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Structured Review

Proteintech rabbit polyclonal anti srsf1
Circ_0007432 maintained KLF12 mRNA stability by recruiting <t>SRSF1</t> (A) KLF12 expression was detected in tumor tissues and corresponding adjacent tissues from NSCLC patients using RT-qPCR. n = 50. (B) The relationship between circ_0007432 and KLF12 in NSCLC was analyzed using Pearson correlation analysis. n = 50. (C and D) KLF12 expression was measured in NSCLC cells (PC-9, Calu-3, H1975, A549, and H358) and BEAS-2B cells using RT-qPCR and western blot. n = 3. (E and F) KLF12 expression was evaluated in sh-NC- or sh-circ_0007432-transfected H1975 and A549 cells by RT-qPCR and western blot. n = 3. (G) The stability of KLF12 mRNA was detected in sh-NC- or sh-circ_0007432-transfected NSCLC cells by RT-qPCR. n = 3. (H) The interaction between circ_0007432 and Ago2 in NSCLC cells were evaluated using RIP. n = 3. (I and J) The interaction between circ_0007432 and SRSF1 was validated using RNA pull down and RIP. n = 3. (K and L) The interaction between KLF12 and SRSF1 was validated using RIP. n = 3. (M–O) SRSF1 and KLF12 expression was detected in sh-NC- or sh-SRSF1-transfected H1975 and A549 cells by RT-qPCR and western blot. n = 3. (P) The stability of KLF12 mRNA was detected in sh-NC- or sh-SRSF1-transfected NSCLC cells by RT-qPCR. n = 3. Data were shown as mean ± SD. Each experiment was accomplished in triplicates. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001. Student’s t test for (A), (C), (D), (H), (J), (K), and (L). Pearson correlation analysis for (B). One-way analysis of variance (ANOVA) test for (E), (F), (G), (M), (N), (O), and (P).
Rabbit Polyclonal Anti Srsf1, supplied by Proteintech, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1) Product Images from "Circ_0007432 promotes non-small cell lung cancer progression and macrophage M2 polarization through SRSF1/KLF12 axis"

Article Title: Circ_0007432 promotes non-small cell lung cancer progression and macrophage M2 polarization through SRSF1/KLF12 axis

Journal: iScience

doi: 10.1016/j.isci.2024.109861

Circ_0007432 maintained KLF12 mRNA stability by recruiting SRSF1 (A) KLF12 expression was detected in tumor tissues and corresponding adjacent tissues from NSCLC patients using RT-qPCR. n = 50. (B) The relationship between circ_0007432 and KLF12 in NSCLC was analyzed using Pearson correlation analysis. n = 50. (C and D) KLF12 expression was measured in NSCLC cells (PC-9, Calu-3, H1975, A549, and H358) and BEAS-2B cells using RT-qPCR and western blot. n = 3. (E and F) KLF12 expression was evaluated in sh-NC- or sh-circ_0007432-transfected H1975 and A549 cells by RT-qPCR and western blot. n = 3. (G) The stability of KLF12 mRNA was detected in sh-NC- or sh-circ_0007432-transfected NSCLC cells by RT-qPCR. n = 3. (H) The interaction between circ_0007432 and Ago2 in NSCLC cells were evaluated using RIP. n = 3. (I and J) The interaction between circ_0007432 and SRSF1 was validated using RNA pull down and RIP. n = 3. (K and L) The interaction between KLF12 and SRSF1 was validated using RIP. n = 3. (M–O) SRSF1 and KLF12 expression was detected in sh-NC- or sh-SRSF1-transfected H1975 and A549 cells by RT-qPCR and western blot. n = 3. (P) The stability of KLF12 mRNA was detected in sh-NC- or sh-SRSF1-transfected NSCLC cells by RT-qPCR. n = 3. Data were shown as mean ± SD. Each experiment was accomplished in triplicates. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001. Student’s t test for (A), (C), (D), (H), (J), (K), and (L). Pearson correlation analysis for (B). One-way analysis of variance (ANOVA) test for (E), (F), (G), (M), (N), (O), and (P).
Figure Legend Snippet: Circ_0007432 maintained KLF12 mRNA stability by recruiting SRSF1 (A) KLF12 expression was detected in tumor tissues and corresponding adjacent tissues from NSCLC patients using RT-qPCR. n = 50. (B) The relationship between circ_0007432 and KLF12 in NSCLC was analyzed using Pearson correlation analysis. n = 50. (C and D) KLF12 expression was measured in NSCLC cells (PC-9, Calu-3, H1975, A549, and H358) and BEAS-2B cells using RT-qPCR and western blot. n = 3. (E and F) KLF12 expression was evaluated in sh-NC- or sh-circ_0007432-transfected H1975 and A549 cells by RT-qPCR and western blot. n = 3. (G) The stability of KLF12 mRNA was detected in sh-NC- or sh-circ_0007432-transfected NSCLC cells by RT-qPCR. n = 3. (H) The interaction between circ_0007432 and Ago2 in NSCLC cells were evaluated using RIP. n = 3. (I and J) The interaction between circ_0007432 and SRSF1 was validated using RNA pull down and RIP. n = 3. (K and L) The interaction between KLF12 and SRSF1 was validated using RIP. n = 3. (M–O) SRSF1 and KLF12 expression was detected in sh-NC- or sh-SRSF1-transfected H1975 and A549 cells by RT-qPCR and western blot. n = 3. (P) The stability of KLF12 mRNA was detected in sh-NC- or sh-SRSF1-transfected NSCLC cells by RT-qPCR. n = 3. Data were shown as mean ± SD. Each experiment was accomplished in triplicates. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001. Student’s t test for (A), (C), (D), (H), (J), (K), and (L). Pearson correlation analysis for (B). One-way analysis of variance (ANOVA) test for (E), (F), (G), (M), (N), (O), and (P).

