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Proteintech primary antibodies for ptbp1
Primary Antibodies For Ptbp1, supplied by Proteintech, used in various techniques. Bioz Stars score: 94/100, based on 73 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/anti+ptbp1/PTBP1+Antibody/pm42894639-158-0-5
Average 94 stars, based on 73 article reviews

primary antibodies for ptbp1 - by Bioz Stars, 2026-11

94/100 stars

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Article Title: LncRNA SNHG1 promotes the development of preeclampsia by interacting with PTBP1 and modulating NGFR mRNA stability.
Article Snippet: Background: Preeclampsia (PE) is a serious complication of pregnancy associated with trophoblast dysfunction accompanied by lncRNA dysregulation.. This study investigated the functions of lncRNA SNHG1 in PE

Incubation:

Article Title: Characterization of gRNA-dependent and gRNA-independent off-target binding sites of PspCas13b and RfxCas13d in mammalian cells
Article Snippet: .. The cells were incubated with anti-PTBP1 (Proteintech, 12582-1-AP) or anti-HA (Abmart, M20003L) antibodies overnight at 4°C. .. After washing three times with PBST, the cells were incubated with Alexa 488-conjugated donkey anti-mouse IgG (Molecular Probes, A-21202) or Cy3-conjugated donkey anti-rabbit IgG (Jackson ImmunoResearch, 711-165-152) for 1 h at 25°C.

other:

Article Title: USP5 regulates purine metabolism and represents a therapeutic target in esophageal cancer.
Article Snippet: Primary antibodies used in this study included anti-USP5 (Proteintech, 66213-1-Ig), anti-IMPDH2 (Proteintech, 67663-1-Ig), anti-ubiquitin (Proteintech, 10201-2-AP), anti-β-actin (Santa Cruz Biotechnology, sc-47778), anti-GAPDH (ZSGB-BIO, TA-08), anti-HNRNPC (Proteintech, 11760-1-AP), anti-G3BP1 (Proteintech, 13057-2-AP), anti-PPP1R10 (Proteintech, 24450-1-AP), anti-CNBP (Proteintech, 14717-1-AP), anti-DRG1 (Proteintech, 13190-1-AP), anti-HNRNPA1 (Proteintech, 11176- 1-AP), anti-HNRNPA0 (Proteintech, 10848-1-AP), anti-SAFB (Proteintech, 21857-1-AP), anti-PTBP1 (Proteintech, 12582-1-AP), and anti-FBL (Proteintech, 16021-1-AP).

Article Title: Characterization of gRNA-dependent and gRNA-independent off-target binding sites of PspCas13b and RfxCas13d in mammalian cells.
Article Snippet: The following antibodies were used for western blot analysis in this study: PTBP1 polyclonal antibody (Proteintech, 12582-1-AP), RHOA polyclonal antibody (Proteintech, 10749-1-AP), CTSH polyclonal antibody (Proteintech, 10315-1-AP), CDK19 polyclonal antibody (Proteintech, 13761-1-AP), HMGN2 polyclonal antibody (Proteintech, 10953-1-AP), ACVR2B antibody (Abmart, T58048), NUCKS1 polyclonal antibody (Proteintech, 12023- 2-AP), HMGA1 polyclonal antibody (Proteintech, 29895- 1-AP), EZH2 polyclonal antibody (Proteintech, 21800-1- AP), EFNA3 polyclonal antibody (Proteintech, 12480-1-AP), HPSE polyclonal antibody (Proteintech, 24529-1-AP), SPG7 polyclonal antibody (Proteintech, 27801-1-AP), TRAF3 polyclonal antibody (Proteintech, 18099-1-AP), MDK polyclonal antibody (Proteintech, 11009-1-AP), SCRN1 polyclonal antibody (Proteintech, 14303-1-AP), HA-Tag (26D11) mAb (Abmart, M20003L), GAPDH (3B3) mAb (Abmart, M20006L), ACSL1 polyclonal antibody (Proteintech, 13989-1-AP), FASN polyclonal antibody (Proteintech, 10624-2-AP), RPL14 polyclonal antibody (Proteintech, 14991-1-AP), A CO X1 polyclonal antibody (Proteintech, 10957-1-AP), ACO2 polyclonal antibody (Proteintech, 11134-1-AP), EIF2D polyclonal antibody (Proteintech, 12840-1-AP).

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ZIKV infection upregulates PTBP1 expression in A549 cells. ( A–C ) A549 cells were infected with ZIKV at an MOI of 1 for different durations (0, 12, 24, and 48 h). The cells were collected for ZIKV RNA level detected by qRT-PCR ( A ), PTBP1 mRNA ( B ), and protein ( C ) levels detected by qRT-PCR and Western blot, respectively. ( D–F ) A549 cells were infected with ZIKV at MOIs of 0, 0.25, 0.5, and 1.0 for 24 h. ZIKV RNA level was detected by qRT-PCR ( A ), while PTBP1 mRNA ( B ) and protein ( C ) levels were detected by qRT-PCR and Western blot, respectively. Graphs were expressed as Mean ± SD, n = 3. ns, not significant; **, P < 0.01; ***, P < 0.001.

