotic exit. HeLa cells arrested at mitosis by nocodazole treatment (0 h) were released into nocodazole-free medium and analyzed

    Techniques Used:

    Overexpression of TMAP/CKAP2 results in mitotic arrest. (A) The proportion of G 2 /M cell population is significantly increased in TMAP/CKAP2-overexpressing cells. HeLa or HEK 293 cells were transfected with a vector control (Vector) or a myc-tagged (human)
    Figure Legend Snippet: Overexpression of TMAP/CKAP2 results in mitotic arrest. (A) The proportion of G 2 /M cell population is significantly increased in TMAP/CKAP2-overexpressing cells. HeLa or HEK 293 cells were transfected with a vector control (Vector) or a myc-tagged (human)

    Techniques Used: Over Expression, Transfection, Plasmid Preparation

    Expression of nondegradable KENmut TMAP/CKAP2 results in the formation of spindle defects and failure of cytokinesis. (A) HEK 293 cells were transfected with GFP-WT CKAP2 (WT) or GFP-KENmut CKAP2 (KEN) and were observed using time-lapse video microscopy.
    Figure Legend Snippet: Expression of nondegradable KENmut TMAP/CKAP2 results in the formation of spindle defects and failure of cytokinesis. (A) HEK 293 cells were transfected with GFP-WT CKAP2 (WT) or GFP-KENmut CKAP2 (KEN) and were observed using time-lapse video microscopy.

    Techniques Used: Expressing, Transfection, Microscopy

    Subcellular localization of TMAP/CKAP2 during mitosis. NIH 3T3 cells were fixed and doubly immunostained for TMAP/CKAP2 (green) and α-tubulin (red). Representative images of cells at different stages of mitosis are shown.
    Figure Legend Snippet: Subcellular localization of TMAP/CKAP2 during mitosis. NIH 3T3 cells were fixed and doubly immunostained for TMAP/CKAP2 (green) and α-tubulin (red). Representative images of cells at different stages of mitosis are shown.

    Techniques Used:

    Overexpression of TMAP/CKAP2 results in formation of spindle abnormalities due to a defect in centrosome separation. (A) Quantitative analysis of the percentage of mitotic cells with abnormal spindles among GFP- or GFP-CKAP2-expressing HEK 293A. HEK 293
    Figure Legend Snippet: Overexpression of TMAP/CKAP2 results in formation of spindle abnormalities due to a defect in centrosome separation. (A) Quantitative analysis of the percentage of mitotic cells with abnormal spindles among GFP- or GFP-CKAP2-expressing HEK 293A. HEK 293

    Techniques Used: Over Expression, Expressing

    Fate of TMAP/CKAP2-overexpressing cells developing spindle defects. HEK 293 cells transfected with GFP-CKAP2 were observed for 48 h using a time-lapse video microscope as described in Materials and Methods. (A) A total of 38 individual GFP-CKAP2-positive
    Figure Legend Snippet: Fate of TMAP/CKAP2-overexpressing cells developing spindle defects. HEK 293 cells transfected with GFP-CKAP2 were observed for 48 h using a time-lapse video microscope as described in Materials and Methods. (A) A total of 38 individual GFP-CKAP2-positive

    Techniques Used: Transfection, Microscopy

    Degradation of TMAP/CKAP2 is mediated by the KEN box destruction motif located near the N terminus. (A) Degradability of deletion mutants of TMAP/CKAP2 during mitotic exit. HeLa cells transfected with the myc-tagged full-length or indicated deletion mutants
    Figure Legend Snippet: Degradation of TMAP/CKAP2 is mediated by the KEN box destruction motif located near the N terminus. (A) Degradability of deletion mutants of TMAP/CKAP2 during mitotic exit. HeLa cells transfected with the myc-tagged full-length or indicated deletion mutants

