Journal: Journal of Enzyme Inhibition and Medicinal Chemistry

Article Title: Rational structure-guided identification of a Bcl-2-targeting peptide with antiproliferative effects on colorectal cancer cells

doi: 10.1080/14756366.2026.2747402

Figure Lengend Snippet: Primers used for RT-qPCR analysis. All primer sequences are shown in the 5′–3′ direction.

Article Snippet: The levels of Bax and Bcl-2 proteins were quantified using human Bax (Bcl-2 Associated X Protein) ELISA kit (Elabscience, Wuhan, China; E-EL-H0562) and human Bcl-2 (B-cell Leukemia/Lymphoma 2) ELISA kit (Elabscience, Wuhan, China; E-EL-H0114), respectively.

Techniques: Analysis

Journal: Journal of Enzyme Inhibition and Medicinal Chemistry

Article Title: Rational structure-guided identification of a Bcl-2-targeting peptide with antiproliferative effects on colorectal cancer cells

doi: 10.1080/14756366.2026.2747402

Figure Lengend Snippet: Workflow for the identification of a Bcl-2-targeting peptide. A library of 59,319 peptides was screened against Bcl-2 by molecular docking, and the selected peptides are further evaluated by MST assays, SAR analysis, and MD simulations. Based on the combined results, Peptide-1 was selected for subsequent in vitro studies.

Article Snippet: The levels of Bax and Bcl-2 proteins were quantified using human Bax (Bcl-2 Associated X Protein) ELISA kit (Elabscience, Wuhan, China; E-EL-H0562) and human Bcl-2 (B-cell Leukemia/Lymphoma 2) ELISA kit (Elabscience, Wuhan, China; E-EL-H0114), respectively.

Techniques: Docking Assay, Analysis, In Vitro

Journal: Journal of Enzyme Inhibition and Medicinal Chemistry

Article Title: Rational structure-guided identification of a Bcl-2-targeting peptide with antiproliferative effects on colorectal cancer cells

doi: 10.1080/14756366.2026.2747402

Figure Lengend Snippet: Predicted binding scores of Peptides 1–4 towards Bcl-2. The values represent docking scores calculated using the MOE GBVI/WSA dG scoring function.

Article Snippet: The levels of Bax and Bcl-2 proteins were quantified using human Bax (Bcl-2 Associated X Protein) ELISA kit (Elabscience, Wuhan, China; E-EL-H0562) and human Bcl-2 (B-cell Leukemia/Lymphoma 2) ELISA kit (Elabscience, Wuhan, China; E-EL-H0114), respectively.

Techniques: Binding Assay, Docking Assay

Journal: Journal of Enzyme Inhibition and Medicinal Chemistry

Article Title: Rational structure-guided identification of a Bcl-2-targeting peptide with antiproliferative effects on colorectal cancer cells

doi: 10.1080/14756366.2026.2747402

Figure Lengend Snippet: Predicted binding modes of Peptides 1–4 in the Bcl-2 binding pocket. (A, C, E, and G) Close-up views of the predicted binding conformations of Peptides 1–4 in the Bcl-2 pocket. Bcl-2 is shown as a gray cartoon, with key pocket residues shown as sticks and labelled. Peptides are presented as stick models in distinct colours, and dashed lines denote putative hydrogen-bond interactions. (B, D, F, and H) Surface views of the corresponding peptide-occupied Bcl-2 binding pocket.

Article Snippet: The levels of Bax and Bcl-2 proteins were quantified using human Bax (Bcl-2 Associated X Protein) ELISA kit (Elabscience, Wuhan, China; E-EL-H0562) and human Bcl-2 (B-cell Leukemia/Lymphoma 2) ELISA kit (Elabscience, Wuhan, China; E-EL-H0114), respectively.

Techniques: Binding Assay

Journal: Journal of Enzyme Inhibition and Medicinal Chemistry

Article Title: Rational structure-guided identification of a Bcl-2-targeting peptide with antiproliferative effects on colorectal cancer cells

doi: 10.1080/14756366.2026.2747402

Figure Lengend Snippet: LigPlot + diagrams of the predicted interactions of Peptides 1–4 with Bcl-2. (A–D) Two-dimensional interaction maps of Peptides 1–4 bound to Bcl-2. The upper molecule in each panel represents the peptide, and the lower molecule represents Bcl-2. Hydrogen bonds are depicted as green dashed lines, whereas hydrophobic contacts are shown as red spoked arcs. Key residues involved in the predicted interactions are labelled.

