goat anti mouse igg1 cross adsorbed secondary antibody  (Thermo Fisher)


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    Name:
    Goat anti Mouse IgG1 Cross Adsorbed Secondary Antibody
    Description:
    Goat anti Mouse IgG1 Cross Adsorbed Secondary Antibody for Western Blot IF ICC IHC Flow IP
    Catalog Number:
    31236
    Price:
    None
    Category:
    Antibodies Secondary Detection Reagents
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    Structured Review

    Thermo Fisher goat anti mouse igg1 cross adsorbed secondary antibody
    12B2 and 15C2 are specific for nonphospho-S GSK3 in brain lysates of human, mouse, and rat, and both effectively immunoprecipitate GSK3 from cell lysates. (A) Protein sequence alignments for GSK3β (amino acids 1–25) and GSK3α (amino acids 13–37) from human, mouse and rat (Uniprot IDs in parentheses). (B,C) Blots of lysates from human, mouse and rat cortical tissue and GAPDH was used as a loading control (40 μg/lane total protein loaded; experiment repeated three times). (B) 12B2 (red) specifically labeled GSK3β, not GSK3α, in lysates and total GSK3α/β (green) was used to identify both isoforms. (C) 15C2 (red) labeled both GSK3β and GSK3α in lysates and total GSK3α/β (green) was used to identify both isoforms. (D–F) The 12B2 (D) , 15C2 (E) , or control mouse <t>IgG</t> ( F , Ms IgG) were used to immunoprecipitate GSK3 enzymes from HEK293T cell lysates. The starting lysate (Input) was incubated with magnetic beads coated with 12B2 (D) , 15C2 (E) , or Ms IgG control (F) antibodies. 12B2 pulled down only GSK3β (12B2-IP), 15C2 pulled down both GSK3α and β (15C2-IP) and Ms IgG did not pull down GSK3α or β (MsIgG-IP). The post-IP lysates were also run for comparisons to the input samples. These experiments were performed three independent times.
    Goat anti Mouse IgG1 Cross Adsorbed Secondary Antibody for Western Blot IF ICC IHC Flow IP
    https://www.bioz.com/result/goat anti mouse igg1 cross adsorbed secondary antibody/product/Thermo Fisher
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    goat anti mouse igg1 cross adsorbed secondary antibody - by Bioz Stars, 2021-04
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    Images

    1) Product Images from "Novel Non-phosphorylated Serine 9/21 GSK3β/α Antibodies: Expanding the Tools for Studying GSK3 Regulation"

    Article Title: Novel Non-phosphorylated Serine 9/21 GSK3β/α Antibodies: Expanding the Tools for Studying GSK3 Regulation

    Journal: Frontiers in Molecular Neuroscience

    doi: 10.3389/fnmol.2016.00123

    12B2 and 15C2 are specific for nonphospho-S GSK3 in brain lysates of human, mouse, and rat, and both effectively immunoprecipitate GSK3 from cell lysates. (A) Protein sequence alignments for GSK3β (amino acids 1–25) and GSK3α (amino acids 13–37) from human, mouse and rat (Uniprot IDs in parentheses). (B,C) Blots of lysates from human, mouse and rat cortical tissue and GAPDH was used as a loading control (40 μg/lane total protein loaded; experiment repeated three times). (B) 12B2 (red) specifically labeled GSK3β, not GSK3α, in lysates and total GSK3α/β (green) was used to identify both isoforms. (C) 15C2 (red) labeled both GSK3β and GSK3α in lysates and total GSK3α/β (green) was used to identify both isoforms. (D–F) The 12B2 (D) , 15C2 (E) , or control mouse IgG ( F , Ms IgG) were used to immunoprecipitate GSK3 enzymes from HEK293T cell lysates. The starting lysate (Input) was incubated with magnetic beads coated with 12B2 (D) , 15C2 (E) , or Ms IgG control (F) antibodies. 12B2 pulled down only GSK3β (12B2-IP), 15C2 pulled down both GSK3α and β (15C2-IP) and Ms IgG did not pull down GSK3α or β (MsIgG-IP). The post-IP lysates were also run for comparisons to the input samples. These experiments were performed three independent times.
    Figure Legend Snippet: 12B2 and 15C2 are specific for nonphospho-S GSK3 in brain lysates of human, mouse, and rat, and both effectively immunoprecipitate GSK3 from cell lysates. (A) Protein sequence alignments for GSK3β (amino acids 1–25) and GSK3α (amino acids 13–37) from human, mouse and rat (Uniprot IDs in parentheses). (B,C) Blots of lysates from human, mouse and rat cortical tissue and GAPDH was used as a loading control (40 μg/lane total protein loaded; experiment repeated three times). (B) 12B2 (red) specifically labeled GSK3β, not GSK3α, in lysates and total GSK3α/β (green) was used to identify both isoforms. (C) 15C2 (red) labeled both GSK3β and GSK3α in lysates and total GSK3α/β (green) was used to identify both isoforms. (D–F) The 12B2 (D) , 15C2 (E) , or control mouse IgG ( F , Ms IgG) were used to immunoprecipitate GSK3 enzymes from HEK293T cell lysates. The starting lysate (Input) was incubated with magnetic beads coated with 12B2 (D) , 15C2 (E) , or Ms IgG control (F) antibodies. 12B2 pulled down only GSK3β (12B2-IP), 15C2 pulled down both GSK3α and β (15C2-IP) and Ms IgG did not pull down GSK3α or β (MsIgG-IP). The post-IP lysates were also run for comparisons to the input samples. These experiments were performed three independent times.

