Journal: Viruses

Article Title: Downregulation of miRNA-26a by HIV-1 Enhances CD59 Expression and Packaging, Impacting Virus Susceptibility to Antibody-Dependent Complement-Mediated Lysis

doi: 10.3390/v16071076

Figure Lengend Snippet: CD59 is predicted to be regulated, in infected cells, by three miRNAs. ( A ) Example of genes for which expression is dysregulated in infected cells (GFP-pos) compared to uninfected cells and that are relevant in the context of HIV-1 infection based on the current literature. The FC values indicated correspond to the values obtained based on the RNA-seq analysis. ( B ) Graph representing the upregulated gene ontology pathways (from B, left panel), which include CD59. ( C ) Shown are the 10 most downregulated miRNAs in GFP-pos cells compared to uninfected, ranked from most to least decreased. The FC values indicated correspond to the values based on the RNA-seq analysis. ( D ) MiRNAs-21, -26a and 29a potentially target many dysregulated genes in GFP-pos cells, including CD59. Cross-referencing of miRNA and transcriptomic RNA data was performed using online databases (mirDIP, http://ophid.utoronto.ca/mirDIP/ (accessed on 26 January 2024)).

Article Snippet: The following Abs were used in flow cytometry assays: BV421 anti-human CCR5 (Biolegend, #359118), PE/Cyanine7 anti-human CD4 (Biolegend, #317414) and PE anti-human CD59 (Miltenyi, #130-120-048), as well as its isotype control (Miltenyi, #130-113-438).

Techniques: Infection, Expressing, RNA Sequencing

Journal: Viruses

Article Title: Downregulation of miRNA-26a by HIV-1 Enhances CD59 Expression and Packaging, Impacting Virus Susceptibility to Antibody-Dependent Complement-Mediated Lysis

doi: 10.3390/v16071076

Figure Lengend Snippet: Validation of the differential expression of predicted CD59-targeting miRNAs (miRNAs-21, miRNA-26a and miRNA-29a) and CD59 upon HIV-1 infection. Expression levels of miRNAs-21, -26a and -29a ( A ) and CD59 mRNA ( B ) in uninfected and productively infected (GFP-pos) CD4 + T cells (n = 6) were measured via real-time qPCR. Shown are the mean fold-changes compared to uninfected cells (in gray, which is set at 1). Error bars represent the standard error of the mean (SEM). Statistical significance was determined using the nonparametric Mann–Whitney’s test, values: ** p < 0.01. ( C ) CD59 cell-surface expression was evaluated via flow cytometry, and the mean fluorescent intensity (MFI) was compared between uninfected and infected CD4 + T cells (GFP-positive) obtained from healthy blood donors. The left panel is representative data from cells from one donor, the middle panel is the MFI of cells from three donors and the right panel is normalized data (as compared to uninfected cells). Error bars represent the SEM (n = 3). Mann–Whitney’s test, values: * p = 0.05.

Article Snippet: The following Abs were used in flow cytometry assays: BV421 anti-human CCR5 (Biolegend, #359118), PE/Cyanine7 anti-human CD4 (Biolegend, #317414) and PE anti-human CD59 (Miltenyi, #130-120-048), as well as its isotype control (Miltenyi, #130-113-438).

Techniques: Biomarker Discovery, Quantitative Proteomics, Infection, Expressing, Flow Cytometry

Journal: Viruses

Article Title: Downregulation of miRNA-26a by HIV-1 Enhances CD59 Expression and Packaging, Impacting Virus Susceptibility to Antibody-Dependent Complement-Mediated Lysis