Article Snippet: The levels of Bax and Bcl-2 proteins were quantified using human Bax (Bcl-2 Associated X Protein) ELISA kit (Elabscience, Wuhan, China; E-EL-H0562) and human Bcl-2 (B-cell Leukemia/Lymphoma 2) ELISA kit (Elabscience, Wuhan, China; E-EL-H0114), respectively.

Techniques:

Journal: Journal of Enzyme Inhibition and Medicinal Chemistry

Article Title: Rational structure-guided identification of a Bcl-2-targeting peptide with antiproliferative effects on colorectal cancer cells

doi: 10.1080/14756366.2026.2747402

Figure Lengend Snippet: Key intermolecular interactions between Peptides 1–4 and Bcl-2 predicted by molecular docking.

Article Snippet: The levels of Bax and Bcl-2 proteins were quantified using human Bax (Bcl-2 Associated X Protein) ELISA kit (Elabscience, Wuhan, China; E-EL-H0562) and human Bcl-2 (B-cell Leukemia/Lymphoma 2) ELISA kit (Elabscience, Wuhan, China; E-EL-H0114), respectively.

Techniques: Docking Assay

Journal: Journal of Enzyme Inhibition and Medicinal Chemistry

Article Title: Rational structure-guided identification of a Bcl-2-targeting peptide with antiproliferative effects on colorectal cancer cells

doi: 10.1080/14756366.2026.2747402

Figure Lengend Snippet: Molecular dynamics simulations of Bcl-2–Peptide-1 complex. (A) RMSD analysis derived from the MD trajectory of the Bcl-2–Peptide-1 complex. RMSD values were computed for the Bcl-2 subunit, bound Peptide-1, and the full complex from the same simulation trajectory. (B) RMSD distribution profiles of Bcl-2, Peptide-1, and the complex. (C) RMSF values of Bcl-2 residues in the complex. (D) Relative frequency distribution of RMSF values. (E) Time evolution of the Rg of the complex. (F) Relative frequency distribution of Rg values. (G) Number of intermolecular hydrogen bonds between Bcl-2 and Peptide-1 over time. (H) Time-dependent changes in total, hydrophobic, and hydrophilic SASA of the complex. (I) Relative frequency distributions of hydrophobic and hydrophilic SASA values. (J) Secondary structure changes of Bcl-2. (K) Secondary structure occupancy of Bcl-2 over the MD trajectory.

Article Snippet: The levels of Bax and Bcl-2 proteins were quantified using human Bax (Bcl-2 Associated X Protein) ELISA kit (Elabscience, Wuhan, China; E-EL-H0562) and human Bcl-2 (B-cell Leukemia/Lymphoma 2) ELISA kit (Elabscience, Wuhan, China; E-EL-H0114), respectively.

Techniques: Analysis, Derivative Assay

Journal: Journal of Enzyme Inhibition and Medicinal Chemistry

Article Title: Rational structure-guided identification of a Bcl-2-targeting peptide with antiproliferative effects on colorectal cancer cells

doi: 10.1080/14756366.2026.2747402

Figure Lengend Snippet: MM/GBSA energy decomposition analysis of the Bcl-2–Peptide-1 complex. (A) Contributions of the major energy terms to the predicted binding free energy, including van der Waals (VDWAALS), electrostatic (EEL), polar solvation (EGB), nonpolar solvation (ESURF), gas-phase interaction (GGAS), solvation free energy (GSOLV), and total binding free energy (TOTAL). (B) Per-residue decomposition of the predicted binding energy contributions of Bcl-2 residues at the peptide interface. (C) Per-residue decomposition of the individual interaction components, including van der Waals, electrostatic, polar solvation, and nonpolar solvation energies.

Article Snippet: The levels of Bax and Bcl-2 proteins were quantified using human Bax (Bcl-2 Associated X Protein) ELISA kit (Elabscience, Wuhan, China; E-EL-H0562) and human Bcl-2 (B-cell Leukemia/Lymphoma 2) ELISA kit (Elabscience, Wuhan, China; E-EL-H0114), respectively.

