Review



rabbit polyclonal anti s100a11 antibody  (Proteintech)


Bioz Verified Symbol Proteintech is a verified supplier  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 94

    Structured Review

    Proteintech rabbit polyclonal anti s100a11 antibody
    Rabbit Polyclonal Anti S100a11 Antibody, supplied by Proteintech, used in various techniques. Bioz Stars score: 94/100, based on 25 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rabbit+polyclonal+anti+s100a11/Neuropeptide+Y+Antibody/pm41933371-75-2-6
    Average 94 stars, based on 25 article reviews
    rabbit polyclonal anti s100a11 antibody - by Bioz Stars, 2026-10
    94/100 stars

    Images

    Related Articles

    Incubation:

    Article Title: Inhibiting NF-κB-S100A11 signaling and targeting S100A11 for anticancer effects of demethylzeylasteral in human colon cancer.
    Article Snippet: .. The primary antibodies used included rabbit monoclonal anti-cleaved caspase 3 (#9664, CST, 1:1000), rabbit polyclonal anti-Bax (50599–2-Ig, Proteintech, 1:1000), rabbit polyclonal anti-Bcl2 (12789–1-AP, Proteintech, 1:1000), rabbit monoclonal anti-NF-κB (# 8242 S, CST, 1:1000), rabbit polyclonal anti-β-actin (81115–1-RR, Proteintech, 1:1000), and rabbit polyclonal anti-S100A11 (10237–1-AP, Proteintech, 1:1000), which were incubated overnight at 4 ◦C. ..

    other:

    Article Title: CHIP-dependent regulation of the actin cytoskeleton is linked to neuronal cell membrane integrity
    Article Snippet: Rabbit polyclonal anti-S100A11 , Proteintech , 10237-1-ap; RRID: AB_2183478.



    Similar Products

    94
    Proteintech rabbit polyclonal anti s100a11 antibody
    Rabbit Polyclonal Anti S100a11 Antibody, supplied by Proteintech, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rabbit+polyclonal+anti+s100a11/Neuropeptide+Y+Antibody/pm41933371-75-2-6
    Average 94 stars, based on 1 article reviews
    rabbit polyclonal anti s100a11 antibody - by Bioz Stars, 2026-10
    94/100 stars
      Buy from Supplier

    94
    Proteintech rabbit anti human s100a11 polyclonal antibody
    Annexin A2 can bind with plasminogen by fashioning a complex with <t>S100A11.</t> (A) Endogenous lysyl oxidase-like 4 (LOXL4), annexin A2, and S100A11 proteins in the indicated cell lines were detected using the Western blotting (WB) procedure. The running gel was also stained with Coomassie brilliant blue (CBB) as a sample control of proper loading. (B) We evaluated the invasion ability of MDA-MB-231 cells after the treatment with or without tranexamic acid (TXA) (1 mg/mL). (C) HEK293T cells were co-transfected with HA-tagged S100A11 and Myc-tagged ANXA2. After precipitation of the expressed products with the beads, bound foreign proteins were analyzed by WB using the HA or Myc antibody. (D) Prepared recombinant proteins (GST, GST-ANXA2, S100A10, and S100A11) from the Escherichia coli expression system were checked for their purity. (E) Paired blots of the indicated proteins [GST, GST-annexin A2, and S100A10 (upper) or S100A11 (lower)] were dot-blotted onto the nitrocellulose filter membranes in a duplicate manner. The blotted membranes were then incubated with either biotinylated plasminogen (bio-PLG) alone or a blend of bio-PLG and S100A10 (upper) or S100A11 (lower). After incubation was completed, the bound proteins were detected by anti-S100A10 or anti-S100A11 (left) or streptavidin–horseradish peroxidase (HRP) (right). (F) The schematic diagram resumed the results from panel (E) The red or blue circles correspond to those highlighted in the results in panel (E) Data from panel (B) are means ± SD, ***p < 0.001. The individual symbols (*)mean exploit of preparations of the purified recombinant proteins as their predicted sizes.
    Rabbit Anti Human S100a11 Polyclonal Antibody, supplied by Proteintech, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rabbit+polyclonal+anti+s100a11/S100A11+Antibody/pmc11002074-67-13-21
    Average 94 stars, based on 1 article reviews
    rabbit anti human s100a11 polyclonal antibody - by Bioz Stars, 2026-10
    94/100 stars
      Buy from Supplier

    94
    Proteintech rabbit polyclonal anti s100a11 antibodies
    Fig. 1. Potential targets of Demethylzeylasteral against colon cancer. (A) A differential gene expression volcano map was generated. (B) KEGG pathway enrichment analysis of the differential genes revealed the calcium ion signaling pathway (marked by the red box) as a significant pathway. (C) <t>S100A11</t> was identified as a candidate target for demethylzeylasteral in treating colon cancer.
    Rabbit Polyclonal Anti S100a11 Antibodies, supplied by Proteintech, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rabbit+polyclonal+anti+s100a11/S100A11+Antibody/pm37879212-68-24-29
    Average 94 stars, based on 1 article reviews
    rabbit polyclonal anti s100a11 antibodies - by Bioz Stars, 2026-10
    94/100 stars
      Buy from Supplier

    94
    Proteintech rabbit polyclonal anti β actin
    Fig. 1. Potential targets of Demethylzeylasteral against colon cancer. (A) A differential gene expression volcano map was generated. (B) KEGG pathway enrichment analysis of the differential genes revealed the calcium ion signaling pathway (marked by the red box) as a significant pathway. (C) <t>S100A11</t> was identified as a candidate target for demethylzeylasteral in treating colon cancer.
    Rabbit Polyclonal Anti β Actin, supplied by Proteintech, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rabbit+polyclonal+anti+s100a11/S100A11+Antibody/pm37879212-71-33-37
    Average 94 stars, based on 1 article reviews
    rabbit polyclonal anti β actin - by Bioz Stars, 2026-10
    94/100 stars
      Buy from Supplier

    94
    Proteintech rabbit polyclonal anti s100a11
    Fig. 1. Potential targets of Demethylzeylasteral against colon cancer. (A) A differential gene expression volcano map was generated. (B) KEGG pathway enrichment analysis of the differential genes revealed the calcium ion signaling pathway (marked by the red box) as a significant pathway. (C) <t>S100A11</t> was identified as a candidate target for demethylzeylasteral in treating colon cancer.
    Rabbit Polyclonal Anti S100a11, supplied by Proteintech, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rabbit+polyclonal+anti+s100a11/S100A11+Antibody/pm37879212-71-40-44
    Average 94 stars, based on 1 article reviews
    rabbit polyclonal anti s100a11 - by Bioz Stars, 2026-10
    94/100 stars
      Buy from Supplier