    Techniques Used: Sequencing, Labeling, Mass Spectrometry, Incubation, Magnetic Beads

    2) Product Images from "Tollip coordinates Parkin‐dependent trafficking of mitochondrial‐derived vesicles"

    Article Title: Tollip coordinates Parkin‐dependent trafficking of mitochondrial‐derived vesicles

    Journal: The EMBO Journal

    doi: 10.15252/embj.2019102539

    Tollip and Parkin are in complex in a CUE domain‐dependent manner, but independent of autophagy and Tom1 HeLa cells expressing mycBioID–Tollip and HA‐Parkin were either left untreated or treated with 5 μM antimycin A/10 μM oligomycin (AO) or AO/100 μM bafilomycin A (BfnA1) for 6 h in the presence of biotin. Cells were lysed and streptavidin pulldowns performed overnight to isolate biotinylated proteins. Proteins in whole‐cell extracts and pulldowns from each condition were then separated by SDS–PAGE and membranes probed with specific antibodies. Immunoblotting for Tom1 and mycBioID–Tollip was used as positive controls. Cells cultured in media lacking biotin were used as a negative control to assess background levels. Biotinylation of Parkin suggested Tollip specifically interacted with Parkin under these conditions. HeLa cells expressing mycBioID alone and HA‐Parkin were used to confirm the specificity of the Tollip–Parkin interaction. HeLa cells coexpressing GFP‐Tollip and HA‐Parkin were either left untreated or treated with AO for 2 h prior to lysis. Cell lysates were subjected to either a normal rabbit IgG IP or HA IP, and Western blot analysis was performed using antibodies against Parkin and GFP. HeLa cells expressing mycBioID–Tollip containing the CUE domain mutation (CUEmut) and HA‐Parkin were subjected to biotinylation and streptavidin pulldowns, followed by Western blot analysis. HeLa wild type (WT), Tom1 KO and ATG5 KO cells expressing mycBioID–Tollip and HA‐Parkin underwent the same conditions as those above and immunoblotted for the indicated proteins. Source data are available online for this figure.
    Figure Legend Snippet: Tollip and Parkin are in complex in a CUE domain‐dependent manner, but independent of autophagy and Tom1 HeLa cells expressing mycBioID–Tollip and HA‐Parkin were either left untreated or treated with 5 μM antimycin A/10 μM oligomycin (AO) or AO/100 μM bafilomycin A (BfnA1) for 6 h in the presence of biotin. Cells were lysed and streptavidin pulldowns performed overnight to isolate biotinylated proteins. Proteins in whole‐cell extracts and pulldowns from each condition were then separated by SDS–PAGE and membranes probed with specific antibodies. Immunoblotting for Tom1 and mycBioID–Tollip was used as positive controls. Cells cultured in media lacking biotin were used as a negative control to assess background levels. Biotinylation of Parkin suggested Tollip specifically interacted with Parkin under these conditions. HeLa cells expressing mycBioID alone and HA‐Parkin were used to confirm the specificity of the Tollip–Parkin interaction. HeLa cells coexpressing GFP‐Tollip and HA‐Parkin were either left untreated or treated with AO for 2 h prior to lysis. Cell lysates were subjected to either a normal rabbit IgG IP or HA IP, and Western blot analysis was performed using antibodies against Parkin and GFP. HeLa cells expressing mycBioID–Tollip containing the CUE domain mutation (CUEmut) and HA‐Parkin were subjected to biotinylation and streptavidin pulldowns, followed by Western blot analysis. HeLa wild type (WT), Tom1 KO and ATG5 KO cells expressing mycBioID–Tollip and HA‐Parkin underwent the same conditions as those above and immunoblotted for the indicated proteins. Source data are available online for this figure.

    Techniques Used: Expressing, SDS Page, Cell Culture, Negative Control, Lysis, Western Blot, Mutagenesis

    3) Product Images from "TonEBP recognizes R-loops and initiates m6A RNA methylation for R-loop resolution"

    Article Title: TonEBP recognizes R-loops and initiates m6A RNA methylation for R-loop resolution

    Journal: Nucleic Acids Research

    doi: 10.1093/nar/gkaa1162

    TonEBP interacts with METTL3 and m6A methylase. ( A ) The TonEBP interactome includes METTL3 and R-loop-related proteins. ( B ) HEK293T cell lysates were immunoprecipitated with normal serum (Serum) or anti-TonEBP antibody (TonEBP). Precipitates and cell lysates were blotted for TonEBP and METTL3. ( C ) Cell lysates were immunoprecipitated with normal rabbit IgG (IgG) or anti-METTL3 IgG (METTL3). ( D ) Domain structures of human TonEBP (WT), and deletion proteins ΔRHD and Yc1. ( E ) Domain structures of human METTL3 (WT) and deletion proteins 1–380, 1–200 and 381–580. ( F ) Cells were transfected with plasmids expressing Flag-METTL3 together with Myc-tagged TonEBP (WT), ΔRHD, or Yc1. After 24 h, cell lysates were prepared and immunoprecipitated using anti-FLAG antibody. ( G ) Cells were transfected with plasmids expressing Myc-Yc1 together with Flag-tagged METTL3 (WT), 1–380, 1–200 or 381–500 and immunoprecipitation was performed with Myc antibody 24 h later. ( H ) Amino-acid sequence alignment of the highly conserved and charged regions of TonEBP from seven species. 3M is a mutant Yc1 in which R, E and R were all exchanged to A shown in red and 5M is another mutant where K, R, and the three Ks were all replaced by A shown in green. ( I ) Cells were transfected with a plasmid expressing Flag-tagged Yc1, 3M or 5M. Cell lysates were prepared and immunoprecipitated with anti-FLAG antibody after 24 h incubation.
    Figure Legend Snippet: TonEBP interacts with METTL3 and m6A methylase. ( A ) The TonEBP interactome includes METTL3 and R-loop-related proteins. ( B ) HEK293T cell lysates were immunoprecipitated with normal serum (Serum) or anti-TonEBP antibody (TonEBP). Precipitates and cell lysates were blotted for TonEBP and METTL3. ( C ) Cell lysates were immunoprecipitated with normal rabbit IgG (IgG) or anti-METTL3 IgG (METTL3). ( D ) Domain structures of human TonEBP (WT), and deletion proteins ΔRHD and Yc1. ( E ) Domain structures of human METTL3 (WT) and deletion proteins 1–380, 1–200 and 381–580. ( F ) Cells were transfected with plasmids expressing Flag-METTL3 together with Myc-tagged TonEBP (WT), ΔRHD, or Yc1. After 24 h, cell lysates were prepared and immunoprecipitated using anti-FLAG antibody. ( G ) Cells were transfected with plasmids expressing Myc-Yc1 together with Flag-tagged METTL3 (WT), 1–380, 1–200 or 381–500 and immunoprecipitation was performed with Myc antibody 24 h later. ( H ) Amino-acid sequence alignment of the highly conserved and charged regions of TonEBP from seven species. 3M is a mutant Yc1 in which R, E and R were all exchanged to A shown in red and 5M is another mutant where K, R, and the three Ks were all replaced by A shown in green. ( I ) Cells were transfected with a plasmid expressing Flag-tagged Yc1, 3M or 5M. Cell lysates were prepared and immunoprecipitated with anti-FLAG antibody after 24 h incubation.