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


Figure Legend Snippet:

Techniques Used: Recombinant, Enzyme-linked Immunosorbent Assay, Reverse Transcription, Labeling, Software

The primer sequences
Figure Legend Snippet: The primer sequences

Techniques Used:



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Danaher Inc rabbit polyclonal anti srsf1
Circ_0007432 maintained KLF12 mRNA stability by recruiting <t>SRSF1</t> (A) KLF12 expression was detected in tumor tissues and corresponding adjacent tissues from NSCLC patients using RT-qPCR. n = 50. (B) The relationship between circ_0007432 and KLF12 in NSCLC was analyzed using Pearson correlation analysis. n = 50. (C and D) KLF12 expression was measured in NSCLC cells (PC-9, Calu-3, H1975, A549, and H358) and BEAS-2B cells using RT-qPCR and western blot. n = 3. (E and F) KLF12 expression was evaluated in sh-NC- or sh-circ_0007432-transfected H1975 and A549 cells by RT-qPCR and western blot. n = 3. (G) The stability of KLF12 mRNA was detected in sh-NC- or sh-circ_0007432-transfected NSCLC cells by RT-qPCR. n = 3. (H) The interaction between circ_0007432 and Ago2 in NSCLC cells were evaluated using RIP. n = 3. (I and J) The interaction between circ_0007432 and SRSF1 was validated using RNA pull down and RIP. n = 3. (K and L) The interaction between KLF12 and SRSF1 was validated using RIP. n = 3. (M–O) SRSF1 and KLF12 expression was detected in sh-NC- or sh-SRSF1-transfected H1975 and A549 cells by RT-qPCR and western blot. n = 3. (P) The stability of KLF12 mRNA was detected in sh-NC- or sh-SRSF1-transfected NSCLC cells by RT-qPCR. n = 3. Data were shown as mean ± SD. Each experiment was accomplished in triplicates. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001. Student’s t test for (A), (C), (D), (H), (J), (K), and (L). Pearson correlation analysis for (B). One-way analysis of variance (ANOVA) test for (E), (F), (G), (M), (N), (O), and (P).
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Proteintech rabbit polyclonal anti srsf1
Circ_0007432 maintained KLF12 mRNA stability by recruiting <t>SRSF1</t> (A) KLF12 expression was detected in tumor tissues and corresponding adjacent tissues from NSCLC patients using RT-qPCR. n = 50. (B) The relationship between circ_0007432 and KLF12 in NSCLC was analyzed using Pearson correlation analysis. n = 50. (C and D) KLF12 expression was measured in NSCLC cells (PC-9, Calu-3, H1975, A549, and H358) and BEAS-2B cells using RT-qPCR and western blot. n = 3. (E and F) KLF12 expression was evaluated in sh-NC- or sh-circ_0007432-transfected H1975 and A549 cells by RT-qPCR and western blot. n = 3. (G) The stability of KLF12 mRNA was detected in sh-NC- or sh-circ_0007432-transfected NSCLC cells by RT-qPCR. n = 3. (H) The interaction between circ_0007432 and Ago2 in NSCLC cells were evaluated using RIP. n = 3. (I and J) The interaction between circ_0007432 and SRSF1 was validated using RNA pull down and RIP. n = 3. (K and L) The interaction between KLF12 and SRSF1 was validated using RIP. n = 3. (M–O) SRSF1 and KLF12 expression was detected in sh-NC- or sh-SRSF1-transfected H1975 and A549 cells by RT-qPCR and western blot. n = 3. (P) The stability of KLF12 mRNA was detected in sh-NC- or sh-SRSF1-transfected NSCLC cells by RT-qPCR. n = 3. Data were shown as mean ± SD. Each experiment was accomplished in triplicates. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001. Student’s t test for (A), (C), (D), (H), (J), (K), and (L). Pearson correlation analysis for (B). One-way analysis of variance (ANOVA) test for (E), (F), (G), (M), (N), (O), and (P).
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Association between <t> SRSF1 </t> expression and the clinicopathological characteristics of patients with glioma in the Chinese Glioma Genome Atlas cohort.
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Thermo Fisher rabbit polyclonal anti srsf1
Association between <t> SRSF1 </t> expression and the clinicopathological characteristics of patients with glioma in the Chinese Glioma Genome Atlas cohort.
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<t>SRSF1</t> resists GC apoptosis and follicular atresia. ( A ) Venn diagram of the DEGs (differentially expressed genes) between HFs and AFs and miR-9820-5p target genes predicted by PITA, Miranda, and TargetSpy. ( B ) Differentially expressed SRSF1 in HFs and AFs detected by qRT-PCR. ( C , D ) Effective knockdown of SRSF1 by si-SRSF1 qRT-PCR and western blotting (WB). ( E ) The shift of GC apoptosis rates after SRSF1 knockdown was detected by flow cytometry. Data are expressed as the mean ± SEM of three experiments; * p < 0.05, ** p < 0.01.
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Inhibiting SRPKs decreases SR protein phosphorylation and increases cells harboring cytoplasmic SRSF2 granule and tubule structures in HEK293 cells. A , HEK293 cells were incubated with either DMSO (vehicle, VEH) or increasing concentrations of SRPK inhibitor SRPIN340 for a length of 12 h. Immediately following treatment, cells were harvested, run by SDS-PAGE, and immunoblotted for phosphoSR (pSR) proteins using the pan-pSR antibody mAb104. A p-TDP-43 antibody (pTDP-43 band marked by asterisk ) and a Histone H3 antibody were used to confirm specificity of SRPIN340 and equal protein loading, respectively. B , protein band intensities for SRSF4 ( purple ), SRSF6 ( blue ), SRSF10 ( red ), SRSF2/SRSF7 ( gold ), <t>SRSF1/9</t> ( turquoise ), and separately, pTDP-43 ( green ) were quantified and normalized to the VEH condition (artificially set to value = 1) (multiple t tests, ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001). Error bars indicate maximum and minimum ranges of band values. The pSRSF2 signal was significantly decreased at 50 μM SRPIN340 concentration, whereas fellow RBP TDP-43 was not. C , validation of HEK293 cell extract fractionation procedure, yielding total (T), cytosolic (C), and nuclear (N) samples. The fractions were immunoblotted for the cytosolic marker GAPDH ( green ) and nuclear marker Histone H3 ( red ). D , immunoblot of nuclear-cytoplasmic fractions for total, endogenous SRSF2 in VEH and SRPIN340 conditions. E , quantification of percent nuclear SRSF2 (nuclear signal divided by sum of cytoplasmic and nuclear signals) in VEH and SRPIN340 conditions (paired t test, ∗ p value = 0.0130). F and G , immunocytochemical (ICC) staining of HEK293 cells for phosphoSRSF2 (pSRSF2)-positive nuclear speckles ( green ) and DAPI+ nuclei ( blue ) in vehicle-treated cells ( F ) and 50 μM SRPIN340-treated cells ( G ). H , the number of cytoplasmic granules observed was divided by the number of cells counted and averaged for 14 independent images in three independent replicates (two-tailed paired t test, ∗ p value = 0.0191). A minimum of 120 cells were counted in each condition per replicate. The error bars represent the range of standard deviation. I and J , ICC staining of HEK293 cells for hypophosphorylated SRSF2 (hypoSRSF2) ( green ) and DAPI+ nuclei ( blue ) in vehicle-treated cells ( I ) and 50 μM SRPIN340-treated cells ( J ). K , the fraction of cells harboring cytoplasmic SRSF2 tubule structures was quantified in four biological replicates and compared (two-tailed paired t test, ∗ p value = 0.0178). L , vehicle- and ( M ) 50 μM SRPIN340-treated HEK293 cells were stained by ICC for TDP-43 ( green ) and DAPI-stained.
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Effects of valsartan on protein expression of <t>SRSF1.</t> Protein expression of SRSF1 was determined using immunofluorescence in 14 days (A, B, C) and 28 days (D, E, F).
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Image Search Results