    94
    Proteintech rabbit polyclonal s100 a11
    Differentially expressed proteins of HuCCA-1 following apigenin treatment.
    Rabbit Polyclonal S100 A11, supplied by Proteintech, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rabbit+polyclonal+anti+s100a11/S100A11+Antibody/pmc05604180-165-101-109
    Average 94 stars, based on 1 article reviews
    rabbit polyclonal s100 a11 - by Bioz Stars, 2026-10
    94/100 stars
      Buy from Supplier

    94
    Proteintech polyclonal rabbit s100a11 antibodies
    <t>S100A11</t> protein in rheumatoid arthritis (RA) and osteoarthritis (OA) synovial tissue assessed by immunohistochemical (IHC) analysis. Intensive staining for S100A11 was found in the synovial fibroblasts of the lining layer and within the inflammatory cell infiltrates in the RA synovial tissue ( A1 ). The S100A11 expression was negligible or absent in OA synovium ( B1 ). Mouse IgG was used as an isotype control ( A2 , B2 ). Representative images of IHC staining are shown at × 200 magnification. For the detailed view the × 400 magnification is shown ( n = 6 patients with RA and n = 6 patients with OA)
    Polyclonal Rabbit S100a11 Antibodies, supplied by Proteintech, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rabbit+polyclonal+anti+s100a11/S100A11+Antibody/pmc05405489-68-5-9
    Average 94 stars, based on 1 article reviews
    polyclonal rabbit s100a11 antibodies - by Bioz Stars, 2026-10
    94/100 stars
      Buy from Supplier

    Image Search Results


    Annexin A2 can bind with plasminogen by fashioning a complex with S100A11. (A) Endogenous lysyl oxidase-like 4 (LOXL4), annexin A2, and S100A11 proteins in the indicated cell lines were detected using the Western blotting (WB) procedure. The running gel was also stained with Coomassie brilliant blue (CBB) as a sample control of proper loading. (B) We evaluated the invasion ability of MDA-MB-231 cells after the treatment with or without tranexamic acid (TXA) (1 mg/mL). (C) HEK293T cells were co-transfected with HA-tagged S100A11 and Myc-tagged ANXA2. After precipitation of the expressed products with the beads, bound foreign proteins were analyzed by WB using the HA or Myc antibody. (D) Prepared recombinant proteins (GST, GST-ANXA2, S100A10, and S100A11) from the Escherichia coli expression system were checked for their purity. (E) Paired blots of the indicated proteins [GST, GST-annexin A2, and S100A10 (upper) or S100A11 (lower)] were dot-blotted onto the nitrocellulose filter membranes in a duplicate manner. The blotted membranes were then incubated with either biotinylated plasminogen (bio-PLG) alone or a blend of bio-PLG and S100A10 (upper) or S100A11 (lower). After incubation was completed, the bound proteins were detected by anti-S100A10 or anti-S100A11 (left) or streptavidin–horseradish peroxidase (HRP) (right). (F) The schematic diagram resumed the results from panel (E) The red or blue circles correspond to those highlighted in the results in panel (E) Data from panel (B) are means ± SD, ***p < 0.001. The individual symbols (*)mean exploit of preparations of the purified recombinant proteins as their predicted sizes.

    Journal: Frontiers in Oncology

    Article Title: Lysyl oxidase-like 4 promotes the invasiveness of triple-negative breast cancer cells by orchestrating the invasive machinery formed by annexin A2 and S100A11 on the cell surface

    doi: 10.3389/fonc.2024.1371342

    Figure Lengend Snippet: Annexin A2 can bind with plasminogen by fashioning a complex with S100A11. (A) Endogenous lysyl oxidase-like 4 (LOXL4), annexin A2, and S100A11 proteins in the indicated cell lines were detected using the Western blotting (WB) procedure. The running gel was also stained with Coomassie brilliant blue (CBB) as a sample control of proper loading. (B) We evaluated the invasion ability of MDA-MB-231 cells after the treatment with or without tranexamic acid (TXA) (1 mg/mL). (C) HEK293T cells were co-transfected with HA-tagged S100A11 and Myc-tagged ANXA2. After precipitation of the expressed products with the beads, bound foreign proteins were analyzed by WB using the HA or Myc antibody. (D) Prepared recombinant proteins (GST, GST-ANXA2, S100A10, and S100A11) from the Escherichia coli expression system were checked for their purity. (E) Paired blots of the indicated proteins [GST, GST-annexin A2, and S100A10 (upper) or S100A11 (lower)] were dot-blotted onto the nitrocellulose filter membranes in a duplicate manner. The blotted membranes were then incubated with either biotinylated plasminogen (bio-PLG) alone or a blend of bio-PLG and S100A10 (upper) or S100A11 (lower). After incubation was completed, the bound proteins were detected by anti-S100A10 or anti-S100A11 (left) or streptavidin–horseradish peroxidase (HRP) (right). (F) The schematic diagram resumed the results from panel (E) The red or blue circles correspond to those highlighted in the results in panel (E) Data from panel (B) are means ± SD, ***p < 0.001. The individual symbols (*)mean exploit of preparations of the purified recombinant proteins as their predicted sizes.

    Article Snippet: The live cells grown on the cover glasses were treated with bio-PLG or rabbit anti-human S100A11 polyclonal antibody (1:100 dilution, #10237-1-AP, Proteintech) without fixation for 60 min. After the treated live cells were washed with the conditioned medium, they were fixed with 4% paraformaldehyde (PFA) and stained with the fluorescence-labeled streptavidin (1:200 dilution, #S32356, Thermo Fisher Scientific) or anti-rabbit IgG secondary antibody (goat anti-rabbit IgG [H+L] and the highly cross-adsorbed secondary antibody, Alexa FluorTM 594 or Alexa FluorTM 488; 1:200 dilution, #A11012 or #A21441, Thermo Fisher Scientific).