Techniques: Analysis, Binding Assay, Residue

Journal: Journal of Enzyme Inhibition and Medicinal Chemistry

Article Title: Rational structure-guided identification of a Bcl-2-targeting peptide with antiproliferative effects on colorectal cancer cells

doi: 10.1080/14756366.2026.2747402

Figure Lengend Snippet: Free energy landscape of the Bcl-2–Peptide-1 complex derived from molecular dynamics simulations. (A) Two-dimensional free energy contour map constructed using RMSD and Rg as reaction coordinates. (B) Corresponding three-dimensional free energy surface plot. The colour scale represents the relative free energy, with lower-energy regions indicating more populated and conformationally relatively populated conformational states sampled during the simulation.

Article Snippet: The levels of Bax and Bcl-2 proteins were quantified using human Bax (Bcl-2 Associated X Protein) ELISA kit (Elabscience, Wuhan, China; E-EL-H0562) and human Bcl-2 (B-cell Leukemia/Lymphoma 2) ELISA kit (Elabscience, Wuhan, China; E-EL-H0114), respectively.

Techniques: Derivative Assay, Construct

Journal: Journal of Enzyme Inhibition and Medicinal Chemistry

Article Title: Rational structure-guided identification of a Bcl-2-targeting peptide with antiproliferative effects on colorectal cancer cells

doi: 10.1080/14756366.2026.2747402

Figure Lengend Snippet: Effects of Peptide-1 on Bax and Bcl-2 expression in LoVo cells. (A) Relative mRNA expression levels of Bax and Bcl-2 determined by RT-qPCR after treatment with 1 and 10 μM Peptide-1. (B) Protein levels of Bax and Bcl-2 measured by ELISA following Peptide-1 treatment. *** p < 0.001 vs Control.

Article Snippet: The levels of Bax and Bcl-2 proteins were quantified using human Bax (Bcl-2 Associated X Protein) ELISA kit (Elabscience, Wuhan, China; E-EL-H0562) and human Bcl-2 (B-cell Leukemia/Lymphoma 2) ELISA kit (Elabscience, Wuhan, China; E-EL-H0114), respectively.

Techniques: Expressing, Quantitative RT-PCR, Enzyme-linked Immunosorbent Assay, Control

Journal: Cell Communication and Signaling : CCS

Article Title: Extracellular vesicles derived from Enterococcus faecalis : inflammatory activation does not require internalization

doi: 10.1186/s12964-026-02926-9

Figure Lengend Snippet: Isolation and characterization of Ef -EVs. A Growth curve of E. faecalis DSM 20478. The optical density (OD 600 ) was measured from E. faecalis cultures in BHI medium grown under static conditions at 37 °C. Results are shown as mean ± SD ( N = 3, n = 3). B Representative chromatogram obtained by protein concentration analysis of eluted fractions after size exclusion chromatography. Protein concentration was quantified by the BCA assay. The upper panel indicates the protein concentration of the first forty 1-mL fractions, indicating the elution peak corresponding to impurities (black area). The zoomed lower panel shows the protein concentration of the first 20 fractions, highlighting the EV-rich zone (red area). Results are shown as mean ± SD ( n = 3). C Representative size distribution of particles in the vesicle-richest fraction by Nanoparticle Tracking Analysis. D Representative cryo-TEM image of Ef -EVs in the vesicle-richest fraction (scale bar = 200 nm)

Article Snippet: To elucidate whether Ef -EVs induce NF-κB/AP-1 activation by TLR2 engagement, dTHP1-XBlue were pre-incubated for 1 h with fresh medium containing 1 μg/mL of neutralizing monoclonal antibodies (anti-hTLR2-IgA mAb, cat. no. maba2-htlr2-2, Invivogen) or human IgA2 control (cat. no. maba2-ctrl, Invivogen) before adding either Ef -EVs (7000 EVs/cell), ultrapure LPS from E. coli K12 (LPS, 1 ng/mL, cat.no. tlrl-peklps, Invivogen), or Pam 3 CSK 4 (1 ng/mL) in antibody-containing medium.