Circ_0007432 maintained KLF12 mRNA stability by recruiting SRSF1 (A) KLF12 expression was detected in tumor tissues and corresponding adjacent tissues from NSCLC patients using RT-qPCR. n = 50. (B) The relationship between circ_0007432 and KLF12 in NSCLC was analyzed using Pearson correlation analysis. n = 50. (C and D) KLF12 expression was measured in NSCLC cells (PC-9, Calu-3, H1975, A549, and H358) and BEAS-2B cells using RT-qPCR and western blot. n = 3. (E and F) KLF12 expression was evaluated in sh-NC- or sh-circ_0007432-transfected H1975 and A549 cells by RT-qPCR and western blot. n = 3. (G) The stability of KLF12 mRNA was detected in sh-NC- or sh-circ_0007432-transfected NSCLC cells by RT-qPCR. n = 3. (H) The interaction between circ_0007432 and Ago2 in NSCLC cells were evaluated using RIP. n = 3. (I and J) The interaction between circ_0007432 and SRSF1 was validated using RNA pull down and RIP. n = 3. (K and L) The interaction between KLF12 and SRSF1 was validated using RIP. n = 3. (M–O) SRSF1 and KLF12 expression was detected in sh-NC- or sh-SRSF1-transfected H1975 and A549 cells by RT-qPCR and western blot. n = 3. (P) The stability of KLF12 mRNA was detected in sh-NC- or sh-SRSF1-transfected NSCLC cells by RT-qPCR. n = 3. Data were shown as mean ± SD. Each experiment was accomplished in triplicates. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001. Student’s t test for (A), (C), (D), (H), (J), (K), and (L). Pearson correlation analysis for (B). One-way analysis of variance (ANOVA) test for (E), (F), (G), (M), (N), (O), and (P).

Journal: iScience

Article Title: Circ_0007432 promotes non-small cell lung cancer progression and macrophage M2 polarization through SRSF1/KLF12 axis

doi: 10.1016/j.isci.2024.109861

Figure Lengend Snippet: Circ_0007432 maintained KLF12 mRNA stability by recruiting SRSF1 (A) KLF12 expression was detected in tumor tissues and corresponding adjacent tissues from NSCLC patients using RT-qPCR. n = 50. (B) The relationship between circ_0007432 and KLF12 in NSCLC was analyzed using Pearson correlation analysis. n = 50. (C and D) KLF12 expression was measured in NSCLC cells (PC-9, Calu-3, H1975, A549, and H358) and BEAS-2B cells using RT-qPCR and western blot. n = 3. (E and F) KLF12 expression was evaluated in sh-NC- or sh-circ_0007432-transfected H1975 and A549 cells by RT-qPCR and western blot. n = 3. (G) The stability of KLF12 mRNA was detected in sh-NC- or sh-circ_0007432-transfected NSCLC cells by RT-qPCR. n = 3. (H) The interaction between circ_0007432 and Ago2 in NSCLC cells were evaluated using RIP. n = 3. (I and J) The interaction between circ_0007432 and SRSF1 was validated using RNA pull down and RIP. n = 3. (K and L) The interaction between KLF12 and SRSF1 was validated using RIP. n = 3. (M–O) SRSF1 and KLF12 expression was detected in sh-NC- or sh-SRSF1-transfected H1975 and A549 cells by RT-qPCR and western blot. n = 3. (P) The stability of KLF12 mRNA was detected in sh-NC- or sh-SRSF1-transfected NSCLC cells by RT-qPCR. n = 3. Data were shown as mean ± SD. Each experiment was accomplished in triplicates. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001. Student’s t test for (A), (C), (D), (H), (J), (K), and (L). Pearson correlation analysis for (B). One-way analysis of variance (ANOVA) test for (E), (F), (G), (M), (N), (O), and (P).

Article Snippet: Rabbit polyclonal anti-SRSF1 , Abcam , Cat# ab38017; AB_882519.

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

Journal: iScience

Article Title: Circ_0007432 promotes non-small cell lung cancer progression and macrophage M2 polarization through SRSF1/KLF12 axis

doi: 10.1016/j.isci.2024.109861

Figure Lengend Snippet:

Article Snippet: Rabbit polyclonal anti-SRSF1 , Abcam , Cat# ab38017; AB_882519.

Techniques: Recombinant, Enzyme-linked Immunosorbent Assay, Reverse Transcription, Labeling, Software

The primer sequences

Journal: iScience

Article Title: Circ_0007432 promotes non-small cell lung cancer progression and macrophage M2 polarization through SRSF1/KLF12 axis

doi: 10.1016/j.isci.2024.109861

Figure Lengend Snippet: The primer sequences

Article Snippet: Rabbit polyclonal anti-SRSF1 , Abcam , Cat# ab38017; AB_882519.

Techniques:

Circ_0007432 maintained KLF12 mRNA stability by recruiting SRSF1 (A) KLF12 expression was detected in tumor tissues and corresponding adjacent tissues from NSCLC patients using RT-qPCR. n = 50. (B) The relationship between circ_0007432 and KLF12 in NSCLC was analyzed using Pearson correlation analysis. n = 50. (C and D) KLF12 expression was measured in NSCLC cells (PC-9, Calu-3, H1975, A549, and H358) and BEAS-2B cells using RT-qPCR and western blot. n = 3. (E and F) KLF12 expression was evaluated in sh-NC- or sh-circ_0007432-transfected H1975 and A549 cells by RT-qPCR and western blot. n = 3. (G) The stability of KLF12 mRNA was detected in sh-NC- or sh-circ_0007432-transfected NSCLC cells by RT-qPCR. n = 3. (H) The interaction between circ_0007432 and Ago2 in NSCLC cells were evaluated using RIP. n = 3. (I and J) The interaction between circ_0007432 and SRSF1 was validated using RNA pull down and RIP. n = 3. (K and L) The interaction between KLF12 and SRSF1 was validated using RIP. n = 3. (M–O) SRSF1 and KLF12 expression was detected in sh-NC- or sh-SRSF1-transfected H1975 and A549 cells by RT-qPCR and western blot. n = 3. (P) The stability of KLF12 mRNA was detected in sh-NC- or sh-SRSF1-transfected NSCLC cells by RT-qPCR. n = 3. Data were shown as mean ± SD. Each experiment was accomplished in triplicates. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001. Student’s t test for (A), (C), (D), (H), (J), (K), and (L). Pearson correlation analysis for (B). One-way analysis of variance (ANOVA) test for (E), (F), (G), (M), (N), (O), and (P).