    Techniques Used: Transfection

    6) Product Images from "Functional Importance of the Anaphase-Promoting Complex-Cdh1-Mediated Degradation of TMAP/CKAP2 in Regulation of Spindle Function and Cytokinesis ▿Functional Importance of the Anaphase-Promoting Complex-Cdh1-Mediated Degradation of TMAP/CKAP2 in Regulation of Spindle Function and Cytokinesis ▿ †"

    Article Title: Functional Importance of the Anaphase-Promoting Complex-Cdh1-Mediated Degradation of TMAP/CKAP2 in Regulation of Spindle Function and Cytokinesis ▿Functional Importance of the Anaphase-Promoting Complex-Cdh1-Mediated Degradation of TMAP/CKAP2 in Regulation of Spindle Function and Cytokinesis ▿ †

    Journal:

    doi: 10.1128/MCB.01386-06

    Degradation of TMAP/CKAP2 during mitotic exit is mediated by APC-Cdh1. (A) Ectopic overexpression of Cdh1 induces cell cycle-independent degradation of TMAP/CKAP2. HeLa cells were cotransfected with GFP-CKAP2 and various amounts of myc-Cdh1 or myc-Cdc20
    Figure Legend Snippet: Degradation of TMAP/CKAP2 during mitotic exit is mediated by APC-Cdh1. (A) Ectopic overexpression of Cdh1 induces cell cycle-independent degradation of TMAP/CKAP2. HeLa cells were cotransfected with GFP-CKAP2 and various amounts of myc-Cdh1 or myc-Cdc20

    Techniques Used: Over Expression

    TMAP/CKAP2 is rapidly degraded during mitotic exit via the ubiquitin-proteasome pathway. (A) TMAP/CKAP2 is degraded during mitotic exit. HeLa cells arrested at mitosis by nocodazole treatment (0 h) were released into nocodazole-free medium and analyzed
    Figure Legend Snippet: TMAP/CKAP2 is rapidly degraded during mitotic exit via the ubiquitin-proteasome pathway. (A) TMAP/CKAP2 is degraded during mitotic exit. HeLa cells arrested at mitosis by nocodazole treatment (0 h) were released into nocodazole-free medium and analyzed

    Techniques Used:

    Overexpression of TMAP/CKAP2 results in mitotic arrest. (A) The proportion of G 2 /M cell population is significantly increased in TMAP/CKAP2-overexpressing cells. HeLa or HEK 293 cells were transfected with a vector control (Vector) or a myc-tagged (human)
    Figure Legend Snippet: Overexpression of TMAP/CKAP2 results in mitotic arrest. (A) The proportion of G 2 /M cell population is significantly increased in TMAP/CKAP2-overexpressing cells. HeLa or HEK 293 cells were transfected with a vector control (Vector) or a myc-tagged (human)

    Techniques Used: Over Expression, Transfection, Plasmid Preparation

    Expression of nondegradable KENmut TMAP/CKAP2 results in the formation of spindle defects and failure of cytokinesis. (A) HEK 293 cells were transfected with GFP-WT CKAP2 (WT) or GFP-KENmut CKAP2 (KEN) and were observed using time-lapse video microscopy.
    Figure Legend Snippet: Expression of nondegradable KENmut TMAP/CKAP2 results in the formation of spindle defects and failure of cytokinesis. (A) HEK 293 cells were transfected with GFP-WT CKAP2 (WT) or GFP-KENmut CKAP2 (KEN) and were observed using time-lapse video microscopy.

    Techniques Used: Expressing, Transfection, Microscopy

    Subcellular localization of TMAP/CKAP2 during mitosis. NIH 3T3 cells were fixed and doubly immunostained for TMAP/CKAP2 (green) and α-tubulin (red). Representative images of cells at different stages of mitosis are shown.
    Figure Legend Snippet: Subcellular localization of TMAP/CKAP2 during mitosis. NIH 3T3 cells were fixed and doubly immunostained for TMAP/CKAP2 (green) and α-tubulin (red). Representative images of cells at different stages of mitosis are shown.