Journal: Journal of Virology

Article Title: PTBP1 is upregulated in response to Zika virus infection and restrains viral replication by hijacking viral NS1 protein to induce NS1 degradation

doi: 10.1128/jvi.01495-25

Figure Lengend Snippet: ZIKV infection upregulates PTBP1 expression in A549 cells. ( A–C ) A549 cells were infected with ZIKV at an MOI of 1 for different durations (0, 12, 24, and 48 h). The cells were collected for ZIKV RNA level detected by qRT-PCR ( A ), PTBP1 mRNA ( B ), and protein ( C ) levels detected by qRT-PCR and Western blot, respectively. ( D–F ) A549 cells were infected with ZIKV at MOIs of 0, 0.25, 0.5, and 1.0 for 24 h. ZIKV RNA level was detected by qRT-PCR ( A ), while PTBP1 mRNA ( B ) and protein ( C ) levels were detected by qRT-PCR and Western blot, respectively. Graphs were expressed as Mean ± SD, n = 3. ns, not significant; **, P < 0.01; ***, P < 0.001.

Article Snippet: For the staining of endogenous PTBP1 and ZIKV NS1, two rabbit antibodies were labeled with green and red dyes, respectively, with a multiplex immunohistochemistry (IHC)/immunofluorescence (IF) staining kit (Cat #RK05903; ABclonal Biotech, Wuhan, China) according to the manufacturer’s instructions.

Techniques: Infection, Expressing, Quantitative RT-PCR, Western Blot

ZIKV infection promotes PTBP1 expression via HIF-1α signal. ( A ) A549 cells were infected with ZIKV at an MOI of 1 at different time points (0, 12, and 24 h). Cells were collected at the corresponding time points for Western blot analysis. ( B and C ) A549 cells were stimulated with different doses of IOX2 (0, 20, and 40 μM) for 12 h. Cells were collected for qRT-PCR ( B ) and Western blot ( C ) analysis, respectively. ( D and E ) A549 cells were transfected with pcDNA-3.1-HIF-1α-Myc-His (2 μg) ( D ) or stimulated with IOX2 (40 μM) ( E ) for 12 h, followed by infection with ZIKV (MOI = 1) for an additional 24 h. Cells were collected for Western blot analysis, respectively. ( F and G ) A549 cells were transfected with siRNA targeting HIF-1α (siHIF-1α) (50 nM) ( F ) or stimulated with a HIF-1α inhibitor YC-1 (20 μM) ( G ) for 16 h, followed by infection with ZIKV (MOI = 1) for another 24 h. Cells were collected for Western blot analysis, respectively. Graphs were expressed as Mean ± SD, n = 3. ns, not significant; **, P < 0.01; ***, P < 0.001.

Journal: Journal of Virology

Article Title: PTBP1 is upregulated in response to Zika virus infection and restrains viral replication by hijacking viral NS1 protein to induce NS1 degradation

doi: 10.1128/jvi.01495-25

Figure Lengend Snippet: ZIKV infection promotes PTBP1 expression via HIF-1α signal. ( A ) A549 cells were infected with ZIKV at an MOI of 1 at different time points (0, 12, and 24 h). Cells were collected at the corresponding time points for Western blot analysis. ( B and C ) A549 cells were stimulated with different doses of IOX2 (0, 20, and 40 μM) for 12 h. Cells were collected for qRT-PCR ( B ) and Western blot ( C ) analysis, respectively. ( D and E ) A549 cells were transfected with pcDNA-3.1-HIF-1α-Myc-His (2 μg) ( D ) or stimulated with IOX2 (40 μM) ( E ) for 12 h, followed by infection with ZIKV (MOI = 1) for an additional 24 h. Cells were collected for Western blot analysis, respectively. ( F and G ) A549 cells were transfected with siRNA targeting HIF-1α (siHIF-1α) (50 nM) ( F ) or stimulated with a HIF-1α inhibitor YC-1 (20 μM) ( G ) for 16 h, followed by infection with ZIKV (MOI = 1) for another 24 h. Cells were collected for Western blot analysis, respectively. Graphs were expressed as Mean ± SD, n = 3. ns, not significant; **, P < 0.01; ***, P < 0.001.

Techniques: Infection, Expressing, Western Blot, Quantitative RT-PCR, Transfection

The transcriptional regulation of PTBP1 by HIF-1α. ( A ) A549 cells were transfected with 1.0 μg of each plasmid: Vector or pcDNA-3.1-HIF-1α-Myc-His. At 24 h post-transfection, cells were infected with ZIKV (MOI = 1) for 24 h, and the production of ROS was measured by the MFI of 2′,7′-dichlorofluorescein (DCF) by flow cytometry. ( B ) Schematic diagram of the PTBP1 promoter with two HIF-1α binding sites. ( C ) Chromatin prepared from A549 cells was immunoprecipitated with control IgG or phospho-HIF-1α antibodies, followed by qPCR with PTBP1 primers flanking HIF-1α responsive genomic sequence using ChIP DNA. ( D ) Schematic diagram of the predicted HIF-1α binding sites in the PTBP1 promoter. Matches in seed regions are indicated by red letters. The three mutations (black; Mut1, Mut2, and Mut1+2) were introduced into the binding sites of HIF-1α that were subcloned into the pGL3-basic plasmid for the luciferase reporter assay. ( E ) A549 cells were co-transfected with pcDNA-3.1-HIF-1α-Myc-His and pGL3-basic vector or pGL3-PTBP1-promoter (WT and mutants) for 24 h. Cells were lysed, and luciferase activities were measured. Graphs were expressed as Mean ± SD, n ≥ 3. ns, not significant; **, P < 0.01; ***, P < 0.001.