Journal: iScience

Article Title: Circ_0007432 promotes non-small cell lung cancer progression and macrophage M2 polarization through SRSF1/KLF12 axis

doi: 10.1016/j.isci.2024.109861

Figure Lengend Snippet: Circ_0007432 maintained KLF12 mRNA stability by recruiting SRSF1 (A) KLF12 expression was detected in tumor tissues and corresponding adjacent tissues from NSCLC patients using RT-qPCR. n = 50. (B) The relationship between circ_0007432 and KLF12 in NSCLC was analyzed using Pearson correlation analysis. n = 50. (C and D) KLF12 expression was measured in NSCLC cells (PC-9, Calu-3, H1975, A549, and H358) and BEAS-2B cells using RT-qPCR and western blot. n = 3. (E and F) KLF12 expression was evaluated in sh-NC- or sh-circ_0007432-transfected H1975 and A549 cells by RT-qPCR and western blot. n = 3. (G) The stability of KLF12 mRNA was detected in sh-NC- or sh-circ_0007432-transfected NSCLC cells by RT-qPCR. n = 3. (H) The interaction between circ_0007432 and Ago2 in NSCLC cells were evaluated using RIP. n = 3. (I and J) The interaction between circ_0007432 and SRSF1 was validated using RNA pull down and RIP. n = 3. (K and L) The interaction between KLF12 and SRSF1 was validated using RIP. n = 3. (M–O) SRSF1 and KLF12 expression was detected in sh-NC- or sh-SRSF1-transfected H1975 and A549 cells by RT-qPCR and western blot. n = 3. (P) The stability of KLF12 mRNA was detected in sh-NC- or sh-SRSF1-transfected NSCLC cells by RT-qPCR. n = 3. Data were shown as mean ± SD. Each experiment was accomplished in triplicates. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001. Student’s t test for (A), (C), (D), (H), (J), (K), and (L). Pearson correlation analysis for (B). One-way analysis of variance (ANOVA) test for (E), (F), (G), (M), (N), (O), and (P).

Article Snippet: Rabbit polyclonal anti-SRSF1 , Proteintech , Cat# 12929-2-AP; AB_2187211.

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

Journal: iScience

Article Title: Circ_0007432 promotes non-small cell lung cancer progression and macrophage M2 polarization through SRSF1/KLF12 axis

doi: 10.1016/j.isci.2024.109861

Figure Lengend Snippet:

Article Snippet: Rabbit polyclonal anti-SRSF1 , Proteintech , Cat# 12929-2-AP; AB_2187211.

Techniques: Recombinant, Enzyme-linked Immunosorbent Assay, Reverse Transcription, Labeling, Software

The primer sequences

Journal: iScience

Article Title: Circ_0007432 promotes non-small cell lung cancer progression and macrophage M2 polarization through SRSF1/KLF12 axis

doi: 10.1016/j.isci.2024.109861

Figure Lengend Snippet: The primer sequences

Article Snippet: Rabbit polyclonal anti-SRSF1 , Proteintech , Cat# 12929-2-AP; AB_2187211.

Techniques:

Association between  SRSF1  expression and the clinicopathological characteristics of patients with glioma in the Chinese Glioma Genome Atlas cohort.

Journal: Oncology Letters

Article Title: SRSF1 induces glioma progression and has a potential diagnostic application in grading primary glioma

doi: 10.3892/ol.2023.13934

Figure Lengend Snippet: Association between SRSF1 expression and the clinicopathological characteristics of patients with glioma in the Chinese Glioma Genome Atlas cohort.

Article Snippet: After sealing the non-specific binding site with 10% goat serum (Fuzhou MaixinBiotech Co., Ltd.) for 30 min at room temperature, the slices were incubated with the primary rabbit polyclonal anti-SRSF1 (1:300; Santa Cruz Biotechnology, Inc.), anti-Ki-67 (ready-to-use; Fuzhou Maixin Biotech Co., Ltd.) and anti-IDH1 R132 (ready-to-use; Fuzhou Maixin Biotech Co., Ltd.) antibodies for 60 min and secondary antibody for 30 min. DAB (Fuzhou Maixin Biotech Co., Ltd.) was then added for 5 min.

Techniques: Expressing, Mutagenesis

Association between SRSF1 mRNA expression and clinicopathological features in the Chinese Glioma Genome Atlas dataset. (A) SRSF1 expression was increased in older patients. (B) SRSF1 expression increased with WHO grade. (C) Statistical association between SRSF1 expression and histological types. No association was detected between SRSF1 expression and (D) sex, (E) IDH mutation status, (F) 1p/19q co-deletion status, and (G) both IDH mutation and 1p/19q co-deletion status. *P<0.05, **P<0.01, ***P<0.001, ****P<0.0001. SRSF1, serine and arginine rich splicing factor 1; WHO, World Health Organization.

Journal: Oncology Letters

Article Title: SRSF1 induces glioma progression and has a potential diagnostic application in grading primary glioma

doi: 10.3892/ol.2023.13934

Figure Lengend Snippet: Association between SRSF1 mRNA expression and clinicopathological features in the Chinese Glioma Genome Atlas dataset. (A) SRSF1 expression was increased in older patients. (B) SRSF1 expression increased with WHO grade. (C) Statistical association between SRSF1 expression and histological types. No association was detected between SRSF1 expression and (D) sex, (E) IDH mutation status, (F) 1p/19q co-deletion status, and (G) both IDH mutation and 1p/19q co-deletion status. *P<0.05, **P<0.01, ***P<0.001, ****P<0.0001. SRSF1, serine and arginine rich splicing factor 1; WHO, World Health Organization.