    Techniques Used: Immunoprecipitation, Transfection, Expressing, Sequencing, Mutagenesis, Plasmid Preparation, Incubation

    4) Product Images from "Bacterial superglue enables easy development of efficient virus-like particle based vaccines"

    Article Title: Bacterial superglue enables easy development of efficient virus-like particle based vaccines

    Journal: Journal of Nanobiotechnology

    doi: 10.1186/s12951-016-0181-1

    Antigen-specific IgG levels in mice after immunization with soluble or spy-VLP displayed malaria antigens. ( a , upper panels ) Antigen-specific IgG levels (OD Elisa) in serum from mice (n = 5 per group) immunized with a Pfs25 2xSpyTag-VLP vaccine ( filled circles ) or with a control vaccine consisting of soluble Pfs25 mixed with untagged AP205 VLPs ( open squares ). Both vaccines were formulated using aluminum hydroxide adjuvant (Statens Serum Institut, Copenhagen, Denmark). Mice were immunized on days 0, 21 and 42 and serum was collected on the indicated days after first immunization. Differences in median endpoint titers between vaccination groups were analyzed using Mann–Whitney Rank Sum test; day 14 (P
    Figure Legend Snippet: Antigen-specific IgG levels in mice after immunization with soluble or spy-VLP displayed malaria antigens. ( a , upper panels ) Antigen-specific IgG levels (OD Elisa) in serum from mice (n = 5 per group) immunized with a Pfs25 2xSpyTag-VLP vaccine ( filled circles ) or with a control vaccine consisting of soluble Pfs25 mixed with untagged AP205 VLPs ( open squares ). Both vaccines were formulated using aluminum hydroxide adjuvant (Statens Serum Institut, Copenhagen, Denmark). Mice were immunized on days 0, 21 and 42 and serum was collected on the indicated days after first immunization. Differences in median endpoint titers between vaccination groups were analyzed using Mann–Whitney Rank Sum test; day 14 (P

    Techniques Used: Mouse Assay, Enzyme-linked Immunosorbent Assay, MANN-WHITNEY

    Breakage of self-tolerance. IgG autoantibody responses measured by standard ELISA. a , b C57BL/6 mice (n = 10 per group) were immunized with a PD-L1 ( a ) or CTLA-4 ( b ) SpyCatcher-VLP vaccine ( filled circles ) or with a control vaccine (n = 3 per group) consisting of similar amounts of spy-antigen mixed with untagged AP205 VLPs ( open squares ). Both vaccines were formulated using aluminum hydroxide adjuvant (Statens Serum Institut, Copenhagen, Denmark). Mice were immunized with a dose of 5 µg antigen on days 0, 21 and 42 and serum was collected on day 56 after first immunization. Median endpoint titers were compared for the PD-L1 vaccination groups (P = 0.01) and the CTLA-4 vaccination groups (P = 0.01) using Mann–Whitney Rank Sum test. c , d BALB/c mice (n = 4) were immunized with an IL-5 SpyTag-VLP vaccine or a control vaccine (soluble IL-5 + untagged AP205 VLP) (n = 5) which were both formulated with aluminum hydroxide (Statens Serum Institut, Copenhagen, Denmark). Mice were immunized on days 0, 21 and 42 with antigen doses of 5, 2.5 and 2.5 µg, respectively, and serum was collected on days 56 ( c ) and 112 ( d ). Median endpoint titers for the two vaccination groups were compared using Mann–Whitney Rank Sum test; day 56 (P = 0.2) and day 122 (P = 0.2)
    Figure Legend Snippet: Breakage of self-tolerance. IgG autoantibody responses measured by standard ELISA. a , b C57BL/6 mice (n = 10 per group) were immunized with a PD-L1 ( a ) or CTLA-4 ( b ) SpyCatcher-VLP vaccine ( filled circles ) or with a control vaccine (n = 3 per group) consisting of similar amounts of spy-antigen mixed with untagged AP205 VLPs ( open squares ). Both vaccines were formulated using aluminum hydroxide adjuvant (Statens Serum Institut, Copenhagen, Denmark). Mice were immunized with a dose of 5 µg antigen on days 0, 21 and 42 and serum was collected on day 56 after first immunization. Median endpoint titers were compared for the PD-L1 vaccination groups (P = 0.01) and the CTLA-4 vaccination groups (P = 0.01) using Mann–Whitney Rank Sum test. c , d BALB/c mice (n = 4) were immunized with an IL-5 SpyTag-VLP vaccine or a control vaccine (soluble IL-5 + untagged AP205 VLP) (n = 5) which were both formulated with aluminum hydroxide (Statens Serum Institut, Copenhagen, Denmark). Mice were immunized on days 0, 21 and 42 with antigen doses of 5, 2.5 and 2.5 µg, respectively, and serum was collected on days 56 ( c ) and 112 ( d ). Median endpoint titers for the two vaccination groups were compared using Mann–Whitney Rank Sum test; day 56 (P = 0.2) and day 122 (P = 0.2)

    Techniques Used: Enzyme-linked Immunosorbent Assay, Mouse Assay, MANN-WHITNEY

    5) Product Images from "Lupus auto-antibodies act as positive allosteric modulators at NMDA receptors and induce spatial memory deficits"

    Article Title: Lupus auto-antibodies act as positive allosteric modulators at NMDA receptors and induce spatial memory deficits