    Techniques Used:

    Overexpression of TMAP/CKAP2 results in formation of spindle abnormalities due to a defect in centrosome separation. (A) Quantitative analysis of the percentage of mitotic cells with abnormal spindles among GFP- or GFP-CKAP2-expressing HEK 293A. HEK 293
    Figure Legend Snippet: Overexpression of TMAP/CKAP2 results in formation of spindle abnormalities due to a defect in centrosome separation. (A) Quantitative analysis of the percentage of mitotic cells with abnormal spindles among GFP- or GFP-CKAP2-expressing HEK 293A. HEK 293

    Techniques Used: Over Expression, Expressing

    Fate of TMAP/CKAP2-overexpressing cells developing spindle defects. HEK 293 cells transfected with GFP-CKAP2 were observed for 48 h using a time-lapse video microscope as described in Materials and Methods. (A) A total of 38 individual GFP-CKAP2-positive
    Figure Legend Snippet: Fate of TMAP/CKAP2-overexpressing cells developing spindle defects. HEK 293 cells transfected with GFP-CKAP2 were observed for 48 h using a time-lapse video microscope as described in Materials and Methods. (A) A total of 38 individual GFP-CKAP2-positive

    Techniques Used: Transfection, Microscopy

    Degradation of TMAP/CKAP2 is mediated by the KEN box destruction motif located near the N terminus. (A) Degradability of deletion mutants of TMAP/CKAP2 during mitotic exit. HeLa cells transfected with the myc-tagged full-length or indicated deletion mutants
    Figure Legend Snippet: Degradation of TMAP/CKAP2 is mediated by the KEN box destruction motif located near the N terminus. (A) Degradability of deletion mutants of TMAP/CKAP2 during mitotic exit. HeLa cells transfected with the myc-tagged full-length or indicated deletion mutants

    Techniques Used: Transfection

    7) Product Images from "Mitogen-Activated Protein Kinase Cascade MKK7-MPK6 Plays Important Roles in Plant Development and Regulates Shoot Branching by Phosphorylating PIN1 in Arabidopsis"

    Article Title: Mitogen-Activated Protein Kinase Cascade MKK7-MPK6 Plays Important Roles in Plant Development and Regulates Shoot Branching by Phosphorylating PIN1 in Arabidopsis

    Journal: PLoS Biology

    doi: 10.1371/journal.pbio.1002550

    MKK7 can phosphorylate MPK3 and MPK6 in vitro and in vivo. (A) In vitro kinase assays of phosphorylation of MPK3 and MPK6 by constitutively activated MKK7 (cMKK7). The cMKK7 was incubated with MPK3 or MPK6 in the kinase reaction buffer. Aliquots of the samples were separated by SDS-PAGE and subjected to autoradiography. Arrows indicate positions of the detected proteins. (B) Phosphorylation of MPK3 and MPK6 in planta . Samples were prepared from 21-d-old seedlings and subjected to immunoblot analysis with antiphospho-p44/p42 antibody. The Ponceau-stained western blot was used as the loading control.
    Figure Legend Snippet: MKK7 can phosphorylate MPK3 and MPK6 in vitro and in vivo. (A) In vitro kinase assays of phosphorylation of MPK3 and MPK6 by constitutively activated MKK7 (cMKK7). The cMKK7 was incubated with MPK3 or MPK6 in the kinase reaction buffer. Aliquots of the samples were separated by SDS-PAGE and subjected to autoradiography. Arrows indicate positions of the detected proteins. (B) Phosphorylation of MPK3 and MPK6 in planta . Samples were prepared from 21-d-old seedlings and subjected to immunoblot analysis with antiphospho-p44/p42 antibody. The Ponceau-stained western blot was used as the loading control.