Journal: Journal of Virology

Article Title: PTBP1 is upregulated in response to Zika virus infection and restrains viral replication by hijacking viral NS1 protein to induce NS1 degradation

doi: 10.1128/jvi.01495-25

Figure Lengend Snippet: The transcriptional regulation of PTBP1 by HIF-1α. ( A ) A549 cells were transfected with 1.0 μg of each plasmid: Vector or pcDNA-3.1-HIF-1α-Myc-His. At 24 h post-transfection, cells were infected with ZIKV (MOI = 1) for 24 h, and the production of ROS was measured by the MFI of 2′,7′-dichlorofluorescein (DCF) by flow cytometry. ( B ) Schematic diagram of the PTBP1 promoter with two HIF-1α binding sites. ( C ) Chromatin prepared from A549 cells was immunoprecipitated with control IgG or phospho-HIF-1α antibodies, followed by qPCR with PTBP1 primers flanking HIF-1α responsive genomic sequence using ChIP DNA. ( D ) Schematic diagram of the predicted HIF-1α binding sites in the PTBP1 promoter. Matches in seed regions are indicated by red letters. The three mutations (black; Mut1, Mut2, and Mut1+2) were introduced into the binding sites of HIF-1α that were subcloned into the pGL3-basic plasmid for the luciferase reporter assay. ( E ) A549 cells were co-transfected with pcDNA-3.1-HIF-1α-Myc-His and pGL3-basic vector or pGL3-PTBP1-promoter (WT and mutants) for 24 h. Cells were lysed, and luciferase activities were measured. Graphs were expressed as Mean ± SD, n ≥ 3. ns, not significant; **, P < 0.01; ***, P < 0.001.

Techniques: Transfection, Plasmid Preparation, Infection, Flow Cytometry, Binding Assay, Immunoprecipitation, Control, Sequencing, Luciferase, Reporter Assay

PTBP1 suppressed ZIKV replication. ( A–C ) LV-PTBP1 and LV-Vector cells were infected with ZIKV (MOI = 1) at different time points (0, 24, and 48 h). Cells were collected at the corresponding time points for qRT-PCR ( A ) and Western blot ( B ) analysis, respectively. Supernatants were subjected to TCID 50 , and the virus titer was calculated ( C ). ( D–F ) shPTBP1 and shNC cells were infected with ZIKV (MOI = 1) at different time points (0, 24, and 48 h). Cells were collected at the corresponding time points for qRT-PCR ( D ) and Western blot ( E ) analysis, respectively. Supernatants were subjected to TCID 50 , and the virus titer was calculated ( F ). ( G–I ) shPTBP1 cells and shNC control cells were treated with different concentrations of IOX2 (0, 30, 40, 50 μM) for 12 h and then infected with ZIKV (MOI = 1). Cells were collected 24 h post-infection for qRT-PCR ( G ) and Western blot ( H ) analysis, respectively. Supernatants were subjected to TCID 50 , and the virus titer was calculated ( I ). Graphs were expressed as Mean ± SD, n = 3. *, P < 0.05; **, P < 0.01; and ***, P < 0.001.

Journal: Journal of Virology

Article Title: PTBP1 is upregulated in response to Zika virus infection and restrains viral replication by hijacking viral NS1 protein to induce NS1 degradation

doi: 10.1128/jvi.01495-25

Figure Lengend Snippet: PTBP1 suppressed ZIKV replication. ( A–C ) LV-PTBP1 and LV-Vector cells were infected with ZIKV (MOI = 1) at different time points (0, 24, and 48 h). Cells were collected at the corresponding time points for qRT-PCR ( A ) and Western blot ( B ) analysis, respectively. Supernatants were subjected to TCID 50 , and the virus titer was calculated ( C ). ( D–F ) shPTBP1 and shNC cells were infected with ZIKV (MOI = 1) at different time points (0, 24, and 48 h). Cells were collected at the corresponding time points for qRT-PCR ( D ) and Western blot ( E ) analysis, respectively. Supernatants were subjected to TCID 50 , and the virus titer was calculated ( F ). ( G–I ) shPTBP1 cells and shNC control cells were treated with different concentrations of IOX2 (0, 30, 40, 50 μM) for 12 h and then infected with ZIKV (MOI = 1). Cells were collected 24 h post-infection for qRT-PCR ( G ) and Western blot ( H ) analysis, respectively. Supernatants were subjected to TCID 50 , and the virus titer was calculated ( I ). Graphs were expressed as Mean ± SD, n = 3. *, P < 0.05; **, P < 0.01; and ***, P < 0.001.

Techniques: Plasmid Preparation, Infection, Quantitative RT-PCR, Western Blot, Virus, Control

The translocation of PTBP1 upon ZIKV infection. ( A ) Schematic diagram of PTBP1 structure. NLS, nuclear localization signal; RRM, RNA recognition motif. The indicated NLS sequence is from Lys15 to Ala41. ( B and C ) A549 cells were transfected with 1.0 μg of each plasmid: HA-Vector, HA-PTBP1-WT, or HA-PTBP1-dNLS. At 24 h post-transfection, the cells’ nucleus and cytosols were subjected to immunofluorescence assay ( B ) and Western blot analysis ( C ), respectively. Scale bar = 50 µm. ( D ) Schematic diagram of the cleavage site of PTBP1 protein. ( E ) A549 cells were infected with ZIKV (MOI = 2) for 24 h, and then the cells were harvested for protein detection by Western blot analysis with primary antibodies against PTBP1 and ZIKV NS5. Vinculin is used as an internal reference. ( F ) The plasmid expressing the mutant PTBP1 protein at the cleavage site Q153A was constructed. The plasmids HA-PTBP1-WT (2.0 μg) or HA-PTBP1-Q152A (2.0 μg) were transfected into A549 cells. At 24 h post-transfection, the cells were further infected with ZIKV (MOI = 2) for an additional 24 h. The protein in cell lysis was subjected to Western blot analysis. *, cleaved PTBP1.