    Techniques: Western Blot, Staining, Control, Transfection, Recombinant, Expressing, Incubation, Purification

    Co-localization of the cell surface S100A11 with plasminogen. (A) The indicated live cells were treated with biotinylated plasminogen (bio-PLG) or anti-S100A11 antibody to detect the bio-PLG attached to the cell surface or S100A11 intrinsically residing on the cell surface. Representative images (A) are shown, and their signals are quantified. RFUs, relative fluorescent units. (B) The live parental MDA-MB-231 cells were treated with both bio-PLG and anti-S100A11 antibodies, and the bio-PLG and anti-S100A11 antibodies bound to the cell surface together were detected simultaneously by different fluorescence colors. (C) The membrane fractions prepared from the indicated cells were measured for plasmin activities following a chromogenic plasmin assay method. The absence of the membrane fraction (−) was used as a control for calibration of the assessment. (D) Likewise, plasmin activities in the membrane fractions from the parental MDA-MB-231 cells treated with the indicated siRNAs were measured (left). None: MDA-MB-231 cells not treated with any siRNA. The reduced expression of the intrinsic S100A11 was confirmed by Western blotting (WB) (right). Data from panels (A, C, D) are means ± SD. ns: not significant, **p < 0.01, ***p < 0.001.

    Journal: Frontiers in Oncology

    Article Title: Lysyl oxidase-like 4 promotes the invasiveness of triple-negative breast cancer cells by orchestrating the invasive machinery formed by annexin A2 and S100A11 on the cell surface

    doi: 10.3389/fonc.2024.1371342

    Figure Lengend Snippet: Co-localization of the cell surface S100A11 with plasminogen. (A) The indicated live cells were treated with biotinylated plasminogen (bio-PLG) or anti-S100A11 antibody to detect the bio-PLG attached to the cell surface or S100A11 intrinsically residing on the cell surface. Representative images (A) are shown, and their signals are quantified. RFUs, relative fluorescent units. (B) The live parental MDA-MB-231 cells were treated with both bio-PLG and anti-S100A11 antibodies, and the bio-PLG and anti-S100A11 antibodies bound to the cell surface together were detected simultaneously by different fluorescence colors. (C) The membrane fractions prepared from the indicated cells were measured for plasmin activities following a chromogenic plasmin assay method. The absence of the membrane fraction (−) was used as a control for calibration of the assessment. (D) Likewise, plasmin activities in the membrane fractions from the parental MDA-MB-231 cells treated with the indicated siRNAs were measured (left). None: MDA-MB-231 cells not treated with any siRNA. The reduced expression of the intrinsic S100A11 was confirmed by Western blotting (WB) (right). Data from panels (A, C, D) are means ± SD. ns: not significant, **p < 0.01, ***p < 0.001.

    Article Snippet: The live cells grown on the cover glasses were treated with bio-PLG or rabbit anti-human S100A11 polyclonal antibody (1:100 dilution, #10237-1-AP, Proteintech) without fixation for 60 min. After the treated live cells were washed with the conditioned medium, they were fixed with 4% paraformaldehyde (PFA) and stained with the fluorescence-labeled streptavidin (1:200 dilution, #S32356, Thermo Fisher Scientific) or anti-rabbit IgG secondary antibody (goat anti-rabbit IgG [H+L] and the highly cross-adsorbed secondary antibody, Alexa FluorTM 594 or Alexa FluorTM 488; 1:200 dilution, #A11012 or #A21441, Thermo Fisher Scientific).

    Techniques: Fluorescence, Membrane, Control, Expressing, Western Blot

    Transition of plasminogen to active-form plasmin on the cell surface annexin A2/S100A11 complex. (A) Biotinylated plasminogen (bio-PLG) was evaluated for the dose used in its transition reaction to active-form plasmin in MDA-MB-231 cell culture. A treatment duration of 60 min was scheduled. To confirm the ripe plasmin band originating from the added bio-PLG, its reaction stopper tranexamic acid (TXA) (1 mg/mL) was used. (B) The temporal evaluation of the added bio-PLG was performed according to a protocol similar to that described in the former experiment (A) , except for using only 10 µg/mL. (C) The effect of calcium (Ca 2+ , 10 mM) on plasmin and other protease activities was studied. The samples prepared from the cell membrane fractions under non-reducing [dithiothreitol (DTT) (−)] conditions were subjected to gelatin zymography. After running, the gels were soaked in a refolding buffer and then incubated with a reaction buffer with (lower) or without Ca 2+ (upper). (D) Non-triple-negative breast cancer (TNBC) MCF-7 cells and the indicated TNBC cell lines were all treated with bio-PLG at a final concentration of 10 µg/mL for 60 min. The bio-PLG attached to the cell membrane and the manifestation of its active derivative in the individual cell membranes were detected by Western blotting (WB) and zymography. (E) HEK293T cells were co-transfected with HA-tagged full-length or any of several S100A11 variants lacking the C-terminal end (see <xref ref-type= Supplementary Figure 2C ) and Myc-tagged annexin A2. The transfected cells were further treated with bio-PLG (10 µg/mL, 60 min). After fractionation of the membrane compartment from each cell treated, half of the extracts were used for input detection and zymography experiments. The remaining half was subjected to a pull-down procedure using streptavidin-conjugated beads. After precipitation of the samples with the beads, bound proteins were analyzed by WB using streptavidin–horseradish peroxidase (HRP), HA antibody, or Myc antibody. (F) The indicated cells were all treated with bio-PLG (10 µg/mL, 60 min). TGF-β (10 ng/mL, 24 h) stimulation induced intrinsic lysyl oxidase-like 4 (LOXL4) production in the parental MDA-MB-231 cells. After fractionation of the membrane compartment from each cell treated, similar experiments were performed as in panel (E) except for the use of the indicated antibodies to evaluate the endogenous proteins of interest. Cont: non-engineered MDA-MB-231 cells. (G) In vitro , a cell-free reaction was performed to evaluate the effect of annexin A2/S100A11 complex on the emergence of plasmin from inactive plasminogen. The prepared, purified proteins were mixed and incubated according to the formula. After a 30-min reaction at room temperature, the samples were subjected to gelatin zymography. " width="100%" height="100%">

