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Anti cugbp1

Manufactured by Santa Cruz Biotechnology
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Anti-CUGBP1 is a laboratory reagent used for the detection and analysis of CUGBP1 protein expression in various biological samples. It is a specific antibody that binds to and identifies the CUGBP1 protein.

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Lab products found in correlation

Anti hur, by Santa Cruz Biotechnology (3 mentions) Chemiluminescence reagent, by PerkinElmer (2 mentions) Sds page gel, by Bio-Rad (2 mentions) Pvdf membrane, by GE Healthcare (2 mentions) Anti gapdh, by Santa Cruz Biotechnology (2 mentions) Anti human survivin antibody, by R&D Systems (2 mentions) Image lab quantification software, by Bio-Rad (2 mentions) Anti elavl1, by Santa Cruz Biotechnology (1 mentions) Anti khsrp, by Cell Signaling Technology (1 mentions) Anti cdkn1b p27, by Cell Signaling Technology (1 mentions) Anti hnrnpd, by Merck Group (1 mentions) Anti p53, by Cell Signaling Technology (1 mentions) Irdye 800cw, by LI COR (1 mentions) Anti β tubulin, by Merck Group (1 mentions) Anti β actin, by Merck Group (1 mentions) Nitrocellulose membrane, by Bio-Rad (1 mentions) Anti gfp, by Roche (1 mentions) Nitrocellulose membrane, by Thermo Fisher Scientific (1 mentions) β actin antibody, by Santa Cruz Biotechnology (1 mentions) Anti ago2 clone 4g8, by Fujifilm (1 mentions)

7 protocols using anti cugbp1

1

Protein Detection by Western Blotting

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Proteins were resolved on SDS polyacrylamide (PAA) gels (12.5%) and transferred to nitrocellulose membranes (Bio-Rad, #1,620,115). Membranes were blocked in PBS containing 0.1% Tween-20 and 3% BSA and probed with the designated primary antibodies and with IRDye 800CW (Licor #926-32,210, #926-32,211) or IRDye 650RD secondary antibodies (Licor #926-68,070, #926-68,071). The blots were visualized with the Odyssey® CLx Imaging System. The following primary antibodies were used: anti-β-actin (1:2,000; Sigma, #A1978), anti-β-Tubulin (1:2,000; Sigma, #T0198), anti–ELAVL1 (1:500; Santa Cruz, #sc-5261), anti-KHSRP (1;1000; Cell Signalling, #13,398), anti-SNW1 (1:1,000; Abcam, #ab67165), anti-PDAP1 (1:500; Cell Signalling, #4300), anti-p53 (1:1,000; Cell Signalling, #9282), anti-CDKN1B/p27 (1:500; Cell Signalling, #3686), anti-hnRNPD (1:1,000; Millipore, #07-260), anti-CUGBP1 (1:500; Santa Cruz, #sc-20,003) and anti-GFP (1:2,000; Roche, #11,814,460,001).
Iadevaia V., Wouters M.D., Kanitz A., Matia-González A.M., Laing E.E, & Gerber A.P. (2019). Tandem RNA isolation reveals functional rearrangement of RNA-binding proteins on CDKN1B/p27Kip1 3’UTRs in cisplatin treated cells. RNA Biology, 17(1), 33-46.
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2

Western Blot Analysis of Protein Expression

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30 μg of protein from whole cell lysates was resolved on 10% SDS-PAGE gels (Bio-Rad Laboratories, Hercules, CA) and transferred onto PVDF membranes (GE Healthcare, Piscataway, NJ). After transfer, membranes were blocked in 5% nonfat milk in TBST and membranes were incubated with specific antibodies (overnight at 4°C) followed by horseradish peroxidaseconjugated anti-mouse or anti-rabbit (Santa Cruz, Dallas, TX) immunoglobulin for 1 hour at RT. Signal was detected by Chemiluminescence Reagent (PerkinElmer, Waltham, MA) and visualized by autoradiography. Anti-human survivin antibody was purchased from R&D Systems (Minneapolis, MN). Anti-CUG-BP1, anti-HuR, and anti-GAPDH antibodies were purchased from Santa Cruz Biotechnology (Dallas, TX). All primary anti-bodies were used at a dilution of 1:2000 and all secondary antibodies were used at a dilution of 1:4000. Signal intensity was quantified using Image Lab quantification software (Bio-Rad, Hercules, CA).
Phatak P., Byrnes K.A., Mansour D., Liu L., Cao S., Li R., Rao J.N., Turner D.J., Wang J.Y, & Donahue J.M. (2015). Overexpression of miR-214-3p in Esophageal Squamous Cancer Cells Enhances Sensitivity to Cisplatin by Targeting Survivin Directly and Indirectly Through CUG-BP1. Oncogene, 35(16), 2087-2097.
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3