Techniques: Isolation, Protein Concentration, Size-exclusion Chromatography, BIA-KA

Journal: Cell Communication and Signaling : CCS

Article Title: Extracellular vesicles derived from Enterococcus faecalis : inflammatory activation does not require internalization

doi: 10.1186/s12964-026-02926-9

Figure Lengend Snippet: Ef -EVs activate the NF-κB/AP-1 pathways in human reporter macrophages via TLR2 signaling. A dTHP1-XBlue cells were treated with Ef -EVs (100 − 50,000 EVs/cell). LPS (100 ng/mL) was used as a positive control. B dTHP1-XBlue cells were treated with EVs derived from clinical E. faecalis bloodstream isolates (1000-10,000 EVs/cell). LPS (100 ng/mL) and Pam 3 CSK 4 (100 ng/mL) were used as positive controls. C-E) dTHP1-XBlue cells were pretreated with increasing concentrations (from 0.1 to 5 µg/mL) of anti-hTLR2-IgA mAb (dark pink) or human IgA2 control mAb (light pink) for 1 h. Subsequently, cells were treated with either (C) EVs (7000 EVs/cell), (D) Pam 3 CSK 4 (TLR2 ligand, 1 ng/mL), or (E) LPS (TLR4 ligand, 1 ng/mL) in the presence of antibodies for 24 h. Cells treated with cell culture medium supplemented only with Ef -EVs (7000 EVs/cell) in (C, blue), Pam 3 CSK 4 (1 ng/mL) in (D, dark blue), or LPS (1 ng/mL) in (E, red) were used as positive activating controls while cells treated with cell culture medium supplemented alone ( C - E , light green) were used as negative controls. NF-κB/AP-1 activation was measured as the activity of secreted SEAP and expressed as a normalized value relative to the positive controls. Data are shown as means ± SD of three independent experiments ( N = 3, n ≥ 3) and analyzed either by Kruskal-Wallis test followed by Dunn’s multiple comparison post hoc test in (A and B) or by two-way analysis of variance (ANOVA) followed by Šídák multiple comparison post hoc test in ( C - E )

Article Snippet: To elucidate whether Ef -EVs induce NF-κB/AP-1 activation by TLR2 engagement, dTHP1-XBlue were pre-incubated for 1 h with fresh medium containing 1 μg/mL of neutralizing monoclonal antibodies (anti-hTLR2-IgA mAb, cat. no. maba2-htlr2-2, Invivogen) or human IgA2 control (cat. no. maba2-ctrl, Invivogen) before adding either Ef -EVs (7000 EVs/cell), ultrapure LPS from E. coli K12 (LPS, 1 ng/mL, cat.no. tlrl-peklps, Invivogen), or Pam 3 CSK 4 (1 ng/mL) in antibody-containing medium.

Techniques: Positive Control, Derivative Assay, Control, Cell Culture, Activation Assay, Activity Assay, Comparison

Journal: Cell Communication and Signaling : CCS

Article Title: Extracellular vesicles derived from Enterococcus faecalis : inflammatory activation does not require internalization

doi: 10.1186/s12964-026-02926-9

Figure Lengend Snippet: TLR2 controls EV-induced immune activation but does not function as an endocytic receptor for EV uptake. dTHP1-XBlue cells were pretreated with anti-hTLR2-IgA mAb (1 µg/mL) or human IgA2 control mAb (1 µg/mL) for 1 h. Cells were then treated with DiI-labeled Ef -EVs (7000 EVs/cell) in the presence of antibodies for 4 and 24 h. Cells incubated in cell culture medium alone were used as negative controls. Cells treated with cell culture medium supplemented with DiI-labeled Ef -EVs (7000 EVs/cell) were used as positive activating controls. For EV internalization assays, mean fluorescence intensity (B and C, upper panel) and EV-positive cells (B and C, lower panel) were quantified after 4 ( A and B ) and 24 h ( A and C ) of EV treatment by measuring fluorescence intensity associated with DiI-labeled Ef -EVs on the PE channel. NF-κB/AP-1 activation in D was measured after 24 h of EV incubation as the activity of secreted SEAP and expressed normalized to the positive controls. Quantitative results are presented as mean ± SD ( N = 3, n = 3) and were analyzed by Kruskal-Wallis test followed by Dunn’s multiple comparison post hoc test

Article Snippet: To elucidate whether Ef -EVs induce NF-κB/AP-1 activation by TLR2 engagement, dTHP1-XBlue were pre-incubated for 1 h with fresh medium containing 1 μg/mL of neutralizing monoclonal antibodies (anti-hTLR2-IgA mAb, cat. no. maba2-htlr2-2, Invivogen) or human IgA2 control (cat. no. maba2-ctrl, Invivogen) before adding either Ef -EVs (7000 EVs/cell), ultrapure LPS from E. coli K12 (LPS, 1 ng/mL, cat.no. tlrl-peklps, Invivogen), or Pam 3 CSK 4 (1 ng/mL) in antibody-containing medium.