    Journal: bioRxiv

    doi: 10.1101/791715

    Differential sensitivity of N2A- and N2B-containing NMDARs to DNRAbs. ( A B ) Moderate pathophysiological levels of DNRAbs (10 μg/mL) potentiate glutamate-activated currents in N2A-containing, but not in N2B-containing NMDARs. Upper panels , Whole-cell currents from HEK293 cells expressing human NMDAR subunits, either hGluN1/hGluN2A ( A ) or hGluN1/hGluN2B ( B ). Currents were elicited by a 2.5 s application of glutamate (1 mM) in the continuous presence of glycine (0.1 mM) (holding potential, −70 mV). Lower panels , control antibody B1 (IgG1, gray circles) or human-derived DNRAb G11 (green circles) were added 75 s after a baseline recording of 5 sweeps and were included in the bath throughout the remaining period. Current amplitudes for individual recordings were normalized to its baseline. Values are mean ± SEM (hN2A+B1, n = 6; hN2A+G11, n = 6; hN2B+B1, n = 5; hN2B+G11, n = 5). Example traces in upper panels show the +G11 recordings for the initial sweep during baseline (no antibody present) or for the last sweep during steady-state (in antibody). ( C D ) Peak current amplitudes in N2A-containing NMDAR are more strongly potentiated than those in N2B-containing receptors. Bar graphs (mean ± SEM with dots indicating individual values) (from left to right for hN1/hN2A, n = 6, 6, 6, 6, 5, 5; and for hN1/hN2B, n = 5, 5, 6, 5) showing normalized steady-state peak current amplitudes either for control antibody (B1) or DNRAbs (G11). Significance of DNRAb values are measured relative to their respective control (* p
    Figure Legend Snippet: Differential sensitivity of N2A- and N2B-containing NMDARs to DNRAbs. ( A B ) Moderate pathophysiological levels of DNRAbs (10 μg/mL) potentiate glutamate-activated currents in N2A-containing, but not in N2B-containing NMDARs. Upper panels , Whole-cell currents from HEK293 cells expressing human NMDAR subunits, either hGluN1/hGluN2A ( A ) or hGluN1/hGluN2B ( B ). Currents were elicited by a 2.5 s application of glutamate (1 mM) in the continuous presence of glycine (0.1 mM) (holding potential, −70 mV). Lower panels , control antibody B1 (IgG1, gray circles) or human-derived DNRAb G11 (green circles) were added 75 s after a baseline recording of 5 sweeps and were included in the bath throughout the remaining period. Current amplitudes for individual recordings were normalized to its baseline. Values are mean ± SEM (hN2A+B1, n = 6; hN2A+G11, n = 6; hN2B+B1, n = 5; hN2B+G11, n = 5). Example traces in upper panels show the +G11 recordings for the initial sweep during baseline (no antibody present) or for the last sweep during steady-state (in antibody). ( C D ) Peak current amplitudes in N2A-containing NMDAR are more strongly potentiated than those in N2B-containing receptors. Bar graphs (mean ± SEM with dots indicating individual values) (from left to right for hN1/hN2A, n = 6, 6, 6, 6, 5, 5; and for hN1/hN2B, n = 5, 5, 6, 5) showing normalized steady-state peak current amplitudes either for control antibody (B1) or DNRAbs (G11). Significance of DNRAb values are measured relative to their respective control (* p

    Techniques Used: Expressing, Derivative Assay

    Related Articles

    Binding Assay:

    Article Title: Critical role of activation induced cytidine deaminase in Experimental Autoimmune Encephalomyelitis
    Article Snippet: Sera were diluted 1:20 in PBS and incubated for 60 minutes at room temperature. .. After washing with PBS, binding of IgG1 or IgM on brain tissue was detected using IgG1 and IgM specific secondary antibodies (Invitrogen, A21121 and A21042; 5 ug/ml) conjugated to Alexa Fluor 488. ..

    Incubation:

    Article Title: A Formulated TLR7/8 Agonist is a Flexible, Highly Potent and Effective Adjuvant for Pandemic Influenza Vaccines
    Article Snippet: For post-vaccination immune analysis, arrays were initially blocked with PBS + 1% Fetal Bovine Serum + 0.1% Tween-20, washed three times with Protein Array Wash Buffer (ArrayIt), and incubated with 300 μL of a 1:100 dilution of post-immunization mouse serum for 1 hour with shaking. .. Following primary incubation, arrays were washed 5 times with wash buffer, and incubated with fluorophore conjugated secondary antibodies for IgG2c (Jackson Immunoresearch, Part #: 115-495-208) and IgG1 (Life Technologies, Part#: A21123) at a 1:2000 dilution. .. Following a 30 minute incubation at room temperature, arrays were rinsed with Rinse Buffer (Arrayit), and analyzed using a Molecular Dynamics 400B array scanner.

    Article Title: PRMT5 is essential for B cell development and germinal center dynamics
    Article Snippet: ELISPOT Purified splenocytes or BM cells were added at different dilutions to a 96-well 0.45-μm PVDF membrane (Millipore, cat#MSIPS4W10) previously coated overnight at 4 °C with 2 μg/mL NP20 BSA and blocked with complete RPMI cell culture media for 2 h at 37 °C. .. Plates with cells were incubated in a humid chamber 12 h at 37 °C, 5% CO2 , then washed 6× with PBS 0.01% Tween-20, followed by incubation with goat anti-mouse IgG1-HRP (A10551, Life Technologies, 1/2000) diluted in culture media for 2 h at RT. .. Plates were washed and AEC substrate (3′ amino-9-ethylcarbazole; BD Bioscience) was added to reveal the spots.

    Western Blot:

    Article Title: Smurf1 inhibits integrin activation by controlling Kindlin-2 ubiquitination and degradation
    Article Snippet: Antibodies and reagents The following primary antibodies were used at indicated concentrations for Western blot (WB), immunofluorescence (IF), or FACS: mouse anti-Smurf1 (clone 1D7; ab117552; Abcam), WB, 1:1,000; IF, 1:100; mouse anti-Talin (clone 8D4; sc-59881; Santa Cruz Biotechnology, Inc.), WB, 1:1,000; rabbit anti-paxillin (clone Y113; ab32084; Abcam), WB, 1:5,000; IF, 1:200; rabbit anti–β1 integrin (clone EPR1040Y; ab134179; Abcam), WB, 1:500; FACS, 1:100; rat anti–β1 integrin (clone KMI6; ab95623; Abcam), WB, 1:1,000; FACS, 1:200; mouse anti–β3 integrin (clone VI-PL2; ab110131; Abcam), WB, 1:1,000; FACS, 1:200; rabbit anti–Kindlin-2 (K3269; Sigma-Aldrich), WB, 1:1,000; mouse anti-Flag (clone M2; Sigma-Aldrich), WB, 1:2,000; mouse anti-GFP (clone GSN149; G1546; Sigma-Aldrich), WB, 1:2,000; rabbit anti-Myc (SAB4301136; Sigma-Aldrich), WB, 1:2,000; mouse anti-HA (clone HA-7; H9658; Sigma-Aldrich), WB, 1:5,000; mouse anti–Kindlin-2 (clone 3A3; Mab2617; EMD Millipore), WB, 1:1,000; IF, 1:200; goat anti–Kindlin-2 (clone Y-15; sc-30854; Santa Cruz Biotechnology, Inc.), IF, 1:100; rabbit anti-ubiquitin (3933; Cell Signaling Technology), WB, 1:1,000; rat anti–active-integrin β1 9EG7 (clone 9EG7; 553715; BD), IF, 1:200; FACS, 1:200; ligand-mimetic anti–integrin aIIbβ3 mAb PAC-1 (340507; BD); and mouse anti-actin (clone 2Q1055; sc-58673; Santa Cruz Biotechnology, Inc.), WB, 1:2,000. .. Secondary antibodies were goat anti–mouse HRP and goat anti–rabbit HRP (both Santa Cruz Biotechnology, Inc.), WB, 1:5,000; donkey anti-mouse Alexa Fluor 488 ( A21202 ); donkey anti-rabbit Alexa Fluor 488 ( A21206 ); donkey anti-goat Alexa Fluor 488 ( A11055 ); donkey anti-mouse Alexa Fluor 568 ( A10037 ); donkey anti-rabbit Alexa Fluor 568 ( A10042 ); goat anti–mouse Alexa Fluor 633 ( A21126 ); goat anti–rat IgM Alexa Fluor 647 ( A21248 ; all Invitrogen), FACS, 1:300; IF, 1:400. .. Proteasome inhibitor MG132 (SML1135) and protein synthesis inhibitor cycloheximide (C7698) were purchased from Sigma-Aldrich.

    FACS:

    Article Title: Smurf1 inhibits integrin activation by controlling Kindlin-2 ubiquitination and degradation
    Article Snippet: Antibodies and reagents The following primary antibodies were used at indicated concentrations for Western blot (WB), immunofluorescence (IF), or FACS: mouse anti-Smurf1 (clone 1D7; ab117552; Abcam), WB, 1:1,000; IF, 1:100; mouse anti-Talin (clone 8D4; sc-59881; Santa Cruz Biotechnology, Inc.), WB, 1:1,000; rabbit anti-paxillin (clone Y113; ab32084; Abcam), WB, 1:5,000; IF, 1:200; rabbit anti–β1 integrin (clone EPR1040Y; ab134179; Abcam), WB, 1:500; FACS, 1:100; rat anti–β1 integrin (clone KMI6; ab95623; Abcam), WB, 1:1,000; FACS, 1:200; mouse anti–β3 integrin (clone VI-PL2; ab110131; Abcam), WB, 1:1,000; FACS, 1:200; rabbit anti–Kindlin-2 (K3269; Sigma-Aldrich), WB, 1:1,000; mouse anti-Flag (clone M2; Sigma-Aldrich), WB, 1:2,000; mouse anti-GFP (clone GSN149; G1546; Sigma-Aldrich), WB, 1:2,000; rabbit anti-Myc (SAB4301136; Sigma-Aldrich), WB, 1:2,000; mouse anti-HA (clone HA-7; H9658; Sigma-Aldrich), WB, 1:5,000; mouse anti–Kindlin-2 (clone 3A3; Mab2617; EMD Millipore), WB, 1:1,000; IF, 1:200; goat anti–Kindlin-2 (clone Y-15; sc-30854; Santa Cruz Biotechnology, Inc.), IF, 1:100; rabbit anti-ubiquitin (3933; Cell Signaling Technology), WB, 1:1,000; rat anti–active-integrin β1 9EG7 (clone 9EG7; 553715; BD), IF, 1:200; FACS, 1:200; ligand-mimetic anti–integrin aIIbβ3 mAb PAC-1 (340507; BD); and mouse anti-actin (clone 2Q1055; sc-58673; Santa Cruz Biotechnology, Inc.), WB, 1:2,000. .. Secondary antibodies were goat anti–mouse HRP and goat anti–rabbit HRP (both Santa Cruz Biotechnology, Inc.), WB, 1:5,000; donkey anti-mouse Alexa Fluor 488 ( A21202 ); donkey anti-rabbit Alexa Fluor 488 ( A21206 ); donkey anti-goat Alexa Fluor 488 ( A11055 ); donkey anti-mouse Alexa Fluor 568 ( A10037 ); donkey anti-rabbit Alexa Fluor 568 ( A10042 ); goat anti–mouse Alexa Fluor 633 ( A21126 ); goat anti–rat IgM Alexa Fluor 647 ( A21248 ; all Invitrogen), FACS, 1:300; IF, 1:400. .. Proteasome inhibitor MG132 (SML1135) and protein synthesis inhibitor cycloheximide (C7698) were purchased from Sigma-Aldrich.

    Staining:

    Article Title: The paracaspase MALT1 cleaves HOIL1 reducing linear ubiquitination by LUBAC to dampen lymphocyte NF-κB signalling
    Article Snippet: Before staining, the cells were permeabilized with 0.1% Triton X-100 and then blocked with 2% BSA, 10% goat serum and 25 μg ml−1 of the 2.4G2 monoclonal antibody, which blocks Fc receptors on the B cells. .. The cells were then stained with AlexaFluor 568-conjugated goat anti-rat IgG (H+L chain-reactive; Life Technologies, catalogue number A11077) to visualize the anti-Igκ surrogate Ag, and with a mouse IgG1 anti-linear polyubiquitin (LUB9) monoclonal antibody (LifeSensors, catalogue # AB130, the same antibody used to probe the TUBEs assays)), the same antibody was used to probe the TUBE assay blots, followed by staining with an AlexaFluor 647-conjugated goat anti-mouse IgG1 (γ1 H chain-specific; Life Technologies, catalogue number A21240) secondary antibody and AlexaFluor 488 Phalloidin (Life Technologies catalogue # A12379) to visualize F-actin. .. Naive primary B cells, which express IgM and IgD, but not IgG, were not stained to any significant extent by the goat anti-mouse IgG1 secondary antibody in the absence of primary antibody.

    other:

    Article Title: Tollip coordinates Parkin‐dependent trafficking of mitochondrial‐derived vesicles
    Article Snippet: These were Alexa Fluor anti‐rabbit 488 (A11034), anti‐mouse 488 (A11029), anti‐mouse IgG1 488 (A21121), anti‐mouse 568 (A11031), anti‐rabbit 568 (A11036), anti‐mouse IgG2b 568 (A21144), anti‐mouse IgG2b 594 (A21145), anti‐rabbit 633 (A21070) and anti‐mouse IgG1 647 (A21240).