    Techniques Used: In Vitro, In Vivo, Incubation, SDS Page, Autoradiography, Staining, Western Blot

    8) Product Images from "Effect and mechanism of the aβ2-GP I/rhβ2-GP I complex on JEG-3 cell proliferation, migration and invasion"

    Article Title: Effect and mechanism of the aβ2-GP I/rhβ2-GP I complex on JEG-3 cell proliferation, migration and invasion

    Journal: Molecular Medicine Reports

    doi: 10.3892/mmr.2018.8822

    Effects of aβ2-GP I/rhβ2-GP I complexes on JEG-3 cell proliferation. (A) Cell proliferation was assessed by CCK-8 assay (n=3). (B) EdU staining for cell proliferation (magnification, ×100) (n=3). Red: EdU stained nuclei of proliferating cells; blue: All nuclei counterstained with Hoechst (all reagents were from EdU labeling kit). The statistical analysis of EdU staining was performed by Image-Pro Plus 6.0 software. (C) Cell cycle was analyzed by flow cytometry following 24-h incubations. Statistical analysis of % cell population in each stage of cell cycle was performed. IgG, rhβ2-GP I, aβ2-GP I and IgG/rhβ2-GP I were regarded as controls. *P
    Figure Legend Snippet: Effects of aβ2-GP I/rhβ2-GP I complexes on JEG-3 cell proliferation. (A) Cell proliferation was assessed by CCK-8 assay (n=3). (B) EdU staining for cell proliferation (magnification, ×100) (n=3). Red: EdU stained nuclei of proliferating cells; blue: All nuclei counterstained with Hoechst (all reagents were from EdU labeling kit). The statistical analysis of EdU staining was performed by Image-Pro Plus 6.0 software. (C) Cell cycle was analyzed by flow cytometry following 24-h incubations. Statistical analysis of % cell population in each stage of cell cycle was performed. IgG, rhβ2-GP I, aβ2-GP I and IgG/rhβ2-GP I were regarded as controls. *P

    Techniques Used: CCK-8 Assay, Staining, Labeling, Software, Flow Cytometry, Cytometry

    Prokaryotic expression and purification of rhβ2-GP I. (A) The prokaryotic expression fusion protein rhβ2-GP I was identified following 2, 4, 6 h of extension incubation of transfected E. coli BL21 (DE3) cells with 0.1 mM IPTG and bacterium lysate was detected by SDS-PAGE and Coomassie staining, as indicated by the arrow. (B) The fusion protein with His-tag was successfully purified by Ni-NTA chelating agarose and detected by SDS-PAGE and Coomassie staining. Furthermore, the purified protein was detected by western blotting with anti-His antibody and was employed to detected the His-tagged protein (far right). IPTG, isopropyl β-D-1-thiogalactopyranoside; aβ2-GP I, anti-β2-glycoprotein; rh, human recombinant.
    Figure Legend Snippet: Prokaryotic expression and purification of rhβ2-GP I. (A) The prokaryotic expression fusion protein rhβ2-GP I was identified following 2, 4, 6 h of extension incubation of transfected E. coli BL21 (DE3) cells with 0.1 mM IPTG and bacterium lysate was detected by SDS-PAGE and Coomassie staining, as indicated by the arrow. (B) The fusion protein with His-tag was successfully purified by Ni-NTA chelating agarose and detected by SDS-PAGE and Coomassie staining. Furthermore, the purified protein was detected by western blotting with anti-His antibody and was employed to detected the His-tagged protein (far right). IPTG, isopropyl β-D-1-thiogalactopyranoside; aβ2-GP I, anti-β2-glycoprotein; rh, human recombinant.