Techniques: Activation Assay, Control, Labeling, Incubation, Cell Culture, Fluorescence, Activity Assay, Comparison

Journal: Cell Communication and Signaling : CCS

Article Title: Extracellular vesicles derived from Enterococcus faecalis : inflammatory activation does not require internalization

doi: 10.1186/s12964-026-02926-9

Figure Lengend Snippet: Routes of Ef -EV uptake. A and B ) dTHP1-XBlue cells were pretreated with pharmacological endocytosis inhibitors for 30 min. Afterward, cells were incubated with DiI-labeled Ef -EVs (7000 EVs/cell) in the presence of inhibitors for 4 h. Mean fluorescence intensity (B, upper panel) and EV-positive cells (B, lower panel) were quantified by measuring fluorescence intensity associated with DiI-labeled Ef -EVs on the PE channel. Cells treated by EVs dispersed in cell culture medium or medium containing DMSO (1% v/v) were used as positive uptake controls. C ) dTHP1-XBlue cells were pretreated with dynasore at 100 µM for 30 min. Afterward, cells were incubated with Ef -EVs (7000 EVs/cell) in the presence of dynasore at 100 µM for 24 h. Cells treated with cell culture medium supplemented only with Ef -EVs (7000 EVs/cell) were used as positive activating controls. NF-κB/AP-1 activation was measured as the activity of secreted SEAP and expressed as a normalized value relative to the positive control. Quantitative results are presented as mean ± SD of three independent experiments ( N = 3, n ≥ 3) and were analyzed by Kruskal-Wallis test followed by Dunn’s multiple comparison post hoc test

Article Snippet: To elucidate whether Ef -EVs induce NF-κB/AP-1 activation by TLR2 engagement, dTHP1-XBlue were pre-incubated for 1 h with fresh medium containing 1 μg/mL of neutralizing monoclonal antibodies (anti-hTLR2-IgA mAb, cat. no. maba2-htlr2-2, Invivogen) or human IgA2 control (cat. no. maba2-ctrl, Invivogen) before adding either Ef -EVs (7000 EVs/cell), ultrapure LPS from E. coli K12 (LPS, 1 ng/mL, cat.no. tlrl-peklps, Invivogen), or Pam 3 CSK 4 (1 ng/mL) in antibody-containing medium.

Techniques: Incubation, Labeling, Fluorescence, Cell Culture, Activation Assay, Activity Assay, Positive Control, Comparison

Journal: Cell Communication and Signaling : CCS

Article Title: Extracellular vesicles derived from Enterococcus faecalis : inflammatory activation does not require internalization

doi: 10.1186/s12964-026-02926-9

Figure Lengend Snippet: Ef -EVs are internalized by primary human macrophages and modulate their morphology. A and B ) HMDMs were incubated with DiI-labeled Ef -EVs (30,000 EVs/cell) for 24 and 48 h. Mean fluorescence intensity (B, left panel) and EV-positive cells (B, right panel) were quantified by measuring fluorescence intensity associated with DiI-labeled Ef -EVs on the PE channel. Results are presented as mean ± SD of three individual donors ( N = 3, n = 1). C Representative images of macrophages treated with Ef -EVs (1000-10,000 EVs/cell) for 24 h (scale bar in full micrograph = 400 μm, scale bar in zoomed micrograph = 100 μm). D X-fold change of roundness compared to medium-treated cells (0 EVs/cell). Statistical comparisons of two groups in B were performed by Mann-Whitney test. Results in D were analyzed by Kruskal-Wallis test followed by Dunn’s multiple comparison post hoc test

Article Snippet: To elucidate whether Ef -EVs induce NF-κB/AP-1 activation by TLR2 engagement, dTHP1-XBlue were pre-incubated for 1 h with fresh medium containing 1 μg/mL of neutralizing monoclonal antibodies (anti-hTLR2-IgA mAb, cat. no. maba2-htlr2-2, Invivogen) or human IgA2 control (cat. no. maba2-ctrl, Invivogen) before adding either Ef -EVs (7000 EVs/cell), ultrapure LPS from E. coli K12 (LPS, 1 ng/mL, cat.no. tlrl-peklps, Invivogen), or Pam 3 CSK 4 (1 ng/mL) in antibody-containing medium.