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  • 95
    Thermo Fisher cross adsorbed goat anti mouse igg conjugated to alexa fluor 568
    Confocal microscopy and adherence-invasion assays with pharmacologic inhibitors. Lipid raft-independent invasion of bronchial epithelial cells by NTHI. (A) Confocal microscopy. At 4 and 24 h postinoculation of H292 cells, NTHI does not colocalize with vesicles positive for the following markers of lipid rafts: caveolin-1 (shown at 24 h), flotillin-1 (shown at 24 h), and cholesterol (shown at 4 h). NTHI was labeled with anti-11P6H antibody conjugated to <t>Alexa</t> Fluor 488 (green). Caveolin-1 was labeled with anti-caveolin-1 antibody and goat anti-mouse antibody conjugated to Alexa <t>Fluor</t> 568 (red). Flotillin-1 was labeled with anti-flotillin-1 antibody and goat anti-mouse antibody conjugated to Alexa Fluor 568 (red). Cholesterol was labeled with filipin (blue), and those samples were also labeled with anti-human secretory component antibody and donkey anti-goat antibody conjugated to Alexa Fluor 568 (red) to provide additional visualization of the plasma membrane. (B) Confocal microscopy. Filipin (FLP) and nystatin (NST) inhibit the internalization of fluorescently conjugated cholera toxin B subunit (white arrows), a known cargo of lipid raft-mediated endocytosis. H292 cells were pretreated with sRPMI containing inhibitor or inhibitor diluent, followed by addition of the cargo conjugate, incubation for 20 min on ice, and incubation for 2 h at 37°C. (C) Adherence-invasion assays. Filipin and nystatin do not inhibit invasion by NTHI. H292 cells were pretreated with inhibitor or inhibitor diluent for 2 h, followed by a 4-h infection conducted according to the adherence-invasion assay protocol. Data are normalized to samples in the absence of inhibitor. Error bars represent standard errors of the means of three independent experiments. A paired Student t test was used to calculate statistical significance. *, P ≤ 0.05; **, P ≤ 0.005.
    Cross Adsorbed Goat Anti Mouse Igg Conjugated To Alexa Fluor 568, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/cross adsorbed goat anti mouse igg conjugated to alexa fluor 568/product/Thermo Fisher
    Average 95 stars, based on 1 article reviews
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    97
    Thermo Fisher alexa 488 conjugated secondary anti goat antibodies
    Expression analysis of Wnt/β-catenin target genes, CD44 and EphB2, in the gastrointestinal tract of Ad Dkk1- or Ad Fc-treated adult C57BL/6 mice (12–16 weeks old). Organs were harvested 2 days after Ad Dkk1 i.v injection (10 9 pfu). ( Left ) Ad Dkk1 repression of CD44 expression in proliferative zones of all levels of the gastrointestinal epithelium. Arrowheads indicate the absence of CD44 immunoreactivity in proliferative compartments of the intestinal epithelium in Ad Dkk1 animals. * , residual CD44 staining in nonepithelial lamina propria. ( Right ) Ad Dkk1 repression of EphB2 in small intestine and colon. Repression was weaker in ascending colon and no repression was observed in stomach. EphB2 immunofluorescence was performed with <t>Alexa</t> 488 detection of EphB2 immunoreactivity (green) and Hoechst 33342 nuclear counterstain (blue). Stomach (st), duodenum (du), jejunum (je), ileum (il), cecum (ce), ascending colon (ac), and descending colon (dc) are shown.
    Alexa 488 Conjugated Secondary Anti Goat Antibodies, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/alexa 488 conjugated secondary anti goat antibodies/product/Thermo Fisher
    Average 97 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    alexa 488 conjugated secondary anti goat antibodies - by Bioz Stars, 2021-04
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    97
    Thermo Fisher alexa 488 conjugated anti mouse goat antibody
    Expression of IL-6 following MyD88 inhibitor and TLR3 ligand treatment.  (A)  Fluorescent microscopy image of T47D cells, treated with TLR3 ligand (10 μg/ml) with or without MyD88 inhibitor (1 μM) following immunocytochemical staining with antibody against IL-6 and Alexa 488-tagged secondary antibody and counterstained with DAPI. Untreated indicates the cells are not treated with TLR3 ligand (magnification, 40X).  (B)  Bar graph showing the expression of IL-6 following observation through a microscope and analyses through the ImageJ software for all the experiment groups.  (C,D)  Expression of IL-6 in the cell culture supernatant as measured through ELISA. The results are presented as mean ± SD ( p
    Alexa 488 Conjugated Anti Mouse Goat Antibody, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/alexa 488 conjugated anti mouse goat antibody/product/Thermo Fisher
    Average 97 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    alexa 488 conjugated anti mouse goat antibody - by Bioz Stars, 2021-04
    97/100 stars
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    Image Search Results