    Techniques Used: Expressing, Purification, Incubation, Transfection, SDS Page, Staining, Western Blot, Recombinant

    aβ2-GP I/rhβ2-GP I complex induces the activity of NF-κB in JEG-3 cells. (A) Relative mRNA expressions of MyD88, IKKβ, NF-κB and IκBα in JEG-3 cell line. (B) The protein level of MyD88, IκBα and p-IκBα in stimulated JEG-3 cells detected by western blotting. The data statistics of western blot test was performed by Image-Pro Plus 6.0 software. (C) Luciferase activity was measured to assess NF-κB expression. IgG, rhβ2-GP I, aβ2-GP I and IgG/rhβ2-GPI were regarded as controls. *P
    Figure Legend Snippet: aβ2-GP I/rhβ2-GP I complex induces the activity of NF-κB in JEG-3 cells. (A) Relative mRNA expressions of MyD88, IKKβ, NF-κB and IκBα in JEG-3 cell line. (B) The protein level of MyD88, IκBα and p-IκBα in stimulated JEG-3 cells detected by western blotting. The data statistics of western blot test was performed by Image-Pro Plus 6.0 software. (C) Luciferase activity was measured to assess NF-κB expression. IgG, rhβ2-GP I, aβ2-GP I and IgG/rhβ2-GPI were regarded as controls. *P

    Techniques Used: Activity Assay, Western Blot, Software, Luciferase, Expressing

    Effects of the aβ2-GP I/rhβ2-GP I complex on JEG-3 cell migration and invasion, and protein expression levels of tumor metastasis- and diffusion-associated factors. (A and B) Cell migration measured by transwell assay (magnification, ×200). Statistical analysis of the results of the transwell assay was performed using Image-Pro Plus 6.0 software. (C and D) Protein levels of N-cadherin, E-cadherin and γ-caterin were detected by western blotting. Statistical analysis was performed by Image-Pro Plus 6.0 software. IgG, rhβ2-GP I, aβ2-GPIand IgG/rhβ2-GP I were regarded as controls. *P
    Figure Legend Snippet: Effects of the aβ2-GP I/rhβ2-GP I complex on JEG-3 cell migration and invasion, and protein expression levels of tumor metastasis- and diffusion-associated factors. (A and B) Cell migration measured by transwell assay (magnification, ×200). Statistical analysis of the results of the transwell assay was performed using Image-Pro Plus 6.0 software. (C and D) Protein levels of N-cadherin, E-cadherin and γ-caterin were detected by western blotting. Statistical analysis was performed by Image-Pro Plus 6.0 software. IgG, rhβ2-GP I, aβ2-GPIand IgG/rhβ2-GP I were regarded as controls. *P

    Techniques Used: Migration, Expressing, Diffusion-based Assay, Transwell Assay, Software, Western Blot

    9) Product Images from "Effect and mechanism of the aβ2-GP I/rhβ2-GP I complex on JEG-3 cell proliferation, migration and invasion"

    Article Title: Effect and mechanism of the aβ2-GP I/rhβ2-GP I complex on JEG-3 cell proliferation, migration and invasion

    Journal: Molecular Medicine Reports

    doi: 10.3892/mmr.2018.8822

    Prokaryotic expression and purification of rhβ2-GP I. (A) The prokaryotic expression fusion protein rhβ2-GP I was identified following 2, 4, 6 h of extension incubation of transfected E. coli BL21 (DE3) cells with 0.1 mM IPTG and bacterium lysate was detected by SDS-PAGE and Coomassie staining, as indicated by the arrow. (B) The fusion protein with His-tag was successfully purified by Ni-NTA chelating agarose and detected by SDS-PAGE and Coomassie staining. Furthermore, the purified protein was detected by western blotting with anti-His antibody and was employed to detected the His-tagged protein (far right). IPTG, isopropyl β-D-1-thiogalactopyranoside; aβ2-GP I, anti-β2-glycoprotein; rh, human recombinant.
    Figure Legend Snippet: Prokaryotic expression and purification of rhβ2-GP I. (A) The prokaryotic expression fusion protein rhβ2-GP I was identified following 2, 4, 6 h of extension incubation of transfected E. coli BL21 (DE3) cells with 0.1 mM IPTG and bacterium lysate was detected by SDS-PAGE and Coomassie staining, as indicated by the arrow. (B) The fusion protein with His-tag was successfully purified by Ni-NTA chelating agarose and detected by SDS-PAGE and Coomassie staining. Furthermore, the purified protein was detected by western blotting with anti-His antibody and was employed to detected the His-tagged protein (far right). IPTG, isopropyl β-D-1-thiogalactopyranoside; aβ2-GP I, anti-β2-glycoprotein; rh, human recombinant.