    Journal: Frontiers in Oncology

    Article Title: Lysyl oxidase-like 4 promotes the invasiveness of triple-negative breast cancer cells by orchestrating the invasive machinery formed by annexin A2 and S100A11 on the cell surface

    doi: 10.3389/fonc.2024.1371342

    Figure Lengend Snippet: Transition of plasminogen to active-form plasmin on the cell surface annexin A2/S100A11 complex. (A) Biotinylated plasminogen (bio-PLG) was evaluated for the dose used in its transition reaction to active-form plasmin in MDA-MB-231 cell culture. A treatment duration of 60 min was scheduled. To confirm the ripe plasmin band originating from the added bio-PLG, its reaction stopper tranexamic acid (TXA) (1 mg/mL) was used. (B) The temporal evaluation of the added bio-PLG was performed according to a protocol similar to that described in the former experiment (A) , except for using only 10 µg/mL. (C) The effect of calcium (Ca 2+ , 10 mM) on plasmin and other protease activities was studied. The samples prepared from the cell membrane fractions under non-reducing [dithiothreitol (DTT) (−)] conditions were subjected to gelatin zymography. After running, the gels were soaked in a refolding buffer and then incubated with a reaction buffer with (lower) or without Ca 2+ (upper). (D) Non-triple-negative breast cancer (TNBC) MCF-7 cells and the indicated TNBC cell lines were all treated with bio-PLG at a final concentration of 10 µg/mL for 60 min. The bio-PLG attached to the cell membrane and the manifestation of its active derivative in the individual cell membranes were detected by Western blotting (WB) and zymography. (E) HEK293T cells were co-transfected with HA-tagged full-length or any of several S100A11 variants lacking the C-terminal end (see Supplementary Figure 2C ) and Myc-tagged annexin A2. The transfected cells were further treated with bio-PLG (10 µg/mL, 60 min). After fractionation of the membrane compartment from each cell treated, half of the extracts were used for input detection and zymography experiments. The remaining half was subjected to a pull-down procedure using streptavidin-conjugated beads. After precipitation of the samples with the beads, bound proteins were analyzed by WB using streptavidin–horseradish peroxidase (HRP), HA antibody, or Myc antibody. (F) The indicated cells were all treated with bio-PLG (10 µg/mL, 60 min). TGF-β (10 ng/mL, 24 h) stimulation induced intrinsic lysyl oxidase-like 4 (LOXL4) production in the parental MDA-MB-231 cells. After fractionation of the membrane compartment from each cell treated, similar experiments were performed as in panel (E) except for the use of the indicated antibodies to evaluate the endogenous proteins of interest. Cont: non-engineered MDA-MB-231 cells. (G) In vitro , a cell-free reaction was performed to evaluate the effect of annexin A2/S100A11 complex on the emergence of plasmin from inactive plasminogen. The prepared, purified proteins were mixed and incubated according to the formula. After a 30-min reaction at room temperature, the samples were subjected to gelatin zymography.

    Article Snippet: The live cells grown on the cover glasses were treated with bio-PLG or rabbit anti-human S100A11 polyclonal antibody (1:100 dilution, #10237-1-AP, Proteintech) without fixation for 60 min. After the treated live cells were washed with the conditioned medium, they were fixed with 4% paraformaldehyde (PFA) and stained with the fluorescence-labeled streptavidin (1:200 dilution, #S32356, Thermo Fisher Scientific) or anti-rabbit IgG secondary antibody (goat anti-rabbit IgG [H+L] and the highly cross-adsorbed secondary antibody, Alexa FluorTM 594 or Alexa FluorTM 488; 1:200 dilution, #A11012 or #A21441, Thermo Fisher Scientific).

    Techniques: Cell Culture, Membrane, Zymography, Incubation, Concentration Assay, Western Blot, Transfection, Fractionation, In Vitro, Purification

    Fig. 1. Potential targets of Demethylzeylasteral against colon cancer. (A) A differential gene expression volcano map was generated. (B) KEGG pathway enrichment analysis of the differential genes revealed the calcium ion signaling pathway (marked by the red box) as a significant pathway. (C) S100A11 was identified as a candidate target for demethylzeylasteral in treating colon cancer.

    Journal: Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie

    Article Title: Inhibiting NF-κB-S100A11 signaling and targeting S100A11 for anticancer effects of demethylzeylasteral in human colon cancer.

    doi: 10.1016/j.biopha.2023.115725

    Figure Lengend Snippet: Fig. 1. Potential targets of Demethylzeylasteral against colon cancer. (A) A differential gene expression volcano map was generated. (B) KEGG pathway enrichment analysis of the differential genes revealed the calcium ion signaling pathway (marked by the red box) as a significant pathway. (C) S100A11 was identified as a candidate target for demethylzeylasteral in treating colon cancer.

    Article Snippet: The cells were fixed with 4 % paraformaldehyde and blocked with a 5 % BSA solution for 1 h, followed by incubation with primary rabbit polyclonal anti-S100A11 antibodies (10237–1-AP, Proteintech, 1:100) overnight at 4 °C, and then with goat anti-rabbit AF546 (A11035, Invitrogen, 1:1000) at room temperature for 2 h. For immunohistochemical staining, some tumor tissues were treated with high temperature and high pressure to retrieve the antigen before being embedded in paraffin and cut into pathological sections of 5 μm.

    Techniques: Gene Expression, Generated

    Fig. 2. Demethylzeylasteral inhibits HT29 cell proliferation by targeting S100A11. (A) CCK8 assay was used to detect the inhibitory effect of demethylzeylasteral on HT29 cell. (B) CCK8 assay showed that demethylzeylasteral had an inhibitory effect on HT29 cells overexpressing the S100A11 gene, with statistical significance (* P < 0.05, ** P < 0.001, *** P < 0.001) compared to the 0 μM group (n = 3). (C) Tunel staining was used to analyze cell apoptosis at a magnification of 200x. (D) Western blot analysis was performed to detect changes in S100A11 expression in cells. (E) Quantitative analysis of Ki67, Bcl2, Bax, and cleaved caspase3 protein levels was performed using Western blot analysis. (F-J) Quantitative analysis of the corresponding protein expression levels in (D) and (E) is presented, with statistical significance (* P < 0.05, ** P < 0.001, *** P < 0.001) compared to the Control group (n = 3). In the experimental conditions, CD refers to HT29 cells treated with demethylzeylasteral, S100A11 refers to the overexpression of S100A11 gene in HT29 cells, and SD refers to HT29 cells with overexpression of the S100A11 gene and treated with demethylzeylasteral.