    Confocal microscopy and adherence-invasion assays with pharmacologic inhibitors. Lipid raft-independent invasion of bronchial epithelial cells by NTHI. (A) Confocal microscopy. At 4 and 24 h postinoculation of H292 cells, NTHI does not colocalize with vesicles positive for the following markers of lipid rafts: caveolin-1 (shown at 24 h), flotillin-1 (shown at 24 h), and cholesterol (shown at 4 h). NTHI was labeled with anti-11P6H antibody conjugated to Alexa Fluor 488 (green). Caveolin-1 was labeled with anti-caveolin-1 antibody and goat anti-mouse antibody conjugated to Alexa Fluor 568 (red). Flotillin-1 was labeled with anti-flotillin-1 antibody and goat anti-mouse antibody conjugated to Alexa Fluor 568 (red). Cholesterol was labeled with filipin (blue), and those samples were also labeled with anti-human secretory component antibody and donkey anti-goat antibody conjugated to Alexa Fluor 568 (red) to provide additional visualization of the plasma membrane. (B) Confocal microscopy. Filipin (FLP) and nystatin (NST) inhibit the internalization of fluorescently conjugated cholera toxin B subunit (white arrows), a known cargo of lipid raft-mediated endocytosis. H292 cells were pretreated with sRPMI containing inhibitor or inhibitor diluent, followed by addition of the cargo conjugate, incubation for 20 min on ice, and incubation for 2 h at 37°C. (C) Adherence-invasion assays. Filipin and nystatin do not inhibit invasion by NTHI. H292 cells were pretreated with inhibitor or inhibitor diluent for 2 h, followed by a 4-h infection conducted according to the adherence-invasion assay protocol. Data are normalized to samples in the absence of inhibitor. Error bars represent standard errors of the means of three independent experiments. A paired Student t test was used to calculate statistical significance. *, P ≤ 0.05; **, P ≤ 0.005.

    Journal: Infection and Immunity

    Article Title: Internalization and Trafficking of Nontypeable Haemophilus influenzae in Human Respiratory Epithelial Cells and Roles of IgA1 Proteases for Optimal Invasion and Persistence

    doi: 10.1128/IAI.00864-13

    Figure Lengend Snippet: Confocal microscopy and adherence-invasion assays with pharmacologic inhibitors. Lipid raft-independent invasion of bronchial epithelial cells by NTHI. (A) Confocal microscopy. At 4 and 24 h postinoculation of H292 cells, NTHI does not colocalize with vesicles positive for the following markers of lipid rafts: caveolin-1 (shown at 24 h), flotillin-1 (shown at 24 h), and cholesterol (shown at 4 h). NTHI was labeled with anti-11P6H antibody conjugated to Alexa Fluor 488 (green). Caveolin-1 was labeled with anti-caveolin-1 antibody and goat anti-mouse antibody conjugated to Alexa Fluor 568 (red). Flotillin-1 was labeled with anti-flotillin-1 antibody and goat anti-mouse antibody conjugated to Alexa Fluor 568 (red). Cholesterol was labeled with filipin (blue), and those samples were also labeled with anti-human secretory component antibody and donkey anti-goat antibody conjugated to Alexa Fluor 568 (red) to provide additional visualization of the plasma membrane. (B) Confocal microscopy. Filipin (FLP) and nystatin (NST) inhibit the internalization of fluorescently conjugated cholera toxin B subunit (white arrows), a known cargo of lipid raft-mediated endocytosis. H292 cells were pretreated with sRPMI containing inhibitor or inhibitor diluent, followed by addition of the cargo conjugate, incubation for 20 min on ice, and incubation for 2 h at 37°C. (C) Adherence-invasion assays. Filipin and nystatin do not inhibit invasion by NTHI. H292 cells were pretreated with inhibitor or inhibitor diluent for 2 h, followed by a 4-h infection conducted according to the adherence-invasion assay protocol. Data are normalized to samples in the absence of inhibitor. Error bars represent standard errors of the means of three independent experiments. A paired Student t test was used to calculate statistical significance. *, P ≤ 0.05; **, P ≤ 0.005.

    Article Snippet: Host cell components were visualized using filipin III fluorescent dye (final concentration of 333 μg/ml; Cayman Chemical), primary monoclonal antibodies including mouse anti-caveolin-1 antibody (1:50; BD), mouse anti-early endosomal antigen 1 (EEA-1) antibody (1:200; BD), mouse anti-flotillin-1 antibody (1:20; BD), mouse anti-human CD107a antibody (LAMP1) (1:200; BD), and goat anti-human secretory component antibody (1:200; Sigma), and secondary antibodies including highly cross-adsorbed goat anti-mouse IgG conjugated to Alexa Fluor 568 (Life Technologies, 1:200) and donkey anti-goat IgG conjugated to Alexa Fluor 568 (Life Technologies, 1:200).

    Techniques: Confocal Microscopy, Labeling, Incubation, Infection, Invasion Assay

    Confocal microscopy and survival assay with pharmacologic inhibitor of lysosome acidification. NTHI traffics to early endosomes and lysosomes and is killed in lysosomes. IgA1 proteases are required for optimal survival in lysosomes. (A) Confocal microscopy. At 4 and 24 h postinoculation of H292 cells, NTHI is found within vesicles positive for EEA1 (shown at 4 h) and within vesicles positive for LAMP1 (shown at 24 h). NTHI was labeled using anti-11P6H antibody conjugated to Alexa Fluor 488 (green). EEA1 was labeled using anti-EEA1 antibody and goat anti-mouse antibody conjugated to Alexa Fluor 568 (red). LAMP1 was labeled using anti-human LAMP1 antibody and goat anti-mouse antibody conjugated to Alexa Fluor 568 (red). (B) Survival assay in the presence and absence of concanamycin A (CMA). H292 cells were infected for 16 h, treated with gentamicin for 1 h, and treated with concanamycin or diluent for 3 h. Survival data are normalized to samples treated with diluent. Error bars represent standard errors of the means of three independent experiments. A paired Student t test was used to calculate statistical significance. *, P ≤ 0.05; **, P ≤ 0.005.

    Journal: Infection and Immunity

    Article Title: Internalization and Trafficking of Nontypeable Haemophilus influenzae in Human Respiratory Epithelial Cells and Roles of IgA1 Proteases for Optimal Invasion and Persistence

    doi: 10.1128/IAI.00864-13

    Figure Lengend Snippet: Confocal microscopy and survival assay with pharmacologic inhibitor of lysosome acidification. NTHI traffics to early endosomes and lysosomes and is killed in lysosomes. IgA1 proteases are required for optimal survival in lysosomes. (A) Confocal microscopy. At 4 and 24 h postinoculation of H292 cells, NTHI is found within vesicles positive for EEA1 (shown at 4 h) and within vesicles positive for LAMP1 (shown at 24 h). NTHI was labeled using anti-11P6H antibody conjugated to Alexa Fluor 488 (green). EEA1 was labeled using anti-EEA1 antibody and goat anti-mouse antibody conjugated to Alexa Fluor 568 (red). LAMP1 was labeled using anti-human LAMP1 antibody and goat anti-mouse antibody conjugated to Alexa Fluor 568 (red). (B) Survival assay in the presence and absence of concanamycin A (CMA). H292 cells were infected for 16 h, treated with gentamicin for 1 h, and treated with concanamycin or diluent for 3 h. Survival data are normalized to samples treated with diluent. Error bars represent standard errors of the means of three independent experiments. A paired Student t test was used to calculate statistical significance. *, P ≤ 0.05; **, P ≤ 0.005.