    Techniques Used: Expressing, Purification, Incubation, Transfection, SDS Page, Staining, Western Blot, Recombinant

    Related Articles

    Transfection:

    Article Title: NF-kappaB Mediated Transcriptional Repression of Acid Modifying Hormone Gastrin
    Article Snippet: .. Twenty-four hr after transfection, AGS cells were incubated with 150 µM of nemo binding inhibitory peptide (NBD) (Calbiochem-Novabiochem, San Diego, USA) for additional 24 hr and harvested for luciferase assay. .. AGS cells transfected with 240 Gas-Luc were treated with Trichostatin A (Calbiochem-Novabiochem, SanDiego, CA), a histone deactylase inhibitor, at 100 nM for 48 hr and harvested for further experiments.

    Luciferase:

    Article Title: NF-kappaB Mediated Transcriptional Repression of Acid Modifying Hormone Gastrin
    Article Snippet: .. Twenty-four hr after transfection, AGS cells were incubated with 150 µM of nemo binding inhibitory peptide (NBD) (Calbiochem-Novabiochem, San Diego, USA) for additional 24 hr and harvested for luciferase assay. .. AGS cells transfected with 240 Gas-Luc were treated with Trichostatin A (Calbiochem-Novabiochem, SanDiego, CA), a histone deactylase inhibitor, at 100 nM for 48 hr and harvested for further experiments.

    Aqueous Normal-phase Chromatography:

    Article Title: Cinnamyl alcohol attenuates vasoconstriction by activation of K+ channels via NO-cGMP-protein kinase G pathway and inhibition of Rho-kinase
    Article Snippet: .. Cinnamyl alcohol (CAL), phenylephrine (PE), acetylcholine, 1 H-[1,2,4]-oxadiazolole-[4,3-a] quinoxalin-10one (ODQ) and atrial natriuretic peptide (ANP) were purchased from Sigma-Aldrich (St. Louis, MO). .. NG -nitro-L -arginine methyl ester (L -NAME), methylene blue (MB), glibenclamide (Gli) and calpeptin were purchased from Calbiochem (San Diego, CA).

    Immunoprecipitation:

    Article Title: The deubiquitylating enzyme UCHL3 regulates Ku80 retention at sites of DNA damage
    Article Snippet: .. The beads were washed six times with CSK buffer containing 300 mM NaCl and bound proteins were eluted by boiling at 95 °C for 10 min with 1 x Laemmli SDS buffer for GFP-Trap_MA or incubating with 500 μg/ml FLAG peptide (Sigma-Aldrich) for 30 min on ice for samples where anti-FLAG antibody was used for immunoprecipitation. .. For the detection of ubiquitylated proteins in in vivo ubiquitylation assays, beads were washed twice with IP lysis buffer containing 300 mM NaCl, three times with same buffer containing 1 M NaCl and once with the original buffer, followed by elution as described above.