Journal: Journal of Virology

Article Title: PTBP1 is upregulated in response to Zika virus infection and restrains viral replication by hijacking viral NS1 protein to induce NS1 degradation

doi: 10.1128/jvi.01495-25

Figure Lengend Snippet: The translocation of PTBP1 upon ZIKV infection. ( A ) Schematic diagram of PTBP1 structure. NLS, nuclear localization signal; RRM, RNA recognition motif. The indicated NLS sequence is from Lys15 to Ala41. ( B and C ) A549 cells were transfected with 1.0 μg of each plasmid: HA-Vector, HA-PTBP1-WT, or HA-PTBP1-dNLS. At 24 h post-transfection, the cells’ nucleus and cytosols were subjected to immunofluorescence assay ( B ) and Western blot analysis ( C ), respectively. Scale bar = 50 µm. ( D ) Schematic diagram of the cleavage site of PTBP1 protein. ( E ) A549 cells were infected with ZIKV (MOI = 2) for 24 h, and then the cells were harvested for protein detection by Western blot analysis with primary antibodies against PTBP1 and ZIKV NS5. Vinculin is used as an internal reference. ( F ) The plasmid expressing the mutant PTBP1 protein at the cleavage site Q153A was constructed. The plasmids HA-PTBP1-WT (2.0 μg) or HA-PTBP1-Q152A (2.0 μg) were transfected into A549 cells. At 24 h post-transfection, the cells were further infected with ZIKV (MOI = 2) for an additional 24 h. The protein in cell lysis was subjected to Western blot analysis. *, cleaved PTBP1.

Techniques: Translocation Assay, Infection, Sequencing, Transfection, Plasmid Preparation, Immunofluorescence, Western Blot, Expressing, Mutagenesis, Construct, Lysis

PTBP1 binds to ZIKV NS1. ( A–C ) HEK293T cells were transfected with the corresponding plasmids and harvested after 30 h. The cell lysates were incubated with anti-FLAG ( A and B ) or anti-HA ( C ) primary antibody overnight to immunoprecipitate target proteins, followed by Western blot analysis. ( D ) A549 cells were infected with ZIKV (MOI = 2) for 24 h and then harvested. The cell lysates were immunoprecipitated with anti-PTBP1 antibody, followed by Western blot analysis with the indicated antibodies. ( E ) A549 cells were infected with ZIKV (MOI = 2) for 24 h and then incubated with primary antibodies against PTBP1 and ZIKV NS1. The treated cells were labeled with corresponding fluorescent secondary antibodies and examined under a confocal fluorescence microscope. The subcellular distribution of PTBP1 (green) and ZIKV NS1 (red), along with the nucleus stained with DAPI (blue), was captured. Scale bar = 50 µm. ( F ) Schematic of bimolecular fluorescence complementation (BiFc) assay. ( G ) A549 cells were co-transfected with Venus BiFc plasmids expressing control protein (VC155 or VN173), NS1 protein (VC155-NS1), and PTBP1 protein (VN173-PTBP1), respectively. At 24 h post-transfection, the fluorescence was visualized by confocal microscopy. Scale bar = 20 µm.

Journal: Journal of Virology

Article Title: PTBP1 is upregulated in response to Zika virus infection and restrains viral replication by hijacking viral NS1 protein to induce NS1 degradation

doi: 10.1128/jvi.01495-25

Figure Lengend Snippet: PTBP1 binds to ZIKV NS1. ( A–C ) HEK293T cells were transfected with the corresponding plasmids and harvested after 30 h. The cell lysates were incubated with anti-FLAG ( A and B ) or anti-HA ( C ) primary antibody overnight to immunoprecipitate target proteins, followed by Western blot analysis. ( D ) A549 cells were infected with ZIKV (MOI = 2) for 24 h and then harvested. The cell lysates were immunoprecipitated with anti-PTBP1 antibody, followed by Western blot analysis with the indicated antibodies. ( E ) A549 cells were infected with ZIKV (MOI = 2) for 24 h and then incubated with primary antibodies against PTBP1 and ZIKV NS1. The treated cells were labeled with corresponding fluorescent secondary antibodies and examined under a confocal fluorescence microscope. The subcellular distribution of PTBP1 (green) and ZIKV NS1 (red), along with the nucleus stained with DAPI (blue), was captured. Scale bar = 50 µm. ( F ) Schematic of bimolecular fluorescence complementation (BiFc) assay. ( G ) A549 cells were co-transfected with Venus BiFc plasmids expressing control protein (VC155 or VN173), NS1 protein (VC155-NS1), and PTBP1 protein (VN173-PTBP1), respectively. At 24 h post-transfection, the fluorescence was visualized by confocal microscopy. Scale bar = 20 µm.

Techniques: Transfection, Incubation, Western Blot, Infection, Immunoprecipitation, Labeling, Fluorescence, Microscopy, Staining, Bimolecular Fluorescence Complementation Assay, Expressing, Control, Confocal Microscopy