doi: 10.3390/v16071076

Figure Lengend Snippet: CD59 mRNA is a target of miRNA-26a. ( A ) CD59 mRNA levels were measured in miRNAs-21, -26a and -29a mimics or control-nucleofected primary CD4 + T cells via real-time qPCR. Shown is the mean fold-change compared to control transfected cells (in gray, which is set at 1) (n = 4). Error bars represent the SEM. Statistical significance was determined using the nonparametric Kruskal Wallis test, values: ** p < 0.01. ( B ) CD59 surface expression was evaluated in miRNAs-21 and -26a mimics or control-nucleofected primary CD4 + T cells via flow cytometry. Shown is the cell surface expression of CD59 from CD4 + T cells of four blood donors (normalized to CTRL, which was set to 100%) with a representative result on the left (MFI are shown). Error bars represent the SEM. Statistical significance was determined using the nonparametric Kruskal Wallis test, values: * p < 0.05. ( C ) The MIR-Report system was used to validate whether the CD59 3′ UTR was a target of miRNA-26a. MiRNA blue nucleotides represent those predicted to interact with the CD59 3′ UTR. WT or mutated (substituted nucleotides in green) fragments of the 3′ UTR encompassing the predicted sequences recognized by miRNA-26a were fused to the F-Luciferase (F-Luc) gene. ( D ) HEK-293T cells were transfected with miRNA-26 mimics, the reporter plasmids with the indicated fragment of the WT (in yellow) or mutated (in black) 3′ UTR and a Renilla-Luciferase (R-Luc) normalizing control. Following cell lysis, relative light units (RLUs) were measured, and F-Luc was normalized to the negative control (in grey, which is set to 1). Error bars represent the SEM. Statistical significance was determined using the nonparametric Kruskal Wallis test, values: * p < 0.05.

Article Snippet: The following Abs were used in flow cytometry assays: BV421 anti-human CCR5 (Biolegend, #359118), PE/Cyanine7 anti-human CD4 (Biolegend, #317414) and PE anti-human CD59 (Miltenyi, #130-120-048), as well as its isotype control (Miltenyi, #130-113-438).

Techniques: Control, Transfection, Expressing, Flow Cytometry, Luciferase, Lysis, Negative Control

Journal: Viruses

Article Title: Downregulation of miRNA-26a by HIV-1 Enhances CD59 Expression and Packaging, Impacting Virus Susceptibility to Antibody-Dependent Complement-Mediated Lysis

doi: 10.3390/v16071076

Figure Lengend Snippet: Decreased packaging of CD59 in released virions enhances their susceptibility to ADCML. ( A ) Detection of CD59 incorporation into virions produced from HIV-1-infected CEM-CD59_control or CEM-CD59_KO cells via an Ab capture assay. Equal amounts of virus released from each cell line were analyzed. Data shown indicate the mean levels of CD59-containing virus, as measured via ELISA for p24 (pg/mL), following the lysis of anti-CD59 bead-associated virus (background capture with the isotypic control was subtracted). Error bars represent the SEM. Statistical significance was determined using the nonparametric Mann–Whitney’s test, values: * p < 0.05. ( B ) Shown are the normalized total HIV genomic equivalents of PGT121-treated viruses (with either NHS or HIHS) from CEM-CD59_control or CEM-CD59_KO infected cells as measured via real-time qPCR, following the reverse transcription of viral RNA. Values are normalized relative to the mean HIHS condition, which is set at 100%. Error bars represent the SEM. Statistical significance was determined using the nonparametric Mann–Whitney’s test, values: ** p < 0.01. In all conditions, equal amounts of virus released from each cell line were analyzed. See also .

Article Snippet: The following Abs were used in flow cytometry assays: BV421 anti-human CCR5 (Biolegend, #359118), PE/Cyanine7 anti-human CD4 (Biolegend, #317414) and PE anti-human CD59 (Miltenyi, #130-120-048), as well as its isotype control (Miltenyi, #130-113-438).