    Article Snippet: Host cell components were visualized using filipin III fluorescent dye (final concentration of 333 μg/ml; Cayman Chemical), primary monoclonal antibodies including mouse anti-caveolin-1 antibody (1:50; BD), mouse anti-early endosomal antigen 1 (EEA-1) antibody (1:200; BD), mouse anti-flotillin-1 antibody (1:20; BD), mouse anti-human CD107a antibody (LAMP1) (1:200; BD), and goat anti-human secretory component antibody (1:200; Sigma), and secondary antibodies including highly cross-adsorbed goat anti-mouse IgG conjugated to Alexa Fluor 568 (Life Technologies, 1:200) and donkey anti-goat IgG conjugated to Alexa Fluor 568 (Life Technologies, 1:200).

    Techniques: Confocal Microscopy, Clonogenic Cell Survival Assay, Labeling, Infection

    Expression analysis of Wnt/β-catenin target genes, CD44 and EphB2, in the gastrointestinal tract of Ad Dkk1- or Ad Fc-treated adult C57BL/6 mice (12–16 weeks old). Organs were harvested 2 days after Ad Dkk1 i.v injection (10 9 pfu). ( Left ) Ad Dkk1 repression of CD44 expression in proliferative zones of all levels of the gastrointestinal epithelium. Arrowheads indicate the absence of CD44 immunoreactivity in proliferative compartments of the intestinal epithelium in Ad Dkk1 animals. * , residual CD44 staining in nonepithelial lamina propria. ( Right ) Ad Dkk1 repression of EphB2 in small intestine and colon. Repression was weaker in ascending colon and no repression was observed in stomach. EphB2 immunofluorescence was performed with Alexa 488 detection of EphB2 immunoreactivity (green) and Hoechst 33342 nuclear counterstain (blue). Stomach (st), duodenum (du), jejunum (je), ileum (il), cecum (ce), ascending colon (ac), and descending colon (dc) are shown.

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: Essential requirement for Wnt signaling in proliferation of adult small intestine and colon revealed by adenoviral expression of Dickkopf-1

    doi: 10.1073/pnas.2536800100

    Figure Lengend Snippet: Expression analysis of Wnt/β-catenin target genes, CD44 and EphB2, in the gastrointestinal tract of Ad Dkk1- or Ad Fc-treated adult C57BL/6 mice (12–16 weeks old). Organs were harvested 2 days after Ad Dkk1 i.v injection (10 9 pfu). ( Left ) Ad Dkk1 repression of CD44 expression in proliferative zones of all levels of the gastrointestinal epithelium. Arrowheads indicate the absence of CD44 immunoreactivity in proliferative compartments of the intestinal epithelium in Ad Dkk1 animals. * , residual CD44 staining in nonepithelial lamina propria. ( Right ) Ad Dkk1 repression of EphB2 in small intestine and colon. Repression was weaker in ascending colon and no repression was observed in stomach. EphB2 immunofluorescence was performed with Alexa 488 detection of EphB2 immunoreactivity (green) and Hoechst 33342 nuclear counterstain (blue). Stomach (st), duodenum (du), jejunum (je), ileum (il), cecum (ce), ascending colon (ac), and descending colon (dc) are shown.

    Article Snippet: Stainings were visualized with Alexa 488-conjugated secondary anti-goat antibodies (Molecular Probes) and nuclei were counterstained with Hoechst 33342 (Molecular Probes).

    Techniques: Expressing, Mouse Assay, Injection, Staining, Immunofluorescence

    Expression of IL-6 following MyD88 inhibitor and TLR3 ligand treatment.  (A)  Fluorescent microscopy image of T47D cells, treated with TLR3 ligand (10 μg/ml) with or without MyD88 inhibitor (1 μM) following immunocytochemical staining with antibody against IL-6 and Alexa 488-tagged secondary antibody and counterstained with DAPI. Untreated indicates the cells are not treated with TLR3 ligand (magnification, 40X).  (B)  Bar graph showing the expression of IL-6 following observation through a microscope and analyses through the ImageJ software for all the experiment groups.  (C,D)  Expression of IL-6 in the cell culture supernatant as measured through ELISA. The results are presented as mean ± SD ( p

    Journal: Frontiers in Oncology

    Article Title: Myeloid Differentiation Primary Response 88–Cyclin D1 Signaling in Breast Cancer Cells Regulates Toll-Like Receptor 3-Mediated Cell Proliferation

    doi: 10.3389/fonc.2020.01780

    Figure Lengend Snippet: Expression of IL-6 following MyD88 inhibitor and TLR3 ligand treatment. (A) Fluorescent microscopy image of T47D cells, treated with TLR3 ligand (10 μg/ml) with or without MyD88 inhibitor (1 μM) following immunocytochemical staining with antibody against IL-6 and Alexa 488-tagged secondary antibody and counterstained with DAPI. Untreated indicates the cells are not treated with TLR3 ligand (magnification, 40X). (B) Bar graph showing the expression of IL-6 following observation through a microscope and analyses through the ImageJ software for all the experiment groups. (C,D) Expression of IL-6 in the cell culture supernatant as measured through ELISA. The results are presented as mean ± SD ( p

    Article Snippet: For IL-6 expression, cells were fixed, permeabilized, and incubated with primary IL-6 antibody (Invitrogen-AMC0862) and Alexa 488-conjugated anti-mouse goat antibody (Invitrogen-A11001) and mounted with Vecta Shield-DAPI to counterstain the nuclei and were observed under fluorescence microscope (Leica DMI 6000B).

    Techniques: Expressing, Microscopy, Staining, Software, Cell Culture, Enzyme-linked Immunosorbent Assay