    Article Title: Phosphorylation of Eukaryotic Elongation Factor 2 (eEF2) by Cyclin A-Cyclin-Dependent Kinase 2 Regulates Its Inhibition by eEF2 Kinase
    Article Snippet: .. FLAG-eEF2 was immunoprecipitated with M2-agarose (Sigma), washed in lysis and elution buffers, eluted with FLAG peptide (Sigma), and concentrated (Amicon centrifugal filter unit; 50-kDa cutoff). eEF2K assays were performed in eEF2K cocktail (150 nM [γ-32 P]ATP, 0.2 μg eEF2K, eEF2K buffer, 50 U calmodulin), and reaction mixtures were incubated at 30°C for 10 min as described previously ( ). .. For sequential cyclin A-CDK2–eEF2K reactions, 1 μg eluted FLAG-eEF2 (or FLAG-eEF2 S595A) was phosphorylated by 0.375 μl cyclin A-CDK2 (high efficiency; gift of T. Barshevsky, NEB) immobilized on anti-CDK2 antibody-bound Sepharose beads in kinase buffer containing 250 μM ATP.

    Incubation:

    Article Title: NF-kappaB Mediated Transcriptional Repression of Acid Modifying Hormone Gastrin
    Article Snippet: .. Twenty-four hr after transfection, AGS cells were incubated with 150 µM of nemo binding inhibitory peptide (NBD) (Calbiochem-Novabiochem, San Diego, USA) for additional 24 hr and harvested for luciferase assay. .. AGS cells transfected with 240 Gas-Luc were treated with Trichostatin A (Calbiochem-Novabiochem, SanDiego, CA), a histone deactylase inhibitor, at 100 nM for 48 hr and harvested for further experiments.

    Article Title: Phosphorylation of Eukaryotic Elongation Factor 2 (eEF2) by Cyclin A-Cyclin-Dependent Kinase 2 Regulates Its Inhibition by eEF2 Kinase
    Article Snippet: .. FLAG-eEF2 was immunoprecipitated with M2-agarose (Sigma), washed in lysis and elution buffers, eluted with FLAG peptide (Sigma), and concentrated (Amicon centrifugal filter unit; 50-kDa cutoff). eEF2K assays were performed in eEF2K cocktail (150 nM [γ-32 P]ATP, 0.2 μg eEF2K, eEF2K buffer, 50 U calmodulin), and reaction mixtures were incubated at 30°C for 10 min as described previously ( ). .. For sequential cyclin A-CDK2–eEF2K reactions, 1 μg eluted FLAG-eEF2 (or FLAG-eEF2 S595A) was phosphorylated by 0.375 μl cyclin A-CDK2 (high efficiency; gift of T. Barshevsky, NEB) immobilized on anti-CDK2 antibody-bound Sepharose beads in kinase buffer containing 250 μM ATP.

    other:

    Article Title: Survivin Is a Transcriptional Target of STAT3 Critical to Estradiol Neuroprotection in Global Ischemia
    Article Snippet: Both the ischemia- and estradiol-induced increases in survivin were reversed by the STAT3 inhibitor peptide.

    Article Title: Survivin Is a Transcriptional Target of STAT3 Critical to Estradiol Neuroprotection in Global Ischemia
    Article Snippet: STAT3 inhibitor peptide markedly attenuated estradiol neuroprotection in animals subjected to global ischemia ( A–C ), but had little or no effect on neuronal survival in sham-operated animals (data not shown).

    Expressing:

    Article Title: Ribosomal S6 Kinase 2 Directly Phosphorylates the 5-Hydroxytryptamine 2A (5-HT2A) Serotonin Receptor, Thereby Modulating 5-HT2A Signaling
    Article Snippet: .. Briefly, the i3 loop peptide was subcloned (introducing 5′ NdeI and 3′ NheI) into the inducible pET11a expression vector (Novagen, Madison, WI) as a fusion protein located N-terminal to an inducible protein splicing element (intein) attached to a modified chitin binding domain containing a C-terminal hexahistidine affinity tag (IMPACT, New England Biolabs, Inc.). .. Phosphorylation-deficient mutants were constructed as outlined below.