Techniques: Produced, Infection, Control, Virus, Enzyme-linked Immunosorbent Assay, Lysis, Reverse Transcription

Journal: Viruses

Article Title: Downregulation of miRNA-26a by HIV-1 Enhances CD59 Expression and Packaging, Impacting Virus Susceptibility to Antibody-Dependent Complement-Mediated Lysis

doi: 10.3390/v16071076

Figure Lengend Snippet: Enhanced expression of miRNA-26a during HIV-1 infection renders released virions more susceptible to ADCML. ( A ) Primary CD4 + T cells were nucleofected with miRNA-26a or miRNA-control mimics for 72 h and infected with HIV-1 for 48 h (n = 3). Data shown indicate the total HIV-1 produced (as genomic equivalents of HIV-1) from infected cells, as measured via real-time qPCR, following the reverse transcription of viral RNA. Error bars represent the SEM. ( B ) Detection and quantification of CD59-containing virus particles using an Ab-capture assay of virions produced by infected cells transfected with miRNA-26a or negative control mimics. The left panel indicates the mean level of CD59-containing virus as determined via p24 ELISA (pg/mL) after the lysis of virus captured with CD59-antibody-conjugated beads (the capture assay background obtained with the isotypic Ab control was subtracted). The right panel indicates the mean level of CD59-containing virus normalized to the value obtained with the control mimic condition (set to 100%). In all conditions, equal amounts of virus were analyzed. Error bars represent the SEM. Statistical significance was determined using the nonparametric Mann–Whitney’s test, values: ** p < 0.01. ( C ) Shown are the normalized total HIV-1 genomic equivalents of PGT-121-treated viruses from infected cells transfected with either miRNA-26a or negative control mimics, as measured via real-time qPCR, following the reverse transcription of viral RNA. Values are normalized relative to the means of those obtained with HIHS-treated viruses, which were set to 100%. Error bars represent the SEM. Statistical significance was determined using the nonparametric Mann–Whitney’s test, values: ** p < 0.01. ( D ) Shown are the normalized total HIV-1 genomic equivalents of Ab-treated viruses from infected cells transfected with miRNA-26a or negative control mimics, as measured via real-time qPCR, following the reverse transcription of viral RNA. Values are normalized relative to the means of those obtained with HIHS-treated viruses, which were set to 100%. Abs were purified from the sera of viremic individuals #163 (left panel) or #497 (right panel). Error bars represent the SEM. Statistical significance was determined using the nonparametric Mann–Whitney’s test, values: * p < 0.05, ** p < 0.01. In all conditions, equal amounts of virus were analyzed. See also .

Article Snippet: The following Abs were used in flow cytometry assays: BV421 anti-human CCR5 (Biolegend, #359118), PE/Cyanine7 anti-human CD4 (Biolegend, #317414) and PE anti-human CD59 (Miltenyi, #130-120-048), as well as its isotype control (Miltenyi, #130-113-438).

Techniques: Expressing, Infection, Control, Produced, Reverse Transcription, Virus, Transfection, Negative Control, Enzyme-linked Immunosorbent Assay, Lysis, Purification

Journal: PLoS ONE

Article Title: Apolipoprotein J/Clusterin in Human Erythrocytes Is Involved in the Molecular Process of Defected Material Disposal during Vesiculation

doi: 10.1371/journal.pone.0026033

Figure Lengend Snippet: (A, B) TEM immunogold localization of sCLU in RBCs membrane protrusions (A) and vesicles (ves) (B) collected from fresh units of stored RBCs (N = 2, young healthy donors). Solid or dashed arrows indicate sCLU immunogold localization at the periphery or the cytosol of the vesicles, respectively. (C) Representative immunoblot analysis of RBCs-derived purified vesicles (N = 2) probed with either polyclonal anti-sCLU or with monoclonal anti-Band 3 antibodies. Molecular weight markers are indicated to the right of the blot. Bars in (A), (B), 100 nm.

Article Snippet: The polyclonal antibody against CD59 was obtained from R&D Systems (AF 1987).