$PTBP1 induces the degradation of ZIKV NS1 protein through the lysosomal pathway. ( A ) HEK293T cells were transfected with the HA-Vector (2.0, 1.75, 1.5, 1.25, and 0.75 μg) and FLAG-Vector (1.0, 0, 0, 0, 0 μg) or FLAG-NS1 (0, 0, 0, 0, 0.5 μg), or FLAG-NS5 (0, 0, 0, 0, 0.5 μg) or HA-PTBP1 (0, 0, 0.25, 0.5, 1.0) along with eGFP-C1 (0, 0.25, 0.25, 0.25, 0.25 μg) plasmids. After 30 h, the cells were collected and subjected to Western blot analysis. ( B ) The scheme of two main models of protein degradation: UPS (ubiquitin-proteasome system) and ALP (autophagy-lysosome pathway). ( C and D ) HEK293T cells ( C ) or A549 cells ( D ) were transfected with 1.5 μg of each plasmid: HA-Vector, FLAG-NS1, and HA-PTBP1, along with FLAG-NS1. At 18 h post-transfection, the cells were treated with DMSO, 3-MA (1.0 mM), MG132 (2.5 μM), or NH 4 Cl (5 mM) for another 12 h. The protein levels were analyzed by Western blot. ( E ) A549 cells were transfected with 1.0 μg of each plasmid: HA-Vector or HA-PTBP1, along with FLAG-NS1. At 24 h post-transfection, the cells were labeled with anti-FLAG and anti-HA primary antibodies followed by corresponding fluorescent secondary antibodies. The lysosomes were stained with Lyso-Tracker, while the nucleus was stained with DAPI. The images displaying NS1 (red), PTBP1 (green), Lysosome (white), and DAPI (blue) were captured under a confocal fluorescence microscope. Scale bar = 20 µm. ( F ) A549 cells were transfected with 1.0 μg of each plasmid: HA-Vector or HA-PTBP1 along with FLAG-NS1. At 24 h post-transfection, the cells were harvested, and lysosome isolation was performed. The cell’s lysosomal and the rest of the cytosol fractions were subjected to Western blot analysis.$

Journal: Journal of Virology

Article Title: PTBP1 is upregulated in response to Zika virus infection and restrains viral replication by hijacking viral NS1 protein to induce NS1 degradation

doi: 10.1128/jvi.01495-25

Figure Lengend Snippet: PTBP1 induces the degradation of ZIKV NS1 protein through the lysosomal pathway. ( A ) HEK293T cells were transfected with the HA-Vector (2.0, 1.75, 1.5, 1.25, and 0.75 μg) and FLAG-Vector (1.0, 0, 0, 0, 0 μg) or FLAG-NS1 (0, 0, 0, 0, 0.5 μg), or FLAG-NS5 (0, 0, 0, 0, 0.5 μg) or HA-PTBP1 (0, 0, 0.25, 0.5, 1.0) along with eGFP-C1 (0, 0.25, 0.25, 0.25, 0.25 μg) plasmids. After 30 h, the cells were collected and subjected to Western blot analysis. ( B ) The scheme of two main models of protein degradation: UPS (ubiquitin-proteasome system) and ALP (autophagy-lysosome pathway). ( C and D ) HEK293T cells ( C ) or A549 cells ( D ) were transfected with 1.5 μg of each plasmid: HA-Vector, FLAG-NS1, and HA-PTBP1, along with FLAG-NS1. At 18 h post-transfection, the cells were treated with DMSO, 3-MA (1.0 mM), MG132 (2.5 μM), or NH 4 Cl (5 mM) for another 12 h. The protein levels were analyzed by Western blot. ( E ) A549 cells were transfected with 1.0 μg of each plasmid: HA-Vector or HA-PTBP1, along with FLAG-NS1. At 24 h post-transfection, the cells were labeled with anti-FLAG and anti-HA primary antibodies followed by corresponding fluorescent secondary antibodies. The lysosomes were stained with Lyso-Tracker, while the nucleus was stained with DAPI. The images displaying NS1 (red), PTBP1 (green), Lysosome (white), and DAPI (blue) were captured under a confocal fluorescence microscope. Scale bar = 20 µm. ( F ) A549 cells were transfected with 1.0 μg of each plasmid: HA-Vector or HA-PTBP1 along with FLAG-NS1. At 24 h post-transfection, the cells were harvested, and lysosome isolation was performed. The cell’s lysosomal and the rest of the cytosol fractions were subjected to Western blot analysis.

Techniques: Transfection, Plasmid Preparation, Western Blot, Ubiquitin Proteomics, Labeling, Staining, Fluorescence, Microscopy, Isolation

Proposal model underlying PTBP1 interacts with ZIKV NS1 to inhibit viral replication. Upon ZIKV infection, ROS is initiated, and the HIF-1α signal is activated to promote PTBP1 expression. Meanwhile, ZIKV viral RNA is translated into structural and nonstructural proteins, which participate in viral replication. The HIF-1α-induced PTBP1 interacts with ZIKV NS1 and then promotes the degradation of the NS1 protein in a lysosomal pathway and finally disrupts ZIKV replication.

Journal: Journal of Virology

Article Title: PTBP1 is upregulated in response to Zika virus infection and restrains viral replication by hijacking viral NS1 protein to induce NS1 degradation

doi: 10.1128/jvi.01495-25

Figure Lengend Snippet: Proposal model underlying PTBP1 interacts with ZIKV NS1 to inhibit viral replication. Upon ZIKV infection, ROS is initiated, and the HIF-1α signal is activated to promote PTBP1 expression. Meanwhile, ZIKV viral RNA is translated into structural and nonstructural proteins, which participate in viral replication. The HIF-1α-induced PTBP1 interacts with ZIKV NS1 and then promotes the degradation of the NS1 protein in a lysosomal pathway and finally disrupts ZIKV replication.

Techniques: Infection, Expressing

Association between PTBP1 expression and clinicopathological features in breast cancer A. Comparing PTBP1 expression between BC tissues and normal breast tissues through an in-silico search based on the TCGA database (n = 114). B. Tumor grade–specific analysis of PTBP1 expression. In the TCGA cohort, analyses were performed after exclusion of cases with missing tumor grade information. The whole-cohort analysis included n = 583 cases (grade 1/2/3: n = 77/270/236). Subtype-specific analyses included luminal tumors (n = 358; grade 1/2/3: n = 65/201/82), HER2+ (ER-negative) tumors (n = 16; grade 1/2/3: n = 0/2/14), and TNBC (n = 106; grade 1/2/3: n = 1/10/95). In the METABRIC cohort, tumor grade analyses included n = 1399 cases (grade 1/2/3: n = 475/800/115/9), after exclusion of cases with missing grade information. Subtype-specific analyses included ER-positive/HER2-negative tumors (n = 992; grade 1/2/3/4: n = 358/565/61/8), HER2-positive (ER-negative) tumors (n = 90; grade 1/2/3: n = 20/52/18), and TNBC (n = 196; grade 1/2/3: n = 53/120/23). C. Tumor stage–specific analysis of PTBP1 expression. In the TCGA cohort, AJCC pathological tumor stages were consolidated into stage I–IV, and cases with missing or non-standard stage information were excluded. The whole-cohort stage analysis included n = 1069 cases (stage I/II/III/IV: n = 181/619/249/20). Subtype-specific analyses included luminal tumors (n = 578; stage I/II/III/IV: n = 115/320/134/9), HER2+ tumors (n = 42; stage I/II/III/IV: n = 2/28/11/1), and TNBC (n = 156; stage I/II/III/IV: n = 29/100/25/2). In the METABRIC cohort, stage-specific analyses included n = 1399 cases (stage 1/2/3/4: n = 475/800/115/9). Subtype-specific analyses included luminal tumors (n = 992; stage 1/2/3/4: n = 358/565/61/8), HER2+ tumors (n = 90; stage 1/2/3: n = 20/52/18), and TNBC (n = 196; stage 1/2/3: n = 53/120/23). D. Comparison of PTBP1 expression between BC and adjacent normal tissues from frozen surgical specimens by RT-PCR. The samples included 15 cases (luminal: 5, HER2+: 5, TNBC: 5).

Journal: Biochemistry and Biophysics Reports

Article Title: Oncogenic functions of polypyrimidine tract-binding protein 1 in breast cancer metabolism and progression

doi: 10.1016/j.bbrep.2026.102458

Figure Lengend Snippet: Association between PTBP1 expression and clinicopathological features in breast cancer A. Comparing PTBP1 expression between BC tissues and normal breast tissues through an in-silico search based on the TCGA database (n = 114). B. Tumor grade–specific analysis of PTBP1 expression. In the TCGA cohort, analyses were performed after exclusion of cases with missing tumor grade information. The whole-cohort analysis included n = 583 cases (grade 1/2/3: n = 77/270/236). Subtype-specific analyses included luminal tumors (n = 358; grade 1/2/3: n = 65/201/82), HER2+ (ER-negative) tumors (n = 16; grade 1/2/3: n = 0/2/14), and TNBC (n = 106; grade 1/2/3: n = 1/10/95). In the METABRIC cohort, tumor grade analyses included n = 1399 cases (grade 1/2/3: n = 475/800/115/9), after exclusion of cases with missing grade information. Subtype-specific analyses included ER-positive/HER2-negative tumors (n = 992; grade 1/2/3/4: n = 358/565/61/8), HER2-positive (ER-negative) tumors (n = 90; grade 1/2/3: n = 20/52/18), and TNBC (n = 196; grade 1/2/3: n = 53/120/23). C. Tumor stage–specific analysis of PTBP1 expression. In the TCGA cohort, AJCC pathological tumor stages were consolidated into stage I–IV, and cases with missing or non-standard stage information were excluded. The whole-cohort stage analysis included n = 1069 cases (stage I/II/III/IV: n = 181/619/249/20). Subtype-specific analyses included luminal tumors (n = 578; stage I/II/III/IV: n = 115/320/134/9), HER2+ tumors (n = 42; stage I/II/III/IV: n = 2/28/11/1), and TNBC (n = 156; stage I/II/III/IV: n = 29/100/25/2). In the METABRIC cohort, stage-specific analyses included n = 1399 cases (stage 1/2/3/4: n = 475/800/115/9). Subtype-specific analyses included luminal tumors (n = 992; stage 1/2/3/4: n = 358/565/61/8), HER2+ tumors (n = 90; stage 1/2/3: n = 20/52/18), and TNBC (n = 196; stage 1/2/3: n = 53/120/23). D. Comparison of PTBP1 expression between BC and adjacent normal tissues from frozen surgical specimens by RT-PCR. The samples included 15 cases (luminal: 5, HER2+: 5, TNBC: 5).

Article Snippet: The subsequent primary antibodies were utilised: PTBP1 (Cell Signalling, Danvers, MA, USA; 1:5000), PKM1 (NPB2-14833, Novus, Centennial, CO, USA; 1:5000), PKM2 (NPB1-48308, Novus; 1:5000), and β-actin (Thermo Fisher, Tokyo, Japan; 1:5000).

Techniques: Expressing, In Silico, Comparison, Reverse Transcription Polymerase Chain Reaction

Effect of PTBP1 knockdown on cell proliferation in BC lines A. Western blot analysis of PTBP1, PKM1, and PKM2 expression in eight BC cell lines and a normal mammary epithelial cell line (MCF10). β-actin was utilised as a loading control. B. Effects of PTBP1 knockdown in BC cells. Three BC cell lines (MCF7, Luminal; MDA-MB-231, TNBC; SK-BR-3, HER2+) were transfected with two different siRNAs targeting PTBP1. Alterations in the expression of PTBP1, PKM1, and PKM2 are illustrated. Two controls were integrated: No treatment and Control-siRNA. C. Comparison of the PKM1/PKM2 ratio following PTBP1 knockdown in the three BC cell lines. Band intensities were quantified by densitometry using NIH ImageJ software. D. Inhibition of cell proliferation 48 and 72 h after PTBP1 knockdown in the three BC cell lines, measured using the MTS Cell Proliferation Assay. The results are shown as mean ± standard deviation (SD), and statistical significance was determined through the Student's t-test; p-values are provided. Y-axis shows cell proliferation (% of control).

Journal: Biochemistry and Biophysics Reports

Article Title: Oncogenic functions of polypyrimidine tract-binding protein 1 in breast cancer metabolism and progression

doi: 10.1016/j.bbrep.2026.102458

Figure Lengend Snippet: Effect of PTBP1 knockdown on cell proliferation in BC lines A. Western blot analysis of PTBP1, PKM1, and PKM2 expression in eight BC cell lines and a normal mammary epithelial cell line (MCF10). β-actin was utilised as a loading control. B. Effects of PTBP1 knockdown in BC cells. Three BC cell lines (MCF7, Luminal; MDA-MB-231, TNBC; SK-BR-3, HER2+) were transfected with two different siRNAs targeting PTBP1. Alterations in the expression of PTBP1, PKM1, and PKM2 are illustrated. Two controls were integrated: No treatment and Control-siRNA. C. Comparison of the PKM1/PKM2 ratio following PTBP1 knockdown in the three BC cell lines. Band intensities were quantified by densitometry using NIH ImageJ software. D. Inhibition of cell proliferation 48 and 72 h after PTBP1 knockdown in the three BC cell lines, measured using the MTS Cell Proliferation Assay. The results are shown as mean ± standard deviation (SD), and statistical significance was determined through the Student's t-test; p-values are provided. Y-axis shows cell proliferation (% of control).

Techniques: Knockdown, Western Blot, Expressing, Control, Transfection, Comparison, Software, Inhibition, Proliferation Assay, Standard Deviation

Relationship between PTBP1 expression and cellular metabolism A. Cellular ATP levels per cell measured 48 h after PTBP1 knockdown in BC cells. B. Measurement of NAD + or NADH levels and their total amount (μM) in MCF7 and MDA-MB-231 cells 48 h post-PTBP1 knockdown. C. Calculation of the NADH/NAD + ratio in both cell lines based on the measured values. D. Measurement of extracellular lactate levels per cell 48 h after PTBP1 knockdown in MCF7 and MDA-MB-231 cells, normalised by medium volume and cell number. All data are presented as mean ± SD, and statistical significance was assessed using Student's t-test; p-values are provided.

Journal: Biochemistry and Biophysics Reports

Article Title: Oncogenic functions of polypyrimidine tract-binding protein 1 in breast cancer metabolism and progression

doi: 10.1016/j.bbrep.2026.102458

Figure Lengend Snippet: Relationship between PTBP1 expression and cellular metabolism A. Cellular ATP levels per cell measured 48 h after PTBP1 knockdown in BC cells. B. Measurement of NAD + or NADH levels and their total amount (μM) in MCF7 and MDA-MB-231 cells 48 h post-PTBP1 knockdown. C. Calculation of the NADH/NAD + ratio in both cell lines based on the measured values. D. Measurement of extracellular lactate levels per cell 48 h after PTBP1 knockdown in MCF7 and MDA-MB-231 cells, normalised by medium volume and cell number. All data are presented as mean ± SD, and statistical significance was assessed using Student's t-test; p-values are provided.

Techniques: Expressing, Knockdown

Association between PTBP1 expression and patient prognosis ( in silico analysis) Kaplan–Meier survival curves were generated using the METABRIC and TCGA databases. Patients were stratified into high and low PTBP1 expression groups. The analysis included assessments of (A) DFS and (B) OS across all breast cancer cases and within each subtype (Luminal, HER2+, TNBC). Patients were dichotomized into high and low PTBP1 expression groups using the median expression value. In the TCGA cohort, DFS analyses included the following numbers of patients (high/low): whole cohort 508/491, luminal subtype 278/273, HER2+ subtype 20/18, and TNBC 77/73. OS analyses in the TCGA cohort included 547/543 patients in the whole cohort, 294/292 in the luminal subtype, 22/21 in the HER2+ subtype, and 80/79 in the TNBC subtype. In the METABRIC cohort, DFS analyses included 952/952 patients in the whole cohort, 668/668 in the luminal subtype, 62/61 in the HER2+ subtype, and 134/133 in the TNBC subtype. OS analyses in the METABRIC cohort included 951/952 patients in the whole cohort, 667/668 in the luminal subtype, 62/61 in the HER2+ subtype, and 134/133 in the TNBC subtype. The numbers of patients at risk over time are shown below each Kaplan–Meier plot.

Journal: Biochemistry and Biophysics Reports

Article Title: Oncogenic functions of polypyrimidine tract-binding protein 1 in breast cancer metabolism and progression

doi: 10.1016/j.bbrep.2026.102458

Figure Lengend Snippet: Association between PTBP1 expression and patient prognosis ( in silico analysis) Kaplan–Meier survival curves were generated using the METABRIC and TCGA databases. Patients were stratified into high and low PTBP1 expression groups. The analysis included assessments of (A) DFS and (B) OS across all breast cancer cases and within each subtype (Luminal, HER2+, TNBC). Patients were dichotomized into high and low PTBP1 expression groups using the median expression value. In the TCGA cohort, DFS analyses included the following numbers of patients (high/low): whole cohort 508/491, luminal subtype 278/273, HER2+ subtype 20/18, and TNBC 77/73. OS analyses in the TCGA cohort included 547/543 patients in the whole cohort, 294/292 in the luminal subtype, 22/21 in the HER2+ subtype, and 80/79 in the TNBC subtype. In the METABRIC cohort, DFS analyses included 952/952 patients in the whole cohort, 668/668 in the luminal subtype, 62/61 in the HER2+ subtype, and 134/133 in the TNBC subtype. OS analyses in the METABRIC cohort included 951/952 patients in the whole cohort, 667/668 in the luminal subtype, 62/61 in the HER2+ subtype, and 134/133 in the TNBC subtype. The numbers of patients at risk over time are shown below each Kaplan–Meier plot.

Techniques: Expressing, In Silico, Generated

gRNA-dependent off-target binding alters the expression of essential genes and induces substantial alterations in cell proliferation. ( A – D ) RT-qPCR and western blot analyses of on-target EZH2 and three gRNA-dependent off-target genes bound by the PspCas13b-EZH2-g2 complex, with comparisons between non-targeting and EZH2-g2 targeting conditions. ( E – H ) RT-qPCR and western blot analyses of on-target EZH2 and three gRNA-dependent off-target genes bound by the RfxCas13d-EZH2-g2 complex, with comparisons between non-targeting and EZH2-g2 targeting conditions. RT-qPCR data are presented as mean ± SD ( n = 3). Relative changes in protein abundance were quantified by densitometric analysis and are indicated as red numbers at the bottom of each panel. ( I ) Proliferation of cells expressing PspCas13b (left panel) or RfxCas13d (right panel) with either targeting gRNAs or a non-targeting control gRNA (gNT), measured by CCK-8 assay. Proliferation rates were measured by absorbance at days 1–5 and normalized to that at day 1. Data are presented as mean ± SD ( n = 4). * P < 0.05; ** P < 0.01; *** P < 0.001. ns, not significant. ( J ) Apoptosis analysis of cells expressing PspCas13b (left panel) or RfxCas13d (right panel) with either targeting gRNAs or non-targeting control gRNA (gNT). Data are presented as mean ± SD ( n = 3). ns, not significant.

Journal: Nucleic Acids Research

Article Title: Characterization of gRNA-dependent and gRNA-independent off-target binding sites of PspCas13b and RfxCas13d in mammalian cells

doi: 10.1093/nar/gkag112

Figure Lengend Snippet: gRNA-dependent off-target binding alters the expression of essential genes and induces substantial alterations in cell proliferation. ( A – D ) RT-qPCR and western blot analyses of on-target EZH2 and three gRNA-dependent off-target genes bound by the PspCas13b-EZH2-g2 complex, with comparisons between non-targeting and EZH2-g2 targeting conditions. ( E – H ) RT-qPCR and western blot analyses of on-target EZH2 and three gRNA-dependent off-target genes bound by the RfxCas13d-EZH2-g2 complex, with comparisons between non-targeting and EZH2-g2 targeting conditions. RT-qPCR data are presented as mean ± SD ( n = 3). Relative changes in protein abundance were quantified by densitometric analysis and are indicated as red numbers at the bottom of each panel. ( I ) Proliferation of cells expressing PspCas13b (left panel) or RfxCas13d (right panel) with either targeting gRNAs or a non-targeting control gRNA (gNT), measured by CCK-8 assay. Proliferation rates were measured by absorbance at days 1–5 and normalized to that at day 1. Data are presented as mean ± SD ( n = 4). * P < 0.05; ** P < 0.01; *** P < 0.001. ns, not significant. ( J ) Apoptosis analysis of cells expressing PspCas13b (left panel) or RfxCas13d (right panel) with either targeting gRNAs or non-targeting control gRNA (gNT). Data are presented as mean ± SD ( n = 3). ns, not significant.

Article Snippet: The following antibodies were used for western blot analysis in this study: PTBP1 polyclonal antibody (Proteintech, 12582-1-AP), RHOA polyclonal antibody (Proteintech, 10749-1-AP), CTSH polyclonal antibody (Proteintech, 10315-1-AP), CDK19 polyclonal antibody (Proteintech, 13761-1-AP), HMGN2 polyclonal antibody (Proteintech, 10953-1-AP), ACVR2B antibody (Abmart, T58048 ), NUCKS1 polyclonal antibody (Proteintech, 12023-2-AP), HMGA1 polyclonal antibody (Proteintech, 29895-1-AP), EZH2 polyclonal antibody (Proteintech, 21800-1-AP), EFNA3 polyclonal antibody (Proteintech, 12480-1-AP), HPSE polyclonal antibody (Proteintech, 24529-1-AP), SPG7 polyclonal antibody (Proteintech, 27801-1-AP), TRAF3 polyclonal antibody (Proteintech, 18099-1-AP), MDK polyclonal antibody (Proteintech, 11009-1-AP), SCRN1 polyclonal antibody (Proteintech, 14303-1-AP), HA-Tag (26D11) mAb (Abmart, M20003L), GAPDH (3B3) mAb (Abmart, M20006L), ACSL1 polyclonal antibody (Proteintech, 13989-1-AP), FASN polyclonal antibody (Proteintech, 10624-2-AP), RPL14 polyclonal antibody (Proteintech, 14991-1-AP), ACOX1 polyclonal antibody (Proteintech, 10957-1-AP), ACO2 polyclonal antibody (Proteintech, 11134-1-AP), EIF2D polyclonal antibody (Proteintech, 12840-1-AP).

Techniques: Binding Assay, Expressing, Quantitative RT-PCR, Western Blot, Quantitative Proteomics, Control, CCK-8 Assay

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