Immunoblotting Protocol for Protein Detection

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Whole cell extracts or immunoprecipitated protein complexes were resolved by electrophoresis using SDS-10% polyacrylamide gel (Bio-Rad, Hercules, CA) and transferred to nitrocellulose membranes (Thermo Fisher Scientific, Waltham, MA). Membranes were blocked with 5% milk in Tris-buffered saline/Tween-20 for 1 hr at room temperature, and then probed overnight at 4°C with pan-specific anti-NFI (Cat #sc-74444), anti-Ago1 (Cat #sc-376696), anti-HuR (Cat #sc-5261),anti-CUGBP1 (Cat #sc-56649) (Santa Cruz Biotechnology, Santa Cruz, CA), or anti-Ago2 (clone #4G8; Wako, Richmod, VA) antibody. After washing, blots were incubated with the appropriate HRP-conjugated secondary antibody for 2 hr at room temperature. Proteins were detected with the enhanced chemiluminescence detection system (Thermo Fisher Scientific, Waltham, MA), the bands were visualized using the ChemiDoc XRS System (Bio-Rad), and the images were captured with the Image Lab Software V3.0. Membranes were stripped and reprobed with β-actin antibody (Santa Cruz) as a loading control.
Bah I., Alkhateeb T., Kumbhare A., Youssef D., Yao Z., Hawkins G.A., McCall C.E, & El Gazzar M. (2020). HuR promotes miRNA-mediated upregulation of NFI-A protein expression in MDSCs during murine sepsis. Molecular immunology, 123, 97-105.
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4

Western Blot Protein Detection

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Following cell lysis, protein concentration was assessed using the Bio-Rad DC Protein Assay (Bio-Rad:500–0111) and protein (2–40 μg) was resolved by denaturing polyacrylamide gel electrophoresis (SDS-PAGE) and transferred to polyvinylidene fluoride (PDVF) membranes (Immunobilon Transfer Membranes:IPVH00010). Transferred membranes were blocked with 5% milk for 30 minutes and probed with appropriate antibody in 1% milk solution for either 1 hour at room temperature or 12 hours at 4°C, with three 10 min washes with 1XPBS-0.05% Tween 20 between each antibody incubation. Antibodies included: Anti-Stau1 [1:1000] (Abcam:ab73478), Anti-GAPDH [1:10,000] (Abcam:ab8245), Anti-β-Actin [1:500] (Santa Cruz:sc-47778), Anti-CUGBP1 [1:1000] (Santa Cruz:sc-20003), Anti-hnRNP H [1:5000] (Abcam:10374), Anti-MyoD [1:300] (BD Pharmingen: 554130), Anti-MBNL1 antibody [1:300] (Abnova:H00004154), Anti-HA F7 probe [1:1000] (Santa Cruz:sc-7392). Secondary antibodies included: Mouse-anti-Rabbit HRP [1:20,000] (Jackson ImmunoResearch:211-032-171) and Goat-anti-Rabbit HRP [1:10,000] (Molecular Probes:MP 02764). Proteins on membranes were detected with Millipore-Luminata Crescendo Western HRP Substrate (WBLUR0500) and visualized on film (HyBlot CL Autoradiography Film:E3018).
Bondy-Chorney E., Crawford Parks T.E., Ravel-Chapuis A., Klinck R., Rocheleau L., Pelchat M., Chabot B., Jasmin B.J, & Côté J. (2016). Staufen1 Regulates Multiple Alternative Splicing Events either Positively or Negatively in DM1 Indicating Its Role as a Disease Modifier. PLoS Genetics, 12(1), e1005827.
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5

Western Blot Analysis of Protein Expression

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30 μg of protein from whole cell lysates was resolved on 10% SDS-PAGE gels (Bio-Rad Laboratories, Hercules, CA) and transferred onto PVDF membranes (GE Healthcare, Piscataway, NJ). After transfer, membranes were blocked in 5% nonfat milk in TBST and membranes were incubated with specific antibodies (overnight at 4°C) followed by horseradish peroxidaseconjugated anti-mouse or anti-rabbit (Santa Cruz, Dallas, TX) immunoglobulin for 1 hour at RT. Signal was detected by Chemiluminescence Reagent (PerkinElmer, Waltham, MA) and visualized by autoradiography. Anti-human survivin antibody was purchased from R&D Systems (Minneapolis