Techniques: Membrane, Western Blot, Derivative Assay, Purification, Molecular Weight

Journal: PLoS ONE

Article Title: Apolipoprotein J/Clusterin in Human Erythrocytes Is Involved in the Molecular Process of Defected Material Disposal during Vesiculation

doi: 10.1371/journal.pone.0026033

Figure Lengend Snippet: Purified RBCs membranes from healthy subjects (N = 6) were lysed in NP-40 and lysates were immunoprecipitated (IP) with polyclonal antibodies against sCLU, Band 3, stomatin or normal serum (control). Immunoprecipitates were immunoblotted (IB) under reducing conditions for sCLU (A 1 , upper panel), Band 3 (A 1 , middle panel), CD59 (A 1 , lower panel) and Hb (A 3 ); shown IPs are representatives from two independent experiments. (A 2 ) CLSM co-immunolocalization of the sCLU and Band 3 proteins at the RBCs plasma membrane. Cells were co-stained with anti-Band 3 monoclonal (green; upper panel) and anti-sCLU polyclonal antibodies (red; lower panel). Captured images were merged to reveal co-distribution sites (yellow; lower panel, arrows). Bars, 3 µm. (B) Anti-dinitrophenylhydrazone (DNP) immunoblotting of sCLU, Band 3, and control (IgGs) immunoprecipitates for the detection of co-immunoprecipitated carbonylated proteins (arrows) in 2,4-dinitrophenylhydrazine-modified (OX) or unmodified protein material.

Article Snippet: The polyclonal antibody against CD59 was obtained from R&D Systems (AF 1987).

Techniques: Purification, Immunoprecipitation, Control, Clinical Proteomics, Membrane, Staining, Western Blot, Modification

Journal: PLoS ONE

Article Title: Apolipoprotein J/Clusterin in Human Erythrocytes Is Involved in the Molecular Process of Defected Material Disposal during Vesiculation

doi: 10.1371/journal.pone.0026033

Figure Lengend Snippet: Erythrocytic sCLU localizes at both sides of the plasma membrane in association with non-cytoskeletal areas, as well as in the cytosol (see also, Antonelou et al., accompanying paper). At the intracellular side of the RBCs membrane sCLU may bind Band 3, Hb and/or other cytoskeleton-free membrane portions. On the other hand, the sCLU that localizes at the extracellular side of the RBCs membrane can attach to membrane by binding to Band 3, CD59, plasma membrane IgGs or to an currently unknown sCLU-specific receptor. Physiological in vivo or ex vivo RBCs senescence (1) is associated with cytosol, cytoskeleton and membrane structural alterations, including Band 3 modifications, increased membrane binding of IgGs, proteolysis, protein aggregation and increased oxidation defects. Vesiculation (2), a self-protective mechanism of mammalian erythrocytes, removes oxidized proteins and aggregates from both plasma membrane and cytosol thereby postponing the untimely elimination of otherwise healthy erythrocytes. This process takes place through the entire in vivo or ex vivo lifespan of RBCs and is functionally connected to the release of sCLU-, Band 3-, CD59-, Hb- and IgGs-containing vesicles. We propose that vesicular sCLU by following its membrane linkers (e.g. Band 3) or other unknown cytosolic interacting proteins assists via its chaperone function in the disposal of non-functional or death signalling effective material from RBCs.

Article Snippet: The polyclonal antibody against CD59 was obtained from R&D Systems (AF 1987).

Techniques: Clinical Proteomics, Membrane, Binding Assay, In Vivo, Ex Vivo, Functional Assay

Journal: Foods

Article Title: Sea Buckthorn Pericarp Flavonoids Improve Diet-Induced Hyperlipidemia via Coordinated Modulation of Hepatic Lipid Metabolism and Gut Microbiota

doi: 10.3390/foods15061049

Figure Lengend Snippet: TFSP modulates the expression of ACC, FAS, CPT-1α, PPARα and ATGL proteins in the livers of HFD mice. n = 6 per group. Data are presented as mean ± SD. Different letters above bars indicate statistically significant differences ( p < 0.05) by one-way ANOVA followed by LSD post hoc test.