    Journal: Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie

    Article Title: Inhibiting NF-κB-S100A11 signaling and targeting S100A11 for anticancer effects of demethylzeylasteral in human colon cancer.

    doi: 10.1016/j.biopha.2023.115725

    Figure Lengend Snippet: Fig. 2. Demethylzeylasteral inhibits HT29 cell proliferation by targeting S100A11. (A) CCK8 assay was used to detect the inhibitory effect of demethylzeylasteral on HT29 cell. (B) CCK8 assay showed that demethylzeylasteral had an inhibitory effect on HT29 cells overexpressing the S100A11 gene, with statistical significance (* P < 0.05, ** P < 0.001, *** P < 0.001) compared to the 0 μM group (n = 3). (C) Tunel staining was used to analyze cell apoptosis at a magnification of 200x. (D) Western blot analysis was performed to detect changes in S100A11 expression in cells. (E) Quantitative analysis of Ki67, Bcl2, Bax, and cleaved caspase3 protein levels was performed using Western blot analysis. (F-J) Quantitative analysis of the corresponding protein expression levels in (D) and (E) is presented, with statistical significance (* P < 0.05, ** P < 0.001, *** P < 0.001) compared to the Control group (n = 3). In the experimental conditions, CD refers to HT29 cells treated with demethylzeylasteral, S100A11 refers to the overexpression of S100A11 gene in HT29 cells, and SD refers to HT29 cells with overexpression of the S100A11 gene and treated with demethylzeylasteral.

    Article Snippet: The cells were fixed with 4 % paraformaldehyde and blocked with a 5 % BSA solution for 1 h, followed by incubation with primary rabbit polyclonal anti-S100A11 antibodies (10237–1-AP, Proteintech, 1:100) overnight at 4 °C, and then with goat anti-rabbit AF546 (A11035, Invitrogen, 1:1000) at room temperature for 2 h. For immunohistochemical staining, some tumor tissues were treated with high temperature and high pressure to retrieve the antigen before being embedded in paraffin and cut into pathological sections of 5 μm.

    Techniques: CCK-8 Assay, TUNEL Assay, Staining, Western Blot, Expressing, Control, Over Expression

    Fig. 3. Demethylzeylasteral inhibits colon cancer in vivo by targeting S100A11. (A) A figure shows tumor growth after demethylzeylasteral treatment of normal colon cancer and colon cancer models overexpressing the S100A11 gene, with n = 6 mice per group. (B) Immunohistochemical staining for Ki67 and Tunel staining for apoptotic cells in tumor tissue, magnified by 200x. (C) Western blot analysis was used to quantify changes in Ki67, Bcl2, Bax, and cleaved caspase 3 protein levels in tumor tissue. (D) Tumor volume was calculated from (A). (E) Tumor weight was calculated from (A). (F-I) A statistical analysis was performed to compare protein expression levels in (C), n = 3, statistical significance (* P < 0.05, ** P < 0.01, *** P < 0.001) compared to the Control group, as well as compared to the CD group (# P < 0.05, ## P < 0.01, ### P < 0.001). In the experimental conditions, C refers to the Control group, CD refers to the normal colon cancer model group receiving demethylzeylasteral treatment, S refers to the colon cancer model group overexpressing the S100A11 gene, and SD refers to the colon cancer model group overexpressing the S100A11 gene and receiving demethylzeylasteral treatment.

    Journal: Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie

    Article Title: Inhibiting NF-κB-S100A11 signaling and targeting S100A11 for anticancer effects of demethylzeylasteral in human colon cancer.

    doi: 10.1016/j.biopha.2023.115725

    Figure Lengend Snippet: Fig. 3. Demethylzeylasteral inhibits colon cancer in vivo by targeting S100A11. (A) A figure shows tumor growth after demethylzeylasteral treatment of normal colon cancer and colon cancer models overexpressing the S100A11 gene, with n = 6 mice per group. (B) Immunohistochemical staining for Ki67 and Tunel staining for apoptotic cells in tumor tissue, magnified by 200x. (C) Western blot analysis was used to quantify changes in Ki67, Bcl2, Bax, and cleaved caspase 3 protein levels in tumor tissue. (D) Tumor volume was calculated from (A). (E) Tumor weight was calculated from (A). (F-I) A statistical analysis was performed to compare protein expression levels in (C), n = 3, statistical significance (* P < 0.05, ** P < 0.01, *** P < 0.001) compared to the Control group, as well as compared to the CD group (# P < 0.05, ## P < 0.01, ### P < 0.001). In the experimental conditions, C refers to the Control group, CD refers to the normal colon cancer model group receiving demethylzeylasteral treatment, S refers to the colon cancer model group overexpressing the S100A11 gene, and SD refers to the colon cancer model group overexpressing the S100A11 gene and receiving demethylzeylasteral treatment.

    Article Snippet: The cells were fixed with 4 % paraformaldehyde and blocked with a 5 % BSA solution for 1 h, followed by incubation with primary rabbit polyclonal anti-S100A11 antibodies (10237–1-AP, Proteintech, 1:100) overnight at 4 °C, and then with goat anti-rabbit AF546 (A11035, Invitrogen, 1:1000) at room temperature for 2 h. For immunohistochemical staining, some tumor tissues were treated with high temperature and high pressure to retrieve the antigen before being embedded in paraffin and cut into pathological sections of 5 μm.

    Techniques: In Vivo, Immunohistochemical staining, Staining, TUNEL Assay, Western Blot, Expressing, Control

    Fig. 4. Demethylzeylasteral inhibits S100A11 expression via the NF-κB pathway. (A) Western blot analysis was used to measure changes in protein levels of S100A11, Bcl2, Bax, and cleaved caspase3 after cells overexpressing NF-κB. (B-F) Statistical analysis the protein expression levels in (A), n = 3, statistical significance indicated as * P < 0.05, * * P < 0.01, * ** P < 0.001 when compared to the Control group, or # P < 0.05, ## P < 0.01, ### P < 0.001 when compared to the DE group. (G) The expression of S100A11, Bcl2, Bax, and cleaved caspase3 was analyzed by Western blotting after knocking down NF-κB expression in cells. (H-L) Statistical analysis the protein expression levels in (G), n = 3, statistical significance indicated as * P < 0.05, * * P < 0.01, * ** P < 0.001 when compared to the Control group, or # P < 0.05, ## P < 0.01, ### P < 0.001 when compared to the DE group. (M) A double Luciferase reporter assay confirmed that NF-κB is a transcription factor that regulates S100A11 expression, n = 3, statistical significance indicated as * P < 0.05, * * P < 0.01, * ** P < 0.001 when compared to the Control group. In these experiments, DE represents HT29 cells treated with demethylzeylasteral, OV represents HT29 cells overexpressing NF-κB, OV+DE represents HT29 cells overexpressing NF-κB and treated with demethylzeylasteral, KD represents HT29 cells in which NF-κB expression was knocked down, and KD+DE represents HT29 cells in which NF-κB expression was knocked down and treated with demethylzeylasteral. PS represents intracellular expression of the S100A11 promoter, and PS+NF-κB indicates co-expression of the S100A11 promoter and NF-κB in cells. PS Mut represents intracellular expression of a mutated S100A11 promoter, and PS Mut+NF-κB indicates co-expression of the mutated S100A11 promoter and NF-κB in cells.