Article Snippet: After sealing the non-specific binding site with 10% goat serum (Fuzhou MaixinBiotech Co., Ltd.) for 30 min at room temperature, the slices were incubated with the primary rabbit polyclonal anti-SRSF1 (1:300; Santa Cruz Biotechnology, Inc.), anti-Ki-67 (ready-to-use; Fuzhou Maixin Biotech Co., Ltd.) and anti-IDH1 R132 (ready-to-use; Fuzhou Maixin Biotech Co., Ltd.) antibodies for 60 min and secondary antibody for 30 min. DAB (Fuzhou Maixin Biotech Co., Ltd.) was then added for 5 min.

Techniques: Expressing, Mutagenesis

Association between  SRSF1  expression and clinicopathological characteristics of the 70 patients with glioma.

Journal: Oncology Letters

Article Title: SRSF1 induces glioma progression and has a potential diagnostic application in grading primary glioma

doi: 10.3892/ol.2023.13934

Figure Lengend Snippet: Association between SRSF1 expression and clinicopathological characteristics of the 70 patients with glioma.

Article Snippet: After sealing the non-specific binding site with 10% goat serum (Fuzhou MaixinBiotech Co., Ltd.) for 30 min at room temperature, the slices were incubated with the primary rabbit polyclonal anti-SRSF1 (1:300; Santa Cruz Biotechnology, Inc.), anti-Ki-67 (ready-to-use; Fuzhou Maixin Biotech Co., Ltd.) and anti-IDH1 R132 (ready-to-use; Fuzhou Maixin Biotech Co., Ltd.) antibodies for 60 min and secondary antibody for 30 min. DAB (Fuzhou Maixin Biotech Co., Ltd.) was then added for 5 min.

Techniques: Expressing, Mutagenesis

Association between SRSF1 immunoexpression and clinicopathological features in primary glioma cases. (A) Representative H&E and IHC images of SRSF1 protein in glioma samples and normal brain tissues (original magnification, ×200). (B) Violin plot of the IRS of SRSF1 in WHO 1, WHO 2, WHO 3 and WHO 4 glioma samples. (C) Distribution of SRSF1 expression in patients with primary glioma grouped according to age. (D) Representative images of IHC staining of Ki-67 index in glioma samples (original magnifications, ×10 and ×20). (E) Violin plot of the IHC scores of SRSF1 in different Ki-67 index groups. (F) Representative images of IHC staining of IDH1 R132 mutations in glioma samples (original magnifications, ×10 and ×20). (G) Violin plot of the IHC scores of SRSF1 in IDH1 R132 mutation status. HE, hematoxylin and eosin; IHC, immunohistochemistry; SRSF1, serine and arginine rich splicing factor 1; WHO, World Health Organization.

Journal: Oncology Letters

Article Title: SRSF1 induces glioma progression and has a potential diagnostic application in grading primary glioma

doi: 10.3892/ol.2023.13934

Figure Lengend Snippet: Association between SRSF1 immunoexpression and clinicopathological features in primary glioma cases. (A) Representative H&E and IHC images of SRSF1 protein in glioma samples and normal brain tissues (original magnification, ×200). (B) Violin plot of the IRS of SRSF1 in WHO 1, WHO 2, WHO 3 and WHO 4 glioma samples. (C) Distribution of SRSF1 expression in patients with primary glioma grouped according to age. (D) Representative images of IHC staining of Ki-67 index in glioma samples (original magnifications, ×10 and ×20). (E) Violin plot of the IHC scores of SRSF1 in different Ki-67 index groups. (F) Representative images of IHC staining of IDH1 R132 mutations in glioma samples (original magnifications, ×10 and ×20). (G) Violin plot of the IHC scores of SRSF1 in IDH1 R132 mutation status. HE, hematoxylin and eosin; IHC, immunohistochemistry; SRSF1, serine and arginine rich splicing factor 1; WHO, World Health Organization.

Article Snippet: After sealing the non-specific binding site with 10% goat serum (Fuzhou MaixinBiotech Co., Ltd.) for 30 min at room temperature, the slices were incubated with the primary rabbit polyclonal anti-SRSF1 (1:300; Santa Cruz Biotechnology, Inc.), anti-Ki-67 (ready-to-use; Fuzhou Maixin Biotech Co., Ltd.) and anti-IDH1 R132 (ready-to-use; Fuzhou Maixin Biotech Co., Ltd.) antibodies for 60 min and secondary antibody for 30 min. DAB (Fuzhou Maixin Biotech Co., Ltd.) was then added for 5 min.

Techniques: Expressing, Immunohistochemistry, Mutagenesis

Kaplan-Meier overall survival analysis. Kaplan-Meier overall survival curves comparing patients with high and low expression of SRSF1 in the (A) Chinese Glioma Genome Atlas dataset and the (B) clinical cohort containing 70 patients with glioma. SRSF1, serine and arginine rich splicing factor 1.

Journal: Oncology Letters

Article Title: SRSF1 induces glioma progression and has a potential diagnostic application in grading primary glioma

doi: 10.3892/ol.2023.13934

Figure Lengend Snippet: Kaplan-Meier overall survival analysis. Kaplan-Meier overall survival curves comparing patients with high and low expression of SRSF1 in the (A) Chinese Glioma Genome Atlas dataset and the (B) clinical cohort containing 70 patients with glioma. SRSF1, serine and arginine rich splicing factor 1.

Article Snippet: After sealing the non-specific binding site with 10% goat serum (Fuzhou MaixinBiotech Co., Ltd.) for 30 min at room temperature, the slices were incubated with the primary rabbit polyclonal anti-SRSF1 (1:300; Santa Cruz Biotechnology, Inc.), anti-Ki-67 (ready-to-use; Fuzhou Maixin Biotech Co., Ltd.) and anti-IDH1 R132 (ready-to-use; Fuzhou Maixin Biotech Co., Ltd.) antibodies for 60 min and secondary antibody for 30 min. DAB (Fuzhou Maixin Biotech Co., Ltd.) was then added for 5 min.

Techniques: Expressing

SRSF1 increases the proliferation, invasion and migration of U87MG and U251 cells. (A) Knockdown and overexpression efficiency post-transduction with sh-NC, sh1-SRSF1, sh2-SRSF1 and sh3-SRSF1, or LV-SRSF1 and LV-vector, as determined by western blot analysis. Semi-quantification of SRSF1 protein expression in (B) U87MG and (C) U251 cells. OD value at 490 nm of the MTT assay in U251 and U87MG cells with stable (D) overexpression or (E) knockdown of SRSF1. Results of the colony formation assay in U251 and U87MG cells with stable (F) overexpression or (G) knockdown of SRSF1. (H) Images of the wound healing assay in U251 and U87MG cells with stable overexpression or knockdown of SRSF1 (magnification, ×100). Semi-quantification of wound healing assay in (I) U87MG and (J) U251 cells. Results of the Transwell invasion assay in U251 and U87MG cells with stable (K) overexpression (magnification, ×200) or (L) knockdown of SRSF1 (magnification, ×200). *P<0.05, **P<0.01, ***P<0.001 and ****P<0.0001. LV, lentivirus; NC, negative control; ns, not significant; sh, short hairpin; SRSF1, serine and arginine rich splicing factor 1.