Article Snippet: Peroxisome proliferator-activated receptor alpha (PPARα) primary antibody (Cat. No. A00600-2), carnitine palmitoyltransferase-1 alpha (CPT-1α) primary antibody (Cat. No. A00917-3), acetyl-CoA carboxylase (ACC) primary antibody (Cat. No. M01802-2), fatty acid synthase (FAS) primary antibody (Cat. No. BA0484), adipose triglyceride lipase (ATGL) primary antibody (Cat. No. A01800-1), and GAPDH primary antibody (Cat. No. BM1623) were obtained from BOSTER Biological Technology Co., Ltd. (Wuhan, China).

Techniques: Expressing

Journal: Carbohydrate polymers

Article Title: Stability and bioactivity of chitosan as a transfection agent in primary human cell cultures: A case for chitosan-only controls.

doi: 10.1016/j.carbpol.2017.10.021

Figure Lengend Snippet: Fig. 1. Plasmid DNA containing human CD59 on a high-yield promoter (pDNA, A) was incorporated into chitosan microparticles (pCsM, B). Both pCsM and microparticles without pDNA (CsM, C) were precipitated from chitosan polymers (Cs, D). All chitosan treatments were prepared and delivered in mildly acidic Vehicle (pH 5.6, E).

Article Snippet: TrueClone cDNA plasmids containing human CD59 (Origene, Rockville, Maryland) were expanded in Alpha-Gold competent Escherichia coli bacteria (Origene).

Techniques: Plasmid Preparation

Journal: Carbohydrate polymers

Article Title: Stability and bioactivity of chitosan as a transfection agent in primary human cell cultures: A case for chitosan-only controls.

doi: 10.1016/j.carbpol.2017.10.021

Figure Lengend Snippet: Fig. 4. Mean fluorescent intensity from flow cytometry was used to approximate average CD59 expression vSMC (A). CD59 is transiently depressed by pCsM, CsM and Cs (B, p ≤0.001) but recovers to baseline by 24 h despite the presence of Vehicle (C). In the absence of chitosan, Vehicle decreases CD59 expression.

Article Snippet: TrueClone cDNA plasmids containing human CD59 (Origene, Rockville, Maryland) were expanded in Alpha-Gold competent Escherichia coli bacteria (Origene).

Techniques: Cytometry, Expressing

Journal: Carbohydrate polymers

Article Title: Stability and bioactivity of chitosan as a transfection agent in primary human cell cultures: A case for chitosan-only controls.

doi: 10.1016/j.carbpol.2017.10.021

Figure Lengend Snippet: Fig. 5. Flow cytometry gates to determine Live CD59-positive vSMC were set based on living and EtOH-killed controls (A). Chitosan (pCsM, CsM, Cs) initially decreased the number of CD59-positive cells (B, p ≤0.001), an effect that was rapidly, potently and durably reversed, especially in the case of Cs (C, *p ≤0.01, §p ≤0.05).

Article Snippet: TrueClone cDNA plasmids containing human CD59 (Origene, Rockville, Maryland) were expanded in Alpha-Gold competent Escherichia coli bacteria (Origene).

Techniques: Flow Cytometry

Journal: Carbohydrate polymers

Article Title: Stability and bioactivity of chitosan as a transfection agent in primary human cell cultures: A case for chitosan-only controls.

doi: 10.1016/j.carbpol.2017.10.021

Figure Lengend Snippet: Fig. 6. CD59 mRNA was elevated after treatment with pDNA (p < 0.05) and pCsM (p < 0.01) but down-regulated by treatment with Vehicle (p < 0.05).

Article Snippet: TrueClone cDNA plasmids containing human CD59 (Origene, Rockville, Maryland) were expanded in Alpha-Gold competent Escherichia coli bacteria (Origene).

