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Hnrnp f h

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HnRNP F/H is a protein involved in the regulation of gene expression and alternative splicing. It is a member of the heterogeneous nuclear ribonucleoprotein (hnRNP) family and plays a role in mRNA processing and transport.

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Lab products found in correlation

U2af65, by Santa Cruz Biotechnology (2 mentions) Hnrnpa2 b1, by Merck Group (2 mentions) Hnrnpa1, by Merck Group (2 mentions) Hnrnpc1 c2, by Merck Group (2 mentions) Protease inhibitor cocktail, by Merck Group (2 mentions) Dhx36, by Abcam (1 mentions) Ser2p, by Merck Group (1 mentions) Topoisomerase iiα, by Abcam (1 mentions) Gapdh, by Merck Group (1 mentions) Bioruptor, by Diagenode (1 mentions) Histone h3, by Abcam (1 mentions) Puromycin, by Merck Group (1 mentions) Ubiquitin, by Cell Signaling Technology (1 mentions) Caspase 3, by Cell Signaling Technology (1 mentions) Eif4a, by Santa Cruz Biotechnology (1 mentions) Mabe343, by Cell Signaling Technology (1 mentions) Histone h3, by Cell Signaling Technology (1 mentions) Ecl system, by Cytiva (1 mentions) P erk, by Cell Signaling Technology (1 mentions) Gapdh, by Santa Cruz Biotechnology (1 mentions)

6 protocols using hnrnp f h

1

Protein Extraction and Western Blot Analysis

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Cells were harvested on ice and pelleted by centrifugation at 400 g for 5 min at 4°C. Pellets were resuspended in RIPA Buffer containing complete protease inhibitors (EDTA‐free) and sonicated (Bioruptor, Diagenode). Cellular debris was pelleted at 11,000 g for 10 min at 4°C and protein concentration determined. Primary antibodies used in this study from Bethyl Laboratories were: CPSF160, CPSF100, CPSF73, CPSF30, CstF77, CstF64, CstF50, CFIm68, and CFIm59. Other antibodies used include CFIm25 (PTGlabs), PCF11 (Santa‐Cruz), and CLP1 (Epitomics). GAPDH (Sigma), Ser2P (Millipore), Topoisomerase II α (Abcam), Histone H3 (Abcam), DHX36 (Abcam), hnRNP (H/F; Abcam), p21 (Thermofisher), and p53 (Cell Signaling Technology).
Sfaxi R., Biswas B., Boldina G., Cadix M., Servant N., Chen H., Larson D.R., Dutertre M., Robert C, & Vagner S. (2023). Post‐transcriptional polyadenylation site cleavage maintains 3′‐end processing upon DNA damage. The EMBO Journal, 42(7), e112358.
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2

Immunoblotting Protein Detection Protocol

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For immunoblotting analysis, proteins were resolved on 12 or 7% denaturing polyacrylamide gels and were transferred to nitrocellulose membranes. The blots were blocked for 30 min with TBST-5% milk and then probed overnight with primary antibodies against DHX36 (1:1000, Abcam Ab70269), DHX9 (1:1000, Abcam Ab54593), DDX3X (1:1000, Santa Cruz sc-365768), LARP1 (1:1000, Bethyl A302-087A), hnRNP H/F (1:1000, Abcam Ab10689), KSRP (1:500, Bethyl A302-022A), E2F1 (1:500, Santa Cruz sc-251), eIF4A (1:500, Santa Cruz sc-50354), PERK (1:1000, Cell Signaling Technology 3192), Histone H3 (1:1000, Cell Signaling Technology 4499), EEA1 (1:500, Santa Cruz sc-53939), RPS6 (1:1000, Santa Cruz sc-74459), RPL22 (1:1000, Novus Bio NBP1-06069), GAPDH (1:1000, Santa Cruz sc-32233), γH2AX (1:1000, Millipore 05-636), Flag (1:1000, Sigma F3165-2MG), USP1 (1:600, ProteinTech 14346-1-AP), Ubiquitin (1:1000, Cell signaling Technology 3936), Puromycin (1:1000, Millipore, MABE343), PARP (1 :1000, Cell signaling 9542), Caspase-3 (1 :1000, Cell signaling 8G10), Anti-Rabbit IgG (1:5000, Ozyme 7074S), Anti-Mouse IgG (1:5000, Ozyme 7076S). The blots were developed using the ECL system (Amersham Pharmacia Biotech) according to the manufacturer’s directions.
Herviou P., Le Bras M., Dumas L., Hieblot C., Gilhodes J., Cioci G., Hugnot J.P., Ameadan A., Guillonneau F., Dassi E., Cammas A, & Millevoi S. (2020). hnRNP H/F drive RNA G-quadruplex-mediated translation linked to genomic instability and therapy resistance in glioblastoma. Nature Communications, 11, 2661.
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3

