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Proteintech cfim25

(A) <t>CFIm25</t> overexpression increases TAB2 and TBL1XR1 mRNA expression after STM infection, assessed by RT-qPCR analysis in control and CFIm25-OE macrophages at 2 and 6 hours postinfection with STM (n = 3). Data are presented as means ± SD (n = 3); *, P < 0.05; **, P < 0.01. (B) Sequence of primers used for RT-qPCR analysis of TAB2 and TBL1XR1 APA. (C) Schematic representation of the long/total TAB2 and TBL1XR1 transcript regions targeted for RT-qPCR to assess APA and mRNA expression.

Cfim25, supplied by Proteintech, used in various techniques. Bioz Stars score: 94/100, based on 57 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/anti+cfim25/NUDT21+Antibody/bio_rxiv__64898__2026__02__26__707986-64-6-7
Average 94 stars, based on 57 article reviews

cfim25 - by Bioz Stars, 2026-10

94/100 stars

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1) Product Images from "The Alternative Polyadenylation Factor CFIm25 Orchestrates Macrophage Antibacterial Immunity by Amplifying TAB2-Mediated MAPK and NF-κB Signaling During Salmonella Infection"

Article Title: The Alternative Polyadenylation Factor CFIm25 Orchestrates Macrophage Antibacterial Immunity by Amplifying TAB2-Mediated MAPK and NF-κB Signaling During Salmonella Infection

Journal: bioRxiv

doi: 10.64898/2026.02.26.707986

(A) CFIm25 overexpression increases TAB2 and TBL1XR1 mRNA expression after STM infection, assessed by RT-qPCR analysis in control and CFIm25-OE macrophages at 2 and 6 hours postinfection with STM (n = 3). Data are presented as means ± SD (n = 3); *, P < 0.05; **, P < 0.01. (B) Sequence of primers used for RT-qPCR analysis of TAB2 and TBL1XR1 APA. (C) Schematic representation of the long/total TAB2 and TBL1XR1 transcript regions targeted for RT-qPCR to assess APA and mRNA expression.

Figure Legend Snippet: (A) CFIm25 overexpression increases TAB2 and TBL1XR1 mRNA expression after STM infection, assessed by RT-qPCR analysis in control and CFIm25-OE macrophages at 2 and 6 hours postinfection with STM (n = 3). Data are presented as means ± SD (n = 3); *, P < 0.05; **, P < 0.01. (B) Sequence of primers used for RT-qPCR analysis of TAB2 and TBL1XR1 APA. (C) Schematic representation of the long/total TAB2 and TBL1XR1 transcript regions targeted for RT-qPCR to assess APA and mRNA expression.

Techniques Used: Over Expression, Expressing, Infection, Quantitative RT-PCR, Control, Sequencing

(A) Western blot analysis of CFIm25 protein in THP-1 macrophages six hours after infection with Salmonella Typhimurium (STM) compared to uninfected controls. A representative Western blot is shown on the left, and densitometric quantification of protein levels is shown on the right, normalized to GAPDH. (B-C) Flow cytometric quantification of ROS (B) and NO (C) production using DCFH-DA and DAF-FM, respectively, showing reduced microbicidal activity six hours postinfection relative to untreated macrophages. (D-E) Arginase activity, measured by urea production (D) and lactate levels (E), in macrophages six hours postinfection. All assays were compared with untreated macrophages (n = 3). Data are presented as means ± SD using three biological replicates; *, P < 0.05; **, P < 0.01.

Figure Legend Snippet: (A) Western blot analysis of CFIm25 protein in THP-1 macrophages six hours after infection with Salmonella Typhimurium (STM) compared to uninfected controls. A representative Western blot is shown on the left, and densitometric quantification of protein levels is shown on the right, normalized to GAPDH. (B-C) Flow cytometric quantification of ROS (B) and NO (C) production using DCFH-DA and DAF-FM, respectively, showing reduced microbicidal activity six hours postinfection relative to untreated macrophages. (D-E) Arginase activity, measured by urea production (D) and lactate levels (E), in macrophages six hours postinfection. All assays were compared with untreated macrophages (n = 3). Data are presented as means ± SD using three biological replicates; *, P < 0.05; **, P < 0.01.

Techniques Used: Western Blot, Infection, Activity Assay

(A) Intracellular bacterial burden (CFU) in control (−) and CFIm25-overexpressing (CFIm25-OE, +) THP-1 macrophages at two and six hours postinfection. (B) Propidium iodide flow cytometric analysis of cell death in control and CFIm25-OE macrophages at two and six hours postinfection. Graphs show the percent of cells staining with propidium iodide; only dead cells take up the stain. (C) Quantification of ROS production using the DCFH-DA fluorescence assay. (D) Quantification of NO production using the DAF-FM fluorescence assay. (E) Antimicrobial activity of conditioned media from control and CFIm25-OE macrophages against STM, assessed by CFU recovery after incubation of bacteria with media. (F) Western blot analysis of CFIm25 and LL-37 protein levels in control and CFIm25-OE macrophages at two and six hours postinfection, (G) Quantitation of LL-37 levels by densitometry measurements and normalized to GAPDH. (H) Arginase activity measured by urea production in control and CFIm25-OE macrophages at two and six hours postinfection. (I) Lactate levels in control and CFIm25-OE macrophages at two and six hours postinfection were measured using a colorimetric lactate assay kit. (J) Flow cytometric analysis of M1 (CD80) and M2 (CD206) surface marker expression in control and CFIm25-OE macrophages at two and six hours postinfection. (K) Concentrations of the TNF-α, IL-12, TGF-β, and IL-10 cytokines in culture supernatants from control and CFIm25-OE macrophages at two h and six hours postinfection as measured by ELISA. Data are presented as means ± SD from three independent experiments (n = 3); *, P < 0.05; **, P < 0.01.

Figure Legend Snippet: (A) Intracellular bacterial burden (CFU) in control (−) and CFIm25-overexpressing (CFIm25-OE, +) THP-1 macrophages at two and six hours postinfection. (B) Propidium iodide flow cytometric analysis of cell death in control and CFIm25-OE macrophages at two and six hours postinfection. Graphs show the percent of cells staining with propidium iodide; only dead cells take up the stain. (C) Quantification of ROS production using the DCFH-DA fluorescence assay. (D) Quantification of NO production using the DAF-FM fluorescence assay. (E) Antimicrobial activity of conditioned media from control and CFIm25-OE macrophages against STM, assessed by CFU recovery after incubation of bacteria with media. (F) Western blot analysis of CFIm25 and LL-37 protein levels in control and CFIm25-OE macrophages at two and six hours postinfection, (G) Quantitation of LL-37 levels by densitometry measurements and normalized to GAPDH. (H) Arginase activity measured by urea production in control and CFIm25-OE macrophages at two and six hours postinfection. (I) Lactate levels in control and CFIm25-OE macrophages at two and six hours postinfection were measured using a colorimetric lactate assay kit. (J) Flow cytometric analysis of M1 (CD80) and M2 (CD206) surface marker expression in control and CFIm25-OE macrophages at two and six hours postinfection. (K) Concentrations of the TNF-α, IL-12, TGF-β, and IL-10 cytokines in culture supernatants from control and CFIm25-OE macrophages at two h and six hours postinfection as measured by ELISA. Data are presented as means ± SD from three independent experiments (n = 3); *, P < 0.05; **, P < 0.01.

Techniques Used: Control, Staining, Fluorescence, Activity Assay, Incubation, Bacteria, Western Blot, Quantitation Assay, Lactate Assay, Marker, Expressing, Enzyme-linked Immunosorbent Assay

$(A-B) RT-qPCR analysis of the log2 ratio of long/total TAB2 (A) and TBL1XR1 (B) mRNA isoforms in control and CFIm25-OE macrophages at two and six hours postinfection, normalized to GAPDH. (C) Western blot analysis of CFIm25, HLA-DR, CD 163, and the indicated immune signaling proteins (“P”, protein; “p”, phosphorylated form) in control and CFIm25-OE macrophages at two and six hours postinfection, with GAPDH as the loading control. (D) Quantification of changes of the indicated proteins in Western blots of samples from control and CFIm25-OE macrophages at two and six hours postinfection, with values normalized to GAPDH. (E) Representative Western blot showing nuclear and cytoplasmic distribution of NF-κB subunits in control and CFIm25-OE macrophages two and six hours postinfection, assessed by fractionation and immunoblotting. Data from all quantifications are presented as means ± SD from three independent experiments. *, P < 0.05; **, P < 0.01.$
Figure Legend Snippet: (A-B) RT-qPCR analysis of the log2 ratio of long/total TAB2 (A) and TBL1XR1 (B) mRNA isoforms in control and CFIm25-OE macrophages at two and six hours postinfection, normalized to GAPDH. (C) Western blot analysis of CFIm25, HLA-DR, CD 163, and the indicated immune signaling proteins (“P”, protein; “p”, phosphorylated form) in control and CFIm25-OE macrophages at two and six hours postinfection, with GAPDH as the loading control. (D) Quantification of changes of the indicated proteins in Western blots of samples from control and CFIm25-OE macrophages at two and six hours postinfection, with values normalized to GAPDH. (E) Representative Western blot showing nuclear and cytoplasmic distribution of NF-κB subunits in control and CFIm25-OE macrophages two and six hours postinfection, assessed by fractionation and immunoblotting. Data from all quantifications are presented as means ± SD from three independent experiments. *, P < 0.05; **, P < 0.01.

Techniques Used: Quantitative RT-PCR, Control, Western Blot, Fractionation

(A) CFUs recovered at six hours postinfection from Intracellular STM in CFIm25-OE macrophages transfected with control siRNA, TAB2 siRNA, or TBL1XR1 siRNA. (B) Concentrations of TNF-α, IL-12, TGF-β, and IL-10 in culture supernatants from CFIm25-OE macrophages expressing control, TAB2, or TBL1XR1 siRNAs, harvested at six hours postinfection, and measured by ELISA. (C-F) ROS (C), NO (D), arginase activity (E), and lactate (F) levels at six hours postinfection in CFIm25-OE macrophages treated with control, TAB2, or TBL1XR1 siRNA. (G) Flow cytometric analysis of CD80 and CD206 expression at six hours postinfection in CFIm25-OE macrophages treated with control, TAB2, or TBL1XR1 siRNA. (H) Western blot analysis of the indicated NF-κB and MAPK signaling proteins at six hours postinfection in CFIm25-OE macrophages treated with control, TAB2, or TBL1XR1 siRNA, with densitometric quantification from three independent experiments (“P”, protein; “p”, phosphorylated form). Data are presented as means ± SD (n = 3); *, P < 0.05; **, P < 0.01.

Figure Legend Snippet: (A) CFUs recovered at six hours postinfection from Intracellular STM in CFIm25-OE macrophages transfected with control siRNA, TAB2 siRNA, or TBL1XR1 siRNA. (B) Concentrations of TNF-α, IL-12, TGF-β, and IL-10 in culture supernatants from CFIm25-OE macrophages expressing control, TAB2, or TBL1XR1 siRNAs, harvested at six hours postinfection, and measured by ELISA. (C-F) ROS (C), NO (D), arginase activity (E), and lactate (F) levels at six hours postinfection in CFIm25-OE macrophages treated with control, TAB2, or TBL1XR1 siRNA. (G) Flow cytometric analysis of CD80 and CD206 expression at six hours postinfection in CFIm25-OE macrophages treated with control, TAB2, or TBL1XR1 siRNA. (H) Western blot analysis of the indicated NF-κB and MAPK signaling proteins at six hours postinfection in CFIm25-OE macrophages treated with control, TAB2, or TBL1XR1 siRNA, with densitometric quantification from three independent experiments (“P”, protein; “p”, phosphorylated form). Data are presented as means ± SD (n = 3); *, P < 0.05; **, P < 0.01.

Techniques Used: Transfection, Control, Expressing, Enzyme-linked Immunosorbent Assay, Activity Assay, Western Blot

Immunofluorescence:

Article Title: Mammalian cleavage factor 25 targets KLF14 to inhibit hepatic stellate cell activation and liver fibrosis.
Article Snippet: Liver fibrosis is primarily caused by the activation of hepatic stellate cells (HSCs), which results from chronic liver damage.. Understanding the pathogenesis of HSC activation could identify new therapeutic targets to treat liver fibrosis.. In this study, we examined the protective role of the mammalian cleavage factor I 25 kD subunit (CFIm25, NUDT21) in inhibiting hepatic stellate cell activation.

Incubation:

other:

Article Title: Partial loss of CFIm25 causes learning deficits and aberrant neuronal alternative polyadenylation
Article Snippet: Antibody , Anti-CFIm25 (rabbit polyclonal) , Proteintech , Proteintech Cat# 10322–1-AP, RRID: AB_2251496 , 1:50.

Control:

Article Title: A Cancer-Specific Ubiquitin Ligase Drives mRNA Alternative Polyadenylation by Ubiquitinating the mRNA 3' End Processing Complex.
Article Snippet: Cell lysates were incubated with 20 mL pre-coupled antibody-protein A/G PLUS-agarose beads (Santa Cruz Biotechnology) for 3 hr at 4 C rotating. .. Antibodies (10 mg) used were as follows: normal mouse IgG control (Santa Cruz, sc-2025) and anti-CFIm25 (Proteintech, 66335-1-Ig). .. Beads were then washed three times in NP-40 lysis buffer, treated with 20 units of RNase-free DNase I for 15 min at 37 C, and proteins degraded by treatment with 0.5 mg/mL proteinase K (Invitrogen) in 0.5% SDS at 55 C for 15 min. RNA was then separated by phenol: chloroform extraction, followed by ethanol precipitation.

Blocking Assay:

Article Title: Distinct, opposing functions for CFIm59 and CFIm68 in mRNA alternative polyadenylation of Pten and in the PI3K/Akt signalling cascade.
Article Snippet: Precise maintenance of PTEN dosage is crucial for tumor suppression across a wide variety of cancers.. Post-transcriptional regulation of Pten heavily relies on regulatory elements encoded by its 3′UTR.. We previously reported the important diversity of 3′UTR isoforms of Pten mRNAs produced through alternative polyadenylation (APA). .. Precise maintenance of PTEN dosage is crucial for tumor suppression across a wide variety of cancers.. Post-transcriptional regulation of Pten heavily relies on regulatory elements encoded by its 3′UTR.. We previously reported the important diversity of 3′UTR isoforms of Pten mRNAs produced through alternative polyadenylation (APA). .. Precise maintenance of PTEN dosage is crucial for tumor suppression across a wide variety of cancers.. Post-transcriptional regulation of Pten heavily relies on regulatory elements encoded by its 3′UTR.. We previously reported the important diversity of 3′UTR isoforms of Pten mRNAs produced through alternative polyadenylation (APA).

Article Title: Distinct, opposing functions for CFIm59 and CFIm68 in mRNA alternative polyadenylation of Pten and in the PI3K/Akt signalling cascade
Article Snippet: Total cell lysates were prepared using lysis buffer (50 mM Tris–HCl pH 7.4, 150 mM NaCl, 1% IGEPAL CA-630, 1% sodium deoxycholate, 0.1% sodium dodecyl sulphate and 1 mM ethylenediaminetetraacetic acid) supplemented with protease and phosphatase inhibitors (Sigma and Roche). .. Proteins were immobilized on PVDF membranes (Millipore) and probed with the following antibodies diluted in the Odyssey blocking buffer (Li-COR): anti-CFIm68 (Bethyl A301-358A-T, 1:1000), anti-CFIm25 (Proteintech 10322-1-AP, 1:250), anti-CFIm59 (Sigma HPA041094, 1:500), anti-β-actin (CST 8H10D10, 1:5000), anti-PTEN (CST 9552, 1:1000). .. Secondary IR dye antibodies against mouse or rabbit (Li-COR) were used at 1:10 000.

Article Title: Distinct, opposing functions for CFIm59 and CFIm68 in mRNA alternative polyadenylation of Pten and in the PI3K/Akt signalling cascade
Article Snippet: Total cell lysates were prepared using lysis buffer (50 mM Tris-HCl pH 7.4, 150 mM NaCl, 1% IGEPAL CA-630, 1% sodium deoxycholate, 0.1% sodium dodecyl sulphate, and 1 mM ethylenediaminetetraacetic acid) supplemented with protease and phosphatase inhibitors (Sigma and Roche). .. Proteins were immobilized on PVDF membranes (Millipore) and probed with the following antibodies diluted in the Odyssey blocking buffer (Li-COR): anti-CFIm68 (Bethyl A301-358A-T, 1:1,000), anti-CFIm25 (Proteintech 10322-1-AP, 1:250), anti-CFIm59 (Sigma HPA041094, 1:500), anti-β-actin (CST 8H10D10, 1:5,000), anti-PTEN (CST 9552, 1:1,000). .. Secondary IR dye antibodies against mouse or rabbit (Li-COR) were used at 1:10,000.

Image Search Results

Journal: bioRxiv

Article Title: The Alternative Polyadenylation Factor CFIm25 Orchestrates Macrophage Antibacterial Immunity by Amplifying TAB2-Mediated MAPK and NF-κB Signaling During Salmonella Infection

doi: 10.64898/2026.02.26.707986

Figure Lengend Snippet: (A) CFIm25 overexpression increases TAB2 and TBL1XR1 mRNA expression after STM infection, assessed by RT-qPCR analysis in control and CFIm25-OE macrophages at 2 and 6 hours postinfection with STM (n = 3). Data are presented as means ± SD (n = 3); *, P < 0.05; **, P < 0.01. (B) Sequence of primers used for RT-qPCR analysis of TAB2 and TBL1XR1 APA. (C) Schematic representation of the long/total TAB2 and TBL1XR1 transcript regions targeted for RT-qPCR to assess APA and mRNA expression.

Article Snippet: Antibodies used in this study included CFIm25 (Proteintech, 10322-1-AP), LL-37 (Santa Cruz, sc-166770), phosphorylated NF-κB P65 (Ser536) (Cell Signaling, 3033), NF-κB P65 (Cell Signaling, 8242), TAB2 (Cell Signaling, 3744), TBL1XR1 (Novus, NBP1-86996), phosphorylated STAT1 (Tyr701) (Cell Signaling, 9167), STAT1 (Cell Signaling, 14994), phosphorylated STAT3(Tyr705) (Cell Signaling, 9145), STAT3 (Cell Signaling, 4904), IκBα (Cell Signaling, 4814), phosphorylated P38(Thr180/Tyr182) (Cell Signaling, 4511), P38 (Cell Signaling, 9212), CD163 (Proteintech 68218-1-g), histone H3 (Cell Signaling, 9715), and GAPDH (Santa Cruz SC3233).

Techniques: Over Expression, Expressing, Infection, Quantitative RT-PCR, Control, Sequencing

Journal: bioRxiv

Article Title: The Alternative Polyadenylation Factor CFIm25 Orchestrates Macrophage Antibacterial Immunity by Amplifying TAB2-Mediated MAPK and NF-κB Signaling During Salmonella Infection

doi: 10.64898/2026.02.26.707986

Figure Lengend Snippet: (A) Western blot analysis of CFIm25 protein in THP-1 macrophages six hours after infection with Salmonella Typhimurium (STM) compared to uninfected controls. A representative Western blot is shown on the left, and densitometric quantification of protein levels is shown on the right, normalized to GAPDH. (B-C) Flow cytometric quantification of ROS (B) and NO (C) production using DCFH-DA and DAF-FM, respectively, showing reduced microbicidal activity six hours postinfection relative to untreated macrophages. (D-E) Arginase activity, measured by urea production (D) and lactate levels (E), in macrophages six hours postinfection. All assays were compared with untreated macrophages (n = 3). Data are presented as means ± SD using three biological replicates; *, P < 0.05; **, P < 0.01.

Techniques: Western Blot, Infection, Activity Assay

Journal: bioRxiv

Article Title: The Alternative Polyadenylation Factor CFIm25 Orchestrates Macrophage Antibacterial Immunity by Amplifying TAB2-Mediated MAPK and NF-κB Signaling During Salmonella Infection

doi: 10.64898/2026.02.26.707986

Figure Lengend Snippet: (A) Intracellular bacterial burden (CFU) in control (−) and CFIm25-overexpressing (CFIm25-OE, +) THP-1 macrophages at two and six hours postinfection. (B) Propidium iodide flow cytometric analysis of cell death in control and CFIm25-OE macrophages at two and six hours postinfection. Graphs show the percent of cells staining with propidium iodide; only dead cells take up the stain. (C) Quantification of ROS production using the DCFH-DA fluorescence assay. (D) Quantification of NO production using the DAF-FM fluorescence assay. (E) Antimicrobial activity of conditioned media from control and CFIm25-OE macrophages against STM, assessed by CFU recovery after incubation of bacteria with media. (F) Western blot analysis of CFIm25 and LL-37 protein levels in control and CFIm25-OE macrophages at two and six hours postinfection, (G) Quantitation of LL-37 levels by densitometry measurements and normalized to GAPDH. (H) Arginase activity measured by urea production in control and CFIm25-OE macrophages at two and six hours postinfection. (I) Lactate levels in control and CFIm25-OE macrophages at two and six hours postinfection were measured using a colorimetric lactate assay kit. (J) Flow cytometric analysis of M1 (CD80) and M2 (CD206) surface marker expression in control and CFIm25-OE macrophages at two and six hours postinfection. (K) Concentrations of the TNF-α, IL-12, TGF-β, and IL-10 cytokines in culture supernatants from control and CFIm25-OE macrophages at two h and six hours postinfection as measured by ELISA. Data are presented as means ± SD from three independent experiments (n = 3); *, P < 0.05; **, P < 0.01.

Techniques: Control, Staining, Fluorescence, Activity Assay, Incubation, Bacteria, Western Blot, Quantitation Assay, Lactate Assay, Marker, Expressing, Enzyme-linked Immunosorbent Assay

Journal: bioRxiv

Article Title: The Alternative Polyadenylation Factor CFIm25 Orchestrates Macrophage Antibacterial Immunity by Amplifying TAB2-Mediated MAPK and NF-κB Signaling During Salmonella Infection

doi: 10.64898/2026.02.26.707986

Figure Lengend Snippet: (A-B) RT-qPCR analysis of the log2 ratio of long/total TAB2 (A) and TBL1XR1 (B) mRNA isoforms in control and CFIm25-OE macrophages at two and six hours postinfection, normalized to GAPDH. (C) Western blot analysis of CFIm25, HLA-DR, CD 163, and the indicated immune signaling proteins (“P”, protein; “p”, phosphorylated form) in control and CFIm25-OE macrophages at two and six hours postinfection, with GAPDH as the loading control. (D) Quantification of changes of the indicated proteins in Western blots of samples from control and CFIm25-OE macrophages at two and six hours postinfection, with values normalized to GAPDH. (E) Representative Western blot showing nuclear and cytoplasmic distribution of NF-κB subunits in control and CFIm25-OE macrophages two and six hours postinfection, assessed by fractionation and immunoblotting. Data from all quantifications are presented as means ± SD from three independent experiments. *, P < 0.05; **, P < 0.01.

Techniques: Quantitative RT-PCR, Control, Western Blot, Fractionation

Journal: bioRxiv

Article Title: The Alternative Polyadenylation Factor CFIm25 Orchestrates Macrophage Antibacterial Immunity by Amplifying TAB2-Mediated MAPK and NF-κB Signaling During Salmonella Infection

doi: 10.64898/2026.02.26.707986

Figure Lengend Snippet: (A) CFUs recovered at six hours postinfection from Intracellular STM in CFIm25-OE macrophages transfected with control siRNA, TAB2 siRNA, or TBL1XR1 siRNA. (B) Concentrations of TNF-α, IL-12, TGF-β, and IL-10 in culture supernatants from CFIm25-OE macrophages expressing control, TAB2, or TBL1XR1 siRNAs, harvested at six hours postinfection, and measured by ELISA. (C-F) ROS (C), NO (D), arginase activity (E), and lactate (F) levels at six hours postinfection in CFIm25-OE macrophages treated with control, TAB2, or TBL1XR1 siRNA. (G) Flow cytometric analysis of CD80 and CD206 expression at six hours postinfection in CFIm25-OE macrophages treated with control, TAB2, or TBL1XR1 siRNA. (H) Western blot analysis of the indicated NF-κB and MAPK signaling proteins at six hours postinfection in CFIm25-OE macrophages treated with control, TAB2, or TBL1XR1 siRNA, with densitometric quantification from three independent experiments (“P”, protein; “p”, phosphorylated form). Data are presented as means ± SD (n = 3); *, P < 0.05; **, P < 0.01.

Techniques: Transfection, Control, Expressing, Enzyme-linked Immunosorbent Assay, Activity Assay, Western Blot

CFIm25 variably regulates V2 and V3 PAS usage.

Journal: RNA Biology

Article Title: WDR33 alternative polyadenylation is dependent on stochastic poly(a) site usage and splicing efficiencies

doi: 10.1080/15476286.2024.2408708

Figure Lengend Snippet: CFIm25 variably regulates V2 and V3 PAS usage.

Article Snippet: Primary antibodies were: rabbit-anti-NUDT21 (CFIm25) (ABclonal, A4482); rabbit-anti-FIP1L1 (FIP1) (ABclonal, A7138), rabbit-anti-CstF64 [ ]; rabbit anti-Actin (Sigma-Aldrich, A2066) and rabbit anti-GAPDH (Sigma-Aldrich, G9545).

Techniques:

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cfim25 (Proteintech)

Structured Review

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1) Product Images from "The Alternative Polyadenylation Factor CFIm25 Orchestrates Macrophage Antibacterial Immunity by Amplifying TAB2-Mediated MAPK and NF-κB Signaling During Salmonella Infection"

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