    Journal: Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie

    Article Title: Inhibiting NF-κB-S100A11 signaling and targeting S100A11 for anticancer effects of demethylzeylasteral in human colon cancer.

    doi: 10.1016/j.biopha.2023.115725

    Figure Lengend Snippet: Fig. 4. Demethylzeylasteral inhibits S100A11 expression via the NF-κB pathway. (A) Western blot analysis was used to measure changes in protein levels of S100A11, Bcl2, Bax, and cleaved caspase3 after cells overexpressing NF-κB. (B-F) Statistical analysis the protein expression levels in (A), n = 3, statistical significance indicated as * P < 0.05, * * P < 0.01, * ** P < 0.001 when compared to the Control group, or # P < 0.05, ## P < 0.01, ### P < 0.001 when compared to the DE group. (G) The expression of S100A11, Bcl2, Bax, and cleaved caspase3 was analyzed by Western blotting after knocking down NF-κB expression in cells. (H-L) Statistical analysis the protein expression levels in (G), n = 3, statistical significance indicated as * P < 0.05, * * P < 0.01, * ** P < 0.001 when compared to the Control group, or # P < 0.05, ## P < 0.01, ### P < 0.001 when compared to the DE group. (M) A double Luciferase reporter assay confirmed that NF-κB is a transcription factor that regulates S100A11 expression, n = 3, statistical significance indicated as * P < 0.05, * * P < 0.01, * ** P < 0.001 when compared to the Control group. In these experiments, DE represents HT29 cells treated with demethylzeylasteral, OV represents HT29 cells overexpressing NF-κB, OV+DE represents HT29 cells overexpressing NF-κB and treated with demethylzeylasteral, KD represents HT29 cells in which NF-κB expression was knocked down, and KD+DE represents HT29 cells in which NF-κB expression was knocked down and treated with demethylzeylasteral. PS represents intracellular expression of the S100A11 promoter, and PS+NF-κB indicates co-expression of the S100A11 promoter and NF-κB in cells. PS Mut represents intracellular expression of a mutated S100A11 promoter, and PS Mut+NF-κB indicates co-expression of the mutated S100A11 promoter and NF-κB in cells.

    Article Snippet: The cells were fixed with 4 % paraformaldehyde and blocked with a 5 % BSA solution for 1 h, followed by incubation with primary rabbit polyclonal anti-S100A11 antibodies (10237–1-AP, Proteintech, 1:100) overnight at 4 °C, and then with goat anti-rabbit AF546 (A11035, Invitrogen, 1:1000) at room temperature for 2 h. For immunohistochemical staining, some tumor tissues were treated with high temperature and high pressure to retrieve the antigen before being embedded in paraffin and cut into pathological sections of 5 μm.

    Techniques: Expressing, Western Blot, Control, Luciferase, Reporter Assay

    Fig. 5. Demethylzeylasteral directly binds to S100A11 and inhibits S100A11- mediated cell proliferation. (A) SPR analysis shows the interaction between demethylzeylasteral and recombinant S100A11 protein. Demethylzeylasteral was added at different concentrations, and the kinetic values were calculated. (B) The affinity fitting curve between demethylzeylasteral and S100A11 was used to calculate the affinity values. (C) The combination pocket of deme thylzeylasteral and S100A11 was assessed to determine their interaction. (D) The CCK8 assay demonstrated that demethylzeylasteral had a inhibitory effect on HT29 cells overexpressing the mutant S100A11 gene compared to the 0 μM group (n = 3), with statistical significance (* P < 0.05, ** P < 0.001, *** P < 0.001). (E) Immunofluorescence staining was performed to observe the effect of demethylzeylasteral on the expression of S100A11 in cells, with a magnification of 1000 × . (F) Analysis of the intracellular distribution of fluorescent-labeled normal S100A11 protein and mutant S100A11 protein under demethylzeylasteral treatment, with a magnification of 1000 × . (G) Statistical analysis of S100A11 protein expression in (E) showed statistical significance (* P < 0.05, ** P < 0.01, *** P < 0.001) compared to the Control group, as well as compared to the CD group (# P < 0.05, ## P < 0.01, ### P < 0.001). (H) Statistical analysis of S100A11 protein expression in (F) showed statistical significance (* P < 0.05, ** P < 0.01, *** P < 0.001) compared to the SD group. Here,

    Journal: Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie

    Article Title: Inhibiting NF-κB-S100A11 signaling and targeting S100A11 for anticancer effects of demethylzeylasteral in human colon cancer.