    Modification:

    Article Title: Ribosomal S6 Kinase 2 Directly Phosphorylates the 5-Hydroxytryptamine 2A (5-HT2A) Serotonin Receptor, Thereby Modulating 5-HT2A Signaling
    Article Snippet: .. Briefly, the i3 loop peptide was subcloned (introducing 5′ NdeI and 3′ NheI) into the inducible pET11a expression vector (Novagen, Madison, WI) as a fusion protein located N-terminal to an inducible protein splicing element (intein) attached to a modified chitin binding domain containing a C-terminal hexahistidine affinity tag (IMPACT, New England Biolabs, Inc.). .. Phosphorylation-deficient mutants were constructed as outlined below.

    Lysis:

    Article Title: Phosphorylation of Eukaryotic Elongation Factor 2 (eEF2) by Cyclin A-Cyclin-Dependent Kinase 2 Regulates Its Inhibition by eEF2 Kinase
    Article Snippet: .. FLAG-eEF2 was immunoprecipitated with M2-agarose (Sigma), washed in lysis and elution buffers, eluted with FLAG peptide (Sigma), and concentrated (Amicon centrifugal filter unit; 50-kDa cutoff). eEF2K assays were performed in eEF2K cocktail (150 nM [γ-32 P]ATP, 0.2 μg eEF2K, eEF2K buffer, 50 U calmodulin), and reaction mixtures were incubated at 30°C for 10 min as described previously ( ). .. For sequential cyclin A-CDK2–eEF2K reactions, 1 μg eluted FLAG-eEF2 (or FLAG-eEF2 S595A) was phosphorylated by 0.375 μl cyclin A-CDK2 (high efficiency; gift of T. Barshevsky, NEB) immobilized on anti-CDK2 antibody-bound Sepharose beads in kinase buffer containing 250 μM ATP.

    Binding Assay:

    Article Title: NF-kappaB Mediated Transcriptional Repression of Acid Modifying Hormone Gastrin
    Article Snippet: .. Twenty-four hr after transfection, AGS cells were incubated with 150 µM of nemo binding inhibitory peptide (NBD) (Calbiochem-Novabiochem, San Diego, USA) for additional 24 hr and harvested for luciferase assay. .. AGS cells transfected with 240 Gas-Luc were treated with Trichostatin A (Calbiochem-Novabiochem, SanDiego, CA), a histone deactylase inhibitor, at 100 nM for 48 hr and harvested for further experiments.

    Article Title: Ribosomal S6 Kinase 2 Directly Phosphorylates the 5-Hydroxytryptamine 2A (5-HT2A) Serotonin Receptor, Thereby Modulating 5-HT2A Signaling
    Article Snippet: .. Briefly, the i3 loop peptide was subcloned (introducing 5′ NdeI and 3′ NheI) into the inducible pET11a expression vector (Novagen, Madison, WI) as a fusion protein located N-terminal to an inducible protein splicing element (intein) attached to a modified chitin binding domain containing a C-terminal hexahistidine affinity tag (IMPACT, New England Biolabs, Inc.). .. Phosphorylation-deficient mutants were constructed as outlined below.

    Plasmid Preparation:

    Article Title: Ribosomal S6 Kinase 2 Directly Phosphorylates the 5-Hydroxytryptamine 2A (5-HT2A) Serotonin Receptor, Thereby Modulating 5-HT2A Signaling
    Article Snippet: .. Briefly, the i3 loop peptide was subcloned (introducing 5′ NdeI and 3′ NheI) into the inducible pET11a expression vector (Novagen, Madison, WI) as a fusion protein located N-terminal to an inducible protein splicing element (intein) attached to a modified chitin binding domain containing a C-terminal hexahistidine affinity tag (IMPACT, New England Biolabs, Inc.). .. Phosphorylation-deficient mutants were constructed as outlined below.

    Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 86
    Millipore 42a 44a
    42a 44a, supplied by Millipore, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/42a 44a/product/Millipore
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    42a 44a - by Bioz Stars, 2020-09
    86/100 stars
      Buy from Supplier

    Image Search Results