Techniques: Incubation, Labeling, Fluorescence, MANN-WHITNEY, Comparison

Journal: Cell Communication and Signaling : CCS

Article Title: Extracellular vesicles derived from Enterococcus faecalis : inflammatory activation does not require internalization

doi: 10.1186/s12964-026-02926-9

Figure Lengend Snippet: Ef -EVs modulate gene expression and metabolic activity in primary human macrophages. A and B ) HMDMs were incubated with Ef -EVs at different concentrations (1000-10,000 EVs/cell) for 24 (A) and 48 h (B). Data are presented as frequency distributions, median, and quartiles of gene expression results from three individual donors ( N = 3, n = 3) and normalized to medium-treated cells (0 EVs/cell) as control. C and D) HMDMs were treated with Ef -EVs (10,000 and 50,000 EVs/cell) or Pam 3 CSK 4 (10 ng/mL) for 24 h. Cells incubated in cell culture medium alone served as untreated control. C Normalized ECAR values were monitored after injections of glucose, oligomycin, and 2-DG, according to the glycolysis stress test. D Glycolytic activity is shown as the x-fold change of untreated control regarding the normalized ECAR values in glycolysis. Results C and D are shown as mean ± SEM of three individual donors ( N = 3, n = 6). Results were analyzed by Kruskal-Wallis test followed by Dunn’s multiple comparison post hoc test

Article Snippet: To elucidate whether Ef -EVs induce NF-κB/AP-1 activation by TLR2 engagement, dTHP1-XBlue were pre-incubated for 1 h with fresh medium containing 1 μg/mL of neutralizing monoclonal antibodies (anti-hTLR2-IgA mAb, cat. no. maba2-htlr2-2, Invivogen) or human IgA2 control (cat. no. maba2-ctrl, Invivogen) before adding either Ef -EVs (7000 EVs/cell), ultrapure LPS from E. coli K12 (LPS, 1 ng/mL, cat.no. tlrl-peklps, Invivogen), or Pam 3 CSK 4 (1 ng/mL) in antibody-containing medium.

Techniques: Gene Expression, Activity Assay, Incubation, Control, Cell Culture, Comparison

Journal: Cell Communication and Signaling : CCS

Article Title: Extracellular vesicles derived from Enterococcus faecalis : inflammatory activation does not require internalization

doi: 10.1186/s12964-026-02926-9

Figure Lengend Snippet: Ef -EVs are internalized by primary human endothelial cells and modulate their gene expression. A and B ) HUVECs were incubated with DiI-labeled Ef -EVs (30,000 EVs/cell) for 24 and 48 h. Mean fluorescence intensity (B, left panel) and EV-positive cells (B, right panel) were quantified by measuring fluorescence intensity associated with DiI-labeled Ef -EVs on the PE channel. Results are presented as mean ± SD of three individual donors ( N = 3, n = 1). C and D ) HUVECs were incubated with Ef -EVs at different concentrations (1000-10,000 EVs/cell) for 24 (C) and 48 h (D). Data are presented as frequency distributions, median, and quartiles of gene expression results from three individual donors ( N = 3, n = 3) and normalized to medium-treated cells (0 EVs/cell) as control. Statistical comparisons of two groups in B were performed by Mann-Whitney test. Results in C and D were analyzed by Kruskal-Wallis test followed by Dunn’s multiple comparison post hoc test

Article Snippet: To elucidate whether Ef -EVs induce NF-κB/AP-1 activation by TLR2 engagement, dTHP1-XBlue were pre-incubated for 1 h with fresh medium containing 1 μg/mL of neutralizing monoclonal antibodies (anti-hTLR2-IgA mAb, cat. no. maba2-htlr2-2, Invivogen) or human IgA2 control (cat. no. maba2-ctrl, Invivogen) before adding either Ef -EVs (7000 EVs/cell), ultrapure LPS from E. coli K12 (LPS, 1 ng/mL, cat.no. tlrl-peklps, Invivogen), or Pam 3 CSK 4 (1 ng/mL) in antibody-containing medium.

Techniques: Gene Expression, Incubation, Labeling, Fluorescence, Control, MANN-WHITNEY, Comparison