    doi: 10.1016/j.biopha.2023.115725

    Figure Lengend Snippet: Fig. 5. Demethylzeylasteral directly binds to S100A11 and inhibits S100A11- mediated cell proliferation. (A) SPR analysis shows the interaction between demethylzeylasteral and recombinant S100A11 protein. Demethylzeylasteral was added at different concentrations, and the kinetic values were calculated. (B) The affinity fitting curve between demethylzeylasteral and S100A11 was used to calculate the affinity values. (C) The combination pocket of deme thylzeylasteral and S100A11 was assessed to determine their interaction. (D) The CCK8 assay demonstrated that demethylzeylasteral had a inhibitory effect on HT29 cells overexpressing the mutant S100A11 gene compared to the 0 μM group (n = 3), with statistical significance (* P < 0.05, ** P < 0.001, *** P < 0.001). (E) Immunofluorescence staining was performed to observe the effect of demethylzeylasteral on the expression of S100A11 in cells, with a magnification of 1000 × . (F) Analysis of the intracellular distribution of fluorescent-labeled normal S100A11 protein and mutant S100A11 protein under demethylzeylasteral treatment, with a magnification of 1000 × . (G) Statistical analysis of S100A11 protein expression in (E) showed statistical significance (* P < 0.05, ** P < 0.01, *** P < 0.001) compared to the Control group, as well as compared to the CD group (# P < 0.05, ## P < 0.01, ### P < 0.001). (H) Statistical analysis of S100A11 protein expression in (F) showed statistical significance (* P < 0.05, ** P < 0.01, *** P < 0.001) compared to the SD group. Here, "C" refers to the Control group, "CD" refers to HT29 cells receiving demethylzeylasteral treatment, "S" refers to HT29 cells overexpressing the S100A11 gene, "SD" refers to HT29 cells overexpressing the S100A11 gene and receiving demethylzeylasteral treatment, and "SMD" refers to HT29 cells overexpressing the mutant S100A11 gene and receiving demethylzeylas teral treatment.

    Article Snippet: The cells were fixed with 4 % paraformaldehyde and blocked with a 5 % BSA solution for 1 h, followed by incubation with primary rabbit polyclonal anti-S100A11 antibodies (10237–1-AP, Proteintech, 1:100) overnight at 4 °C, and then with goat anti-rabbit AF546 (A11035, Invitrogen, 1:1000) at room temperature for 2 h. For immunohistochemical staining, some tumor tissues were treated with high temperature and high pressure to retrieve the antigen before being embedded in paraffin and cut into pathological sections of 5 μm.

    Techniques: Recombinant, CCK-8 Assay, Mutagenesis, Immunofluorescence, Staining, Expressing, Labeling, Control

    Differentially expressed proteins of HuCCA-1 following apigenin treatment.

    Journal: Oncology Letters

    Article Title: Apigenin inhibits growth and induces apoptosis in human cholangiocarcinoma cells

    doi: 10.3892/ol.2017.6705

    Figure Lengend Snippet: Differentially expressed proteins of HuCCA-1 following apigenin treatment.

    Article Snippet: Subsequent to blocking with 5% nonfat dried milk in TBS-Tween 20 (TBST), 10 mM Tris, pH 7.6, 150 mM NaCl, 0.1% Tween 20, at room temperature for 1 h, the membranes were washed with TBST and incubated with the following primary antibodies: Mouse monoclonal cytokeratin 7 (CK7; cat. no. MAB3554; dilution, 1:2,000; Merck KGaA); mouse monoclonal cytokeratin 8 (CK8; cat. no. MAB3414; dilution, 1:2,000; Merck KGaA); mouse monoclonal cytokeratin 18 (CK18; cat. no. MAB3236; dilution, 1:2,000; Merck KGaA); mouse monoclonal cytokeratin 19 (CK19; cat. no. MAB3238; dilution, 1:2,000; Merck KGaA); mouse monoclonal S100-A6 (cat. no. ab55680; dilution, 1:250; Abcam, Cambridge, UK); rabbit polyclonal S100-A11 (cat. no. 10237–1-AP; dilution, 1:250; Proteintech, Chicago, IL, USA); rabbit monoclonal S100-P (cat. no. ab133554; dilution, 1:1,000; Abcam); mouse monoclonal heterogeneous nuclear ribonucleoprotein A2/B1 (hnRNP A2/B1; cat. no. ab6102; dilution, 1:2,000; Abcam); rabbit polyclonal heterogeneous nuclear ribonucleoprotein H (hnRNP H; cat. no. ab10374; dilution, 1:5,000; Abcam); mouse monoclonal annexin A1 (cat. no. MAB3773; dilution, 1:2,000; Merck KGaA); mouse monoclonal annexin A2 (cat. no. ab54771; dilution, 1:20,000; Abcam); rabbit polyclonal annexin A3 (cat. no. ab33068; dilution, 1:2,000; Abcam); mouse monoclonal peroxiredoxin-1 (cat. no. ab58252; dilution, 1:2,000; Abcam); mouse monoclonal prostaglandin E synthase 3 (PTGES3; cat. no. WH0010728M1; dilution, 1:500; Sigma-Aldrich; Merck KGaA); or rabbit monoclonal GAPDH (cat. no. ab75834; dilution, 1:10,000; Abcam) at 4°C overnight.

    Techniques: Transduction

    S100A11 protein in rheumatoid arthritis (RA) and osteoarthritis (OA) synovial tissue assessed by immunohistochemical (IHC) analysis. Intensive staining for S100A11 was found in the synovial fibroblasts of the lining layer and within the inflammatory cell infiltrates in the RA synovial tissue ( A1 ). The S100A11 expression was negligible or absent in OA synovium ( B1 ). Mouse IgG was used as an isotype control ( A2 , B2 ). Representative images of IHC staining are shown at × 200 magnification. For the detailed view the × 400 magnification is shown ( n = 6 patients with RA and n = 6 patients with OA)

    Journal: Arthritis Research & Therapy

    Article Title: Calgizzarin (S100A11): a novel inflammatory mediator associated with disease activity of rheumatoid arthritis

    doi: 10.1186/s13075-017-1288-y

    Figure Lengend Snippet: S100A11 protein in rheumatoid arthritis (RA) and osteoarthritis (OA) synovial tissue assessed by immunohistochemical (IHC) analysis. Intensive staining for S100A11 was found in the synovial fibroblasts of the lining layer and within the inflammatory cell infiltrates in the RA synovial tissue ( A1 ). The S100A11 expression was negligible or absent in OA synovium ( B1 ). Mouse IgG was used as an isotype control ( A2 , B2 ). Representative images of IHC staining are shown at × 200 magnification. For the detailed view the × 400 magnification is shown ( n = 6 patients with RA and n = 6 patients with OA)

    Article Snippet: The slides were immunoprobed with polyclonal rabbit S100A11 antibodies (ProteinTech, Chicago, IL, USA) in a dilution of 1:20.