Journal: Oncology Letters

Article Title: SRSF1 induces glioma progression and has a potential diagnostic application in grading primary glioma

doi: 10.3892/ol.2023.13934

Figure Lengend Snippet: SRSF1 increases the proliferation, invasion and migration of U87MG and U251 cells. (A) Knockdown and overexpression efficiency post-transduction with sh-NC, sh1-SRSF1, sh2-SRSF1 and sh3-SRSF1, or LV-SRSF1 and LV-vector, as determined by western blot analysis. Semi-quantification of SRSF1 protein expression in (B) U87MG and (C) U251 cells. OD value at 490 nm of the MTT assay in U251 and U87MG cells with stable (D) overexpression or (E) knockdown of SRSF1. Results of the colony formation assay in U251 and U87MG cells with stable (F) overexpression or (G) knockdown of SRSF1. (H) Images of the wound healing assay in U251 and U87MG cells with stable overexpression or knockdown of SRSF1 (magnification, ×100). Semi-quantification of wound healing assay in (I) U87MG and (J) U251 cells. Results of the Transwell invasion assay in U251 and U87MG cells with stable (K) overexpression (magnification, ×200) or (L) knockdown of SRSF1 (magnification, ×200). *P<0.05, **P<0.01, ***P<0.001 and ****P<0.0001. LV, lentivirus; NC, negative control; ns, not significant; sh, short hairpin; SRSF1, serine and arginine rich splicing factor 1.

Article Snippet: After sealing the non-specific binding site with 10% goat serum (Fuzhou MaixinBiotech Co., Ltd.) for 30 min at room temperature, the slices were incubated with the primary rabbit polyclonal anti-SRSF1 (1:300; Santa Cruz Biotechnology, Inc.), anti-Ki-67 (ready-to-use; Fuzhou Maixin Biotech Co., Ltd.) and anti-IDH1 R132 (ready-to-use; Fuzhou Maixin Biotech Co., Ltd.) antibodies for 60 min and secondary antibody for 30 min. DAB (Fuzhou Maixin Biotech Co., Ltd.) was then added for 5 min.

Techniques: Migration, Knockdown, Over Expression, Transduction, Plasmid Preparation, Western Blot, Expressing, MTT Assay, Colony Assay, Wound Healing Assay, Transwell Invasion Assay, Negative Control

SRSF1 resists GC apoptosis and follicular atresia. ( A ) Venn diagram of the DEGs (differentially expressed genes) between HFs and AFs and miR-9820-5p target genes predicted by PITA, Miranda, and TargetSpy. ( B ) Differentially expressed SRSF1 in HFs and AFs detected by qRT-PCR. ( C , D ) Effective knockdown of SRSF1 by si-SRSF1 qRT-PCR and western blotting (WB). ( E ) The shift of GC apoptosis rates after SRSF1 knockdown was detected by flow cytometry. Data are expressed as the mean ± SEM of three experiments; * p < 0.05, ** p < 0.01.

Journal: International Journal of Molecular Sciences

Article Title: circSLC41A1 Resists Porcine Granulosa Cell Apoptosis and Follicular Atresia by Promoting SRSF1 through miR-9820-5p Sponging

doi: 10.3390/ijms23031509

Figure Lengend Snippet: SRSF1 resists GC apoptosis and follicular atresia. ( A ) Venn diagram of the DEGs (differentially expressed genes) between HFs and AFs and miR-9820-5p target genes predicted by PITA, Miranda, and TargetSpy. ( B ) Differentially expressed SRSF1 in HFs and AFs detected by qRT-PCR. ( C , D ) Effective knockdown of SRSF1 by si-SRSF1 qRT-PCR and western blotting (WB). ( E ) The shift of GC apoptosis rates after SRSF1 knockdown was detected by flow cytometry. Data are expressed as the mean ± SEM of three experiments; * p < 0.05, ** p < 0.01.

Article Snippet: The antibodies used in this study were polyclonal anti-SRSF1 (1:1000 dilution, 12929-2-AP, Proteintech Group, Rosemont, IL, USA), polyclonal anti-tubulin (1:1000 dilution, #6181S, Cell Signaling Technology, Boston, MA, USA), polyclonal anti-Cleaved Caspase-3 (C-CASP3) (1:1000 dilution, #9664S, Cell Signaling Technology, Boston, MA, USA), and the secondary antibody (1:2000 dilution, SA00E1–2, Proteintech Group, Rosemont, IL, USA).

Techniques: Quantitative RT-PCR, Western Blot, Flow Cytometry

miR-9820-5p promotes pGCs apoptosis by targeting SRSF1 . ( A , B ) The binding of miR-9820-5p and SRSF1-WT was predicted by RNAhybrid and verified by dual-luciferase activity analysis. ( C , D ) SRSF1 mRNA and protein levels after transfection of miR-9820-5p mimics. ( E , F ) SRSF1 mRNA and protein levels after transfection of miR-9820-5p inhibitors. ( G ) The shift of GC apoptosis rates after co-transfection of miR-9820-5p inhibitors and si-SRSF1 detected by flow cytometry. Data are expressed as the mean ± SEM of three experiments; * p < 0.05, ** p < 0.01.

Journal: International Journal of Molecular Sciences

Article Title: circSLC41A1 Resists Porcine Granulosa Cell Apoptosis and Follicular Atresia by Promoting SRSF1 through miR-9820-5p Sponging

doi: 10.3390/ijms23031509

Figure Lengend Snippet: miR-9820-5p promotes pGCs apoptosis by targeting SRSF1 . ( A , B ) The binding of miR-9820-5p and SRSF1-WT was predicted by RNAhybrid and verified by dual-luciferase activity analysis. ( C , D ) SRSF1 mRNA and protein levels after transfection of miR-9820-5p mimics. ( E , F ) SRSF1 mRNA and protein levels after transfection of miR-9820-5p inhibitors. ( G ) The shift of GC apoptosis rates after co-transfection of miR-9820-5p inhibitors and si-SRSF1 detected by flow cytometry. Data are expressed as the mean ± SEM of three experiments; * p < 0.05, ** p < 0.01.