Whole-Mount Immunostaining in Locust Brain

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Whole‐mount double immunohistochemistry in the locust brain was performed by using affinity‐purified monoclonal mouse antibodies against Piwi1, Piwi2, and Ago3 (1:100, BGI), hnRNP F/H (1:100, Abcam), and U2AF65 (1:50, Santa Cruz Biotechnology). An Alexa Fluor 488‐conjugated goat anti‐mouse antibody (1:500, Life Technologies Cat. A‐11008) was used as the secondary antibody for Piwi1, Piwi2, and Ago3 staining. For lipid staining, lipids were visualized by staining the locust fat body with Nile red (0.5 mg/ml, Thermo Fisher N‐1142) for 1 h at room temperature.
Wang H., Jiang F., Liu X., Liu Q., Fu Y., Li R., Hou L., Zhang J., He J, & Kang L. (2022). Piwi/piRNAs control food intake by promoting neuropeptide F expression in locusts. EMBO Reports, 23(3), e50851.
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4

Protein Extraction and Western Blot

Cited 1 time
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Cells were resuspended in RIPA buffer: 150 mM sodium chloride, 1.0% NP-40, 0.5% sodium deoxycholate, 0.1% SDS, 50 mM Tris pH 8.0, 1 mM dithiothreitol, 0.5 mM NaVO4, and protease inhibitor cocktail (Sigma-Aldrich). After 10 min on ice, extracts were centrifuged for 10 min at 12,000 g ,supernatants were collected and used for western blot as described (49 (link)). Primary antibody incubation (1:1000) was carried out with the following antibodies: PKM1, hnRNPA1, hnRNPA2/B1, hnRNPC1/C2 (Sigma-Aldrich); PKM2 (Cell Signaling Technology, MA, USA); PTBP1, SRSF1, SRP20, SRp40/p55/p75 (Santa Cruz Biotechnology, CA, USA); hnRNPF/H (Abcam, UK). PTBP2 antibody was a generous gift of Professor Douglas L. Black (UCLA, CA). Images of the western blot were acquired as TIFF files.
Calabretta S., Bielli P., Passacantilli I., Pilozzi E., Fendrich V., Capurso G., Delle Fave G, & Sette C. (2015). Modulation of PKM alternative splicing by PTBP1 promotes gemcitabine resistance in pancreatic cancer cells. Oncogene, 35(16), 2031-2039.
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5

Locust Brain Protein Analysis

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Locust brains (8–10 individuals/sample) were collected and homogenized in lysis buffer (CWBIO) containing protease inhibitor (CWBIO). The total protein content was determined using a bicinchoninic acid protein assay kit (Thermo Scientific). The extracts were reduced, denatured, and separated by gel electrophoresis on a 10% SDS‐PAGE gel and transferred to a polyvinylidene difluoride membrane (Millipore). The membrane was incubated separately with specific antibodies against Piwi1, Piwi2, and Ago3 (mouse anti‐Piwi1 serum, 1:500; mouse anti‐Piwi2 serum, 1:500; and mouse anti‐Ago3 serum, 1:500, respectively), hnRNP F/H (Mouse monoclonal antibody, 1:2,000, Abcam), and U2AF65 (Mouse monoclonal antibody, 1:200, Santa Cruz Biotechnology). Tubulin was used as an endogenous control (rabbit polyclonal antibody, 1:5,000, CWBIO). Goat anti‐rabbit IgG was used as the secondary antibody (1:10,000, CWBIO). The intensities of the Western blot bands were quantified using densitometry with Quantity One software.
Wang H., Jiang F., Liu X., Liu Q., Fu Y., Li R., Hou L., Zhang J., He J, & Kang L. (2022). Piwi/piRNAs control food intake by promoting neuropeptide F expression in locusts. EMBO Reports, 23(3), e50851.
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6

Protein Extraction and Western Blot

Cited 1 time
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Cells were resuspended in RIPA buffer: 150 mM sodium chloride, 1.0% NP-40, 0.5% sodium deoxycholate, 0.1% SDS, 50 mM Tris pH 8.0, 1 mM dithiothreitol, 0.5 mM NaVO4, and protease inhibitor cocktail (Sigma-Aldrich). After 10 min on ice, extracts were centrifuged for 10 min at 12,000 g ,supernatants were collected and used for western blot as described (49 (link)). Primary antibody incubation (1:1000) was carried out with the following antibodies: PKM1, hnRNPA1, hnRNPA2/B1, hnRNPC1/C2 (Sigma-Aldrich); PKM2 (Cell Signaling Technology, MA, USA); PTBP1, SRSF1, SRP20, SRp40/p55/p75 (Santa Cruz Biotechnology, CA, USA); hnRNPF/H (Abcam, UK). PTBP2 antibody was a generous gift of Professor Douglas L. Black (UCLA, CA). Images of the western blot were acquired as TIFF files.
Calabretta S., Bielli P., Passacantilli I., Pilozzi E., Fendrich V., Capurso G., Delle Fave G, & Sette C. (2015). Modulation of PKM alternative splicing by PTBP1 promotes gemcitabine resistance in pancreatic cancer cells. Oncogene, 35(16), 2031-2039.
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