    Techniques: Immunohistochemical staining, Staining, Expressing, Immunohistochemistry

    Expression of  S100A11  related to different cellular compartments in synovial tissues from patients with rheumatoid arthritis (RA) and osteoarthritis (OA)

    Journal: Arthritis Research & Therapy

    Article Title: Calgizzarin (S100A11): a novel inflammatory mediator associated with disease activity of rheumatoid arthritis

    doi: 10.1186/s13075-017-1288-y

    Figure Lengend Snippet: Expression of S100A11 related to different cellular compartments in synovial tissues from patients with rheumatoid arthritis (RA) and osteoarthritis (OA)

    Article Snippet: The slides were immunoprobed with polyclonal rabbit S100A11 antibodies (ProteinTech, Chicago, IL, USA) in a dilution of 1:20.

    Techniques: Expressing

    Cellular distribution of the S100A11 protein in rheumatoid arthritis synovial tissue. Representative images of immunofluorescence staining ( a ) for CD68 (macrophages), CD20 (B cells), CD3 (T cells) and vimentin (cells of mesenchymal origin) are shown at × 200 magnification ( n = 4). DAPI 4',6-diamidino-2-phenylindole. b Average percentage of S100A11-positive cells presented as mean ± SEM

    Journal: Arthritis Research & Therapy

    Article Title: Calgizzarin (S100A11): a novel inflammatory mediator associated with disease activity of rheumatoid arthritis

    doi: 10.1186/s13075-017-1288-y

    Figure Lengend Snippet: Cellular distribution of the S100A11 protein in rheumatoid arthritis synovial tissue. Representative images of immunofluorescence staining ( a ) for CD68 (macrophages), CD20 (B cells), CD3 (T cells) and vimentin (cells of mesenchymal origin) are shown at × 200 magnification ( n = 4). DAPI 4',6-diamidino-2-phenylindole. b Average percentage of S100A11-positive cells presented as mean ± SEM

    Article Snippet: The slides were immunoprobed with polyclonal rabbit S100A11 antibodies (ProteinTech, Chicago, IL, USA) in a dilution of 1:20.

    Techniques: Immunofluorescence, Staining

    S100A11 in serum and synovial fluid and its association with disease activity in rheumatoid arthritis ( RA ). Levels of S100A11 in the synovial fluid ( a ) but not in the serum ( b ) were up-regulated in patients with RA compared to patients with osteoarthritis ( OA ) when adjusted for age and sex. Levels of S100A11 in synovial fluid correlated with serum C-reactive protein ( CRP ) ( c ), disease activity score in 28 joints ( DAS28 ) ( d ), synovial fluid leukocyte count ( e ), serum anti-cyclic citrullinated peptide antibodies ( anti-CCP ) ( f ), IL-6 ( g ) and IL-8 ( h ). The horizontal line represents the median

    Journal: Arthritis Research & Therapy

    Article Title: Calgizzarin (S100A11): a novel inflammatory mediator associated with disease activity of rheumatoid arthritis

    doi: 10.1186/s13075-017-1288-y

    Figure Lengend Snippet: S100A11 in serum and synovial fluid and its association with disease activity in rheumatoid arthritis ( RA ). Levels of S100A11 in the synovial fluid ( a ) but not in the serum ( b ) were up-regulated in patients with RA compared to patients with osteoarthritis ( OA ) when adjusted for age and sex. Levels of S100A11 in synovial fluid correlated with serum C-reactive protein ( CRP ) ( c ), disease activity score in 28 joints ( DAS28 ) ( d ), synovial fluid leukocyte count ( e ), serum anti-cyclic citrullinated peptide antibodies ( anti-CCP ) ( f ), IL-6 ( g ) and IL-8 ( h ). The horizontal line represents the median

    Article Snippet: The slides were immunoprobed with polyclonal rabbit S100A11 antibodies (ProteinTech, Chicago, IL, USA) in a dilution of 1:20.

    Techniques: Activity Assay

    Synthesis and release of S100A11 by peripheral blood mononuclear cells (PBMCs) and synovial fibroblasts (SFs). PBMCs and SFs from patients with rheumatoid arthritis ( RA ) synthesize ( a , b ) and spontaneously release ( c, d ) higher levels of S100A11 compared to the cells from patients with osteoarthritis ( OA ). Representative images of protein levels of S100A11 in PBMCs and SFs isolated from patients with RA ( n = 4) and patients with OA ( n = 4) by western blot

    Journal: Arthritis Research & Therapy

    Article Title: Calgizzarin (S100A11): a novel inflammatory mediator associated with disease activity of rheumatoid arthritis

    doi: 10.1186/s13075-017-1288-y

    Figure Lengend Snippet: Synthesis and release of S100A11 by peripheral blood mononuclear cells (PBMCs) and synovial fibroblasts (SFs). PBMCs and SFs from patients with rheumatoid arthritis ( RA ) synthesize ( a , b ) and spontaneously release ( c, d ) higher levels of S100A11 compared to the cells from patients with osteoarthritis ( OA ). Representative images of protein levels of S100A11 in PBMCs and SFs isolated from patients with RA ( n = 4) and patients with OA ( n = 4) by western blot

    Article Snippet: The slides were immunoprobed with polyclonal rabbit S100A11 antibodies (ProteinTech, Chicago, IL, USA) in a dilution of 1:20.

    Techniques: Isolation, Western Blot

    Pro-inflammatory role of extracellular S100A11. S100A11 significantly enhances the release of IL-6 ( a ) and TNF-α ( b ) in peripheral blood mononuclear cells and IL-6 ( c ) in synovial fibroblasts (SFs). Levels of TNF-α were not changed in SFs treated with S100A11 protein ( d ). Protein levels in cell culture supernatants were measured after 24 h. The horizontal line represents the median. Ctrl control, LPS lipopolysaccharide

    Journal: Arthritis Research & Therapy

    Article Title: Calgizzarin (S100A11): a novel inflammatory mediator associated with disease activity of rheumatoid arthritis

    doi: 10.1186/s13075-017-1288-y

    Figure Lengend Snippet: Pro-inflammatory role of extracellular S100A11. S100A11 significantly enhances the release of IL-6 ( a ) and TNF-α ( b ) in peripheral blood mononuclear cells and IL-6 ( c ) in synovial fibroblasts (SFs). Levels of TNF-α were not changed in SFs treated with S100A11 protein ( d ). Protein levels in cell culture supernatants were measured after 24 h. The horizontal line represents the median. Ctrl control, LPS lipopolysaccharide

    Article Snippet: The slides were immunoprobed with polyclonal rabbit S100A11 antibodies (ProteinTech, Chicago, IL, USA) in a dilution of 1:20.

    Techniques: Cell Culture