Techniques:

Journal: bioRxiv

Article Title: A selective alternative pathway complement inhibitor for treatment of paroxysmal nocturnal hemoglobinuria

doi: 10.1101/2024.06.23.600249

Figure Lengend Snippet: Contrary to the antigen-driven CP and LP, the AP is initiated spontaneously by hydrolysis of C3 (“tick-over”), subsequently forming the AP fluid phase C3 convertase. Newly generated C3b is deposited on pathogen surfaces where it nucleates formation of the AP C3 convertase, amplifying the complement activity. Binding of an additional C3b molecule to the C3 convertase forms the C5 convertase, initiating C5 cleavage and thereby progression to the terminal pathway, culminating in the formation of the MAC. On healthy erythrocytes, CD55 inhibits formation and decreases stability of the C3 convertase of AP and CP/LP. For simplicity, the inhibition of the CP/LP C3 convertase is only shown illustratively and a visualization of accelerated decay of the convertases has been omitted. CD59 exerts its inhibitory function by preventing incorporation of MAC components C8 and C9. On PNH erythrocytes devoid of CD55, C3b is readily deposited, and the complement activity is amplified, resulting in progression to the terminal pathway. A lack of CD59 fails to prevent formation of the MAC, resulting in hemolysis. Abbreviations: RBC - red blood cell, Ba - factor B fragment a, Bb - factor B fragment b, fD – factor D, MAC – membrane attack complex.

Article Snippet: Following the incubation period (37°C, 1 hour), RBCs were washed twice with ice cold RBC staining buffer (PBS supplemented with 0.2% BSA) before staining on ice with anti-CD59 AF405 monoclonal antibody (FAB1987V, R&D Systems, 5 ng/μL final concentration) and anti-C3c-FITC polyclonal antibody (ab4212, Abcam, 1:300 final) for 1 h. After the staining, unbound antibodies were removed by washing the erythrocytes with RBC staining buffer twice.

Techniques: Generated, Activity Assay, Binding Assay, Inhibition, Amplification, Membrane

Journal: bioRxiv

Article Title: A selective alternative pathway complement inhibitor for treatment of paroxysmal nocturnal hemoglobinuria

doi: 10.1101/2024.06.23.600249

Figure Lengend Snippet: Flow cytometry analysis of hemolysis and C3b deposition on PNH patient erythrocytes. Two-parameter density plots, divided into four quadrants, illustrate presence of CD59 and C3c on single, intact RBCs. Normal cells (CD59 + ) are shown in Q1+Q2, PNH phenotype cells (CD59 - ) in Q3+Q4. C3b-positive cells are found in Q2+Q4. The percentages of RBCs in each quadrant are indicated. Incubation in acidified human serum (aNHS, triggering AP activation) leads to lysis of most CD59 - cells. Hemolysis of erythrocytes incubated in presence of SH-01 and eculizumab is effectively reduced to baseline levels.

Article Snippet: Following the incubation period (37°C, 1 hour), RBCs were washed twice with ice cold RBC staining buffer (PBS supplemented with 0.2% BSA) before staining on ice with anti-CD59 AF405 monoclonal antibody (FAB1987V, R&D Systems, 5 ng/μL final concentration) and anti-C3c-FITC polyclonal antibody (ab4212, Abcam, 1:300 final) for 1 h. After the staining, unbound antibodies were removed by washing the erythrocytes with RBC staining buffer twice.

Techniques: Flow Cytometry, Incubation, Activation Assay, Lysis

Journal: Clinical and Experimental Medicine

Article Title: CD59 silencing enhances doxorubicin sensitivity in DLBCL cells and is associated with poor prognosis in patients treated with CHOP regimen

doi: 10.1007/s10238-026-02134-2

Figure Lengend Snippet: Validation of CD59 knock-down in DLBCL cell lines. ( A ) Representative immunoblots showing CD59 protein levels in SU-DHL-4 and U2932 cell lines transfected with three distinct CD59-shRNA constructs or control vectors. β-actin served as the loading control. ( B and C ) Quantitative analysis of relative CD59 mRNA (by qRT-PCR) and protein (by densitometry) levels in SU-DHL-4 (B) and U2932 (C) cells. Data are presented as mean ± SD and normalized to the blank control group.** p < 0.01; *** p < 0.001

Article Snippet: Anti-CD59 antibody (BM5003), RIPA lysis buffer (AR0105), and protease inhibitor (AR1178) were sourced from Boster Biological Technology Co., Ltd.

Techniques: Biomarker Discovery, Knockdown, Western Blot, Transfection, shRNA, Construct, Control, Quantitative RT-PCR

Journal: Clinical and Experimental Medicine

Article Title: CD59 silencing enhances doxorubicin sensitivity in DLBCL cells and is associated with poor prognosis in patients treated with CHOP regimen

doi: 10.1007/s10238-026-02134-2

Figure Lengend Snippet: CD59 knock-down promotes G0/G1 cell-cycle arrest in SU-DHL-4 and U2932 cells. ( A and B ) Representative propidium-iodide histograms for wild-type and shCD59 transduced SU-DHL-4 (A) and U2932 (B) cells under indicated treatments. ( C ) Bar graph summarizing the proportions of cells in G0/G1, S, and G2/M phases for SU-DHL-4 (left) and U2932 (right) cell lines. * p < 0.05, ** p < 0.01, *** p < 0.001

Article Snippet: Anti-CD59 antibody (BM5003), RIPA lysis buffer (AR0105), and protease inhibitor (AR1178) were sourced from Boster Biological Technology Co., Ltd.

Techniques: Knockdown

Journal: Clinical and Experimental Medicine

Article Title: CD59 silencing enhances doxorubicin sensitivity in DLBCL cells and is associated with poor prognosis in patients treated with CHOP regimen

doi: 10.1007/s10238-026-02134-2

Figure Lengend Snippet: CD59 knock-down enhances drug-induced apoptosis in DLBCL cell lines. (A-B) Representative Annexin V-PE/7-AAD flow-cytometry plots for wild-type and shCD59 transduced SU-DHL-4 ( A ) and U2932 ( B ) cells under the indicated treatments. ( C ) Bar-graph summarizing the percentage of early + late apoptotic cells. ns p > 0.05, * p < 0.05, ** p < 0.01*** p < 0.001

Article Snippet: Anti-CD59 antibody (BM5003), RIPA lysis buffer (AR0105), and protease inhibitor (AR1178) were sourced from Boster Biological Technology Co., Ltd.

Techniques: Knockdown, Flow Cytometry

Journal: Clinical and Experimental Medicine

Article Title: CD59 silencing enhances doxorubicin sensitivity in DLBCL cells and is associated with poor prognosis in patients treated with CHOP regimen

doi: 10.1007/s10238-026-02134-2

Figure Lengend Snippet: Representative immunohistochemical staining of CD59 in DLBCL tissue specimens. Images show CD59 expression at both 200× (upper panels) and 400× (lower panels) magnification. Representative fields were classified as negative, weakly positive, and positive for CD59 expression. Scale bars: 50 μm (200×) and 20 μm (400×)

Article Snippet: Anti-CD59 antibody (BM5003), RIPA lysis buffer (AR0105), and protease inhibitor (AR1178) were sourced from Boster Biological Technology Co., Ltd.

Techniques: Immunohistochemical staining, Staining, Expressing

Journal: Clinical and Experimental Medicine

Article Title: CD59 silencing enhances doxorubicin sensitivity in DLBCL cells and is associated with poor prognosis in patients treated with CHOP regimen

doi: 10.1007/s10238-026-02134-2

Figure Lengend Snippet: Progression-free (PFS) and overall survival (OS) analyses based on CD59 expression status in DLBCL. (A and B) Kaplan-Meier curves representing PFS ( A ) and OS ( B ) for 36 CHOP-treated patients stratified by CD59 immunostaining. (C and D) Kaplan-Meier curves representing PFS ( C ) and OS ( D ) for 67 patients who received R-CHOP. (E and F) Kaplan-Meier curves representing PFS ( E ) and OS ( F ) for entire cohort according to CD59 expression. P-values were calculated with the log-rank test

Article Snippet: Anti-CD59 antibody (BM5003), RIPA lysis buffer (AR0105), and protease inhibitor (AR1178) were sourced from Boster Biological Technology Co., Ltd.

Techniques: Expressing, Immunostaining