Article Snippet: The antibodies used in this study were polyclonal anti-SRSF1 (1:1000 dilution, 12929-2-AP, Proteintech Group, Rosemont, IL, USA), polyclonal anti-tubulin (1:1000 dilution, #6181S, Cell Signaling Technology, Boston, MA, USA), polyclonal anti-Cleaved Caspase-3 (C-CASP3) (1:1000 dilution, #9664S, Cell Signaling Technology, Boston, MA, USA), and the secondary antibody (1:2000 dilution, SA00E1–2, Proteintech Group, Rosemont, IL, USA).

Techniques: Binding Assay, Luciferase, Activity Assay, Transfection, Cotransfection, Flow Cytometry

circSLC41A1 inhibits GCs apoptosis by upregulating SRSF1 through sponging miR-9820-5p. ( A ) The shift of SRSF1 mRNA levels after co-transfection of si-circSLC41A1 and miR-9820-5p inhibitors detected by qRT-PCR. ( B ) The shift of SRSF1 protein levels after co-transfection of the si-circSLC41A1 and miR-9820-5p inhibitors detected by WB. ( C ) Change of GC apoptosis rates after co-transfection of si-circSLC41A1 and miR-9820-5p inhibitors detected by flow cytometry. Data are expressed as the mean ± SEM of three experiments; * p < 0.05, ** p < 0.01.

Journal: International Journal of Molecular Sciences

Article Title: circSLC41A1 Resists Porcine Granulosa Cell Apoptosis and Follicular Atresia by Promoting SRSF1 through miR-9820-5p Sponging

doi: 10.3390/ijms23031509

Figure Lengend Snippet: circSLC41A1 inhibits GCs apoptosis by upregulating SRSF1 through sponging miR-9820-5p. ( A ) The shift of SRSF1 mRNA levels after co-transfection of si-circSLC41A1 and miR-9820-5p inhibitors detected by qRT-PCR. ( B ) The shift of SRSF1 protein levels after co-transfection of the si-circSLC41A1 and miR-9820-5p inhibitors detected by WB. ( C ) Change of GC apoptosis rates after co-transfection of si-circSLC41A1 and miR-9820-5p inhibitors detected by flow cytometry. Data are expressed as the mean ± SEM of three experiments; * p < 0.05, ** p < 0.01.

Article Snippet: The antibodies used in this study were polyclonal anti-SRSF1 (1:1000 dilution, 12929-2-AP, Proteintech Group, Rosemont, IL, USA), polyclonal anti-tubulin (1:1000 dilution, #6181S, Cell Signaling Technology, Boston, MA, USA), polyclonal anti-Cleaved Caspase-3 (C-CASP3) (1:1000 dilution, #9664S, Cell Signaling Technology, Boston, MA, USA), and the secondary antibody (1:2000 dilution, SA00E1–2, Proteintech Group, Rosemont, IL, USA).

Techniques: Cotransfection, Quantitative RT-PCR, Flow Cytometry

Schematic diagram of circSLC41A1 functions in GC apoptosis. circSLC41A1 can function by competing with SRSF1 mRNA for miR-9820-5p interactions, thereby alleviating the post-transcriptional repression of SRSF1 and thus resisting GC apoptosis and follicular atresia. circSLC41A1 also had the potential to encode small circSLC41A1-134aa peptides.

Journal: International Journal of Molecular Sciences

Article Title: circSLC41A1 Resists Porcine Granulosa Cell Apoptosis and Follicular Atresia by Promoting SRSF1 through miR-9820-5p Sponging

doi: 10.3390/ijms23031509

Figure Lengend Snippet: Schematic diagram of circSLC41A1 functions in GC apoptosis. circSLC41A1 can function by competing with SRSF1 mRNA for miR-9820-5p interactions, thereby alleviating the post-transcriptional repression of SRSF1 and thus resisting GC apoptosis and follicular atresia. circSLC41A1 also had the potential to encode small circSLC41A1-134aa peptides.

Article Snippet: The antibodies used in this study were polyclonal anti-SRSF1 (1:1000 dilution, 12929-2-AP, Proteintech Group, Rosemont, IL, USA), polyclonal anti-tubulin (1:1000 dilution, #6181S, Cell Signaling Technology, Boston, MA, USA), polyclonal anti-Cleaved Caspase-3 (C-CASP3) (1:1000 dilution, #9664S, Cell Signaling Technology, Boston, MA, USA), and the secondary antibody (1:2000 dilution, SA00E1–2, Proteintech Group, Rosemont, IL, USA).

Techniques:

Inhibiting SRPKs decreases SR protein phosphorylation and increases cells harboring cytoplasmic SRSF2 granule and tubule structures in HEK293 cells. A , HEK293 cells were incubated with either DMSO (vehicle, VEH) or increasing concentrations of SRPK inhibitor SRPIN340 for a length of 12 h. Immediately following treatment, cells were harvested, run by SDS-PAGE, and immunoblotted for phosphoSR (pSR) proteins using the pan-pSR antibody mAb104. A p-TDP-43 antibody (pTDP-43 band marked by asterisk ) and a Histone H3 antibody were used to confirm specificity of SRPIN340 and equal protein loading, respectively. B , protein band intensities for SRSF4 ( purple ), SRSF6 ( blue ), SRSF10 ( red ), SRSF2/SRSF7 ( gold ), SRSF1/9 ( turquoise ), and separately, pTDP-43 ( green ) were quantified and normalized to the VEH condition (artificially set to value = 1) (multiple t tests, ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001). Error bars indicate maximum and minimum ranges of band values. The pSRSF2 signal was significantly decreased at 50 μM SRPIN340 concentration, whereas fellow RBP TDP-43 was not. C , validation of HEK293 cell extract fractionation procedure, yielding total (T), cytosolic (C), and nuclear (N) samples. The fractions were immunoblotted for the cytosolic marker GAPDH ( green ) and nuclear marker Histone H3 ( red ). D , immunoblot of nuclear-cytoplasmic fractions for total, endogenous SRSF2 in VEH and SRPIN340 conditions. E , quantification of percent nuclear SRSF2 (nuclear signal divided by sum of cytoplasmic and nuclear signals) in VEH and SRPIN340 conditions (paired t test, ∗ p value = 0.0130). F and G , immunocytochemical (ICC) staining of HEK293 cells for phosphoSRSF2 (pSRSF2)-positive nuclear speckles ( green ) and DAPI+ nuclei ( blue ) in vehicle-treated cells ( F ) and 50 μM SRPIN340-treated cells ( G ). H , the number of cytoplasmic granules observed was divided by the number of cells counted and averaged for 14 independent images in three independent replicates (two-tailed paired t test, ∗ p value = 0.0191). A minimum of 120 cells were counted in each condition per replicate. The error bars represent the range of standard deviation. I and J , ICC staining of HEK293 cells for hypophosphorylated SRSF2 (hypoSRSF2) ( green ) and DAPI+ nuclei ( blue ) in vehicle-treated cells ( I ) and 50 μM SRPIN340-treated cells ( J ). K , the fraction of cells harboring cytoplasmic SRSF2 tubule structures was quantified in four biological replicates and compared (two-tailed paired t test, ∗ p value = 0.0178). L , vehicle- and ( M ) 50 μM SRPIN340-treated HEK293 cells were stained by ICC for TDP-43 ( green ) and DAPI-stained.

Journal: The Journal of Biological Chemistry

Article Title: Phosphorylation regulates arginine-rich RNA-binding protein solubility and oligomerization

doi: 10.1016/j.jbc.2021.101306

Figure Lengend Snippet: Inhibiting SRPKs decreases SR protein phosphorylation and increases cells harboring cytoplasmic SRSF2 granule and tubule structures in HEK293 cells. A , HEK293 cells were incubated with either DMSO (vehicle, VEH) or increasing concentrations of SRPK inhibitor SRPIN340 for a length of 12 h. Immediately following treatment, cells were harvested, run by SDS-PAGE, and immunoblotted for phosphoSR (pSR) proteins using the pan-pSR antibody mAb104. A p-TDP-43 antibody (pTDP-43 band marked by asterisk ) and a Histone H3 antibody were used to confirm specificity of SRPIN340 and equal protein loading, respectively. B , protein band intensities for SRSF4 ( purple ), SRSF6 ( blue ), SRSF10 ( red ), SRSF2/SRSF7 ( gold ), SRSF1/9 ( turquoise ), and separately, pTDP-43 ( green ) were quantified and normalized to the VEH condition (artificially set to value = 1) (multiple t tests, ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001). Error bars indicate maximum and minimum ranges of band values. The pSRSF2 signal was significantly decreased at 50 μM SRPIN340 concentration, whereas fellow RBP TDP-43 was not. C , validation of HEK293 cell extract fractionation procedure, yielding total (T), cytosolic (C), and nuclear (N) samples. The fractions were immunoblotted for the cytosolic marker GAPDH ( green ) and nuclear marker Histone H3 ( red ). D , immunoblot of nuclear-cytoplasmic fractions for total, endogenous SRSF2 in VEH and SRPIN340 conditions. E , quantification of percent nuclear SRSF2 (nuclear signal divided by sum of cytoplasmic and nuclear signals) in VEH and SRPIN340 conditions (paired t test, ∗ p value = 0.0130). F and G , immunocytochemical (ICC) staining of HEK293 cells for phosphoSRSF2 (pSRSF2)-positive nuclear speckles ( green ) and DAPI+ nuclei ( blue ) in vehicle-treated cells ( F ) and 50 μM SRPIN340-treated cells ( G ). H , the number of cytoplasmic granules observed was divided by the number of cells counted and averaged for 14 independent images in three independent replicates (two-tailed paired t test, ∗ p value = 0.0191). A minimum of 120 cells were counted in each condition per replicate. The error bars represent the range of standard deviation. I and J , ICC staining of HEK293 cells for hypophosphorylated SRSF2 (hypoSRSF2) ( green ) and DAPI+ nuclei ( blue ) in vehicle-treated cells ( I ) and 50 μM SRPIN340-treated cells ( J ). K , the fraction of cells harboring cytoplasmic SRSF2 tubule structures was quantified in four biological replicates and compared (two-tailed paired t test, ∗ p value = 0.0178). L , vehicle- and ( M ) 50 μM SRPIN340-treated HEK293 cells were stained by ICC for TDP-43 ( green ) and DAPI-stained.

Article Snippet: The primary antibodies used in this study include: rabbit polyclonal anti-myc (Cell Signaling Technology 2272S), rabbit polyclonal anti-SRSF2 (Abcam ab229473), mouse monoclonal anti-SRSF2 (Clone 1Sc-4F11, Millipore Sigma 04-1550), mouse monoclonal anti-pSRSF2 (Abcam ab11826), rabbit polyclonal anti-LUC7L (Thermo Fisher 17085-1-AP), rabbit polyclonal anti-LUC7L3 (Thermo Fisher PA5-53816), rabbit polyclonal anti-RBM25 (Abcam ab72237), rabbit polyclonal anti-SRSF1 (Abcam ab38017), rabbit polyclonal anti-TDP-43 (ProteinTech Group 10782-2-AP), rabbit anti-pS409-410 TDP-43 (CosmoBio, CAC-TIP-PTD-P02), rabbit polyclonal anti-panQKI (generated by UC Davis/NIH NeuroMab Ab_10671658), rabbit polyclonal anti-ZC3H18 (Thermo Fisher PA5-59322), rabbit polyclonal anti-SRRM1 (ab221061), mouse anti-GAPDH (Abcam ab8245), rabbit polyclonal anti-Histone H3 (Abcam ab1791), rat monoclonal anti-alpha-tubulin clone YL1/2 (MAB1864), rabbit polyclonal anti-TUBB8 (ab97880), and mouse IgM anti-pSR proteins (Clone mAb104, ATCC CRL-2067, see below isolation method).

Techniques: Incubation, SDS Page, Concentration Assay, Fractionation, Marker, Western Blot, Staining, Two Tailed Test, Standard Deviation

Effects of valsartan on protein expression of SRSF1. Protein expression of SRSF1 was determined using immunofluorescence in 14 days (A, B, C) and 28 days (D, E, F).

Journal: Physiological Research

Article Title: Valsartan Prevented Neointimal Hyperplasia and Inhibited SRSF1 Expression and the TLR4–iNOS–ERK–AT1 Receptor Pathway in the Balloon-injured Rat Aorta

doi: 10.33549/physiolres.934579

Figure Lengend Snippet: Effects of valsartan on protein expression of SRSF1. Protein expression of SRSF1 was determined using immunofluorescence in 14 days (A, B, C) and 28 days (D, E, F).

Article Snippet: Polyclonal anti-SRSF1 was provided by Thermo Fisher Inc., Waltham, MA, USA.

Techniques: Expressing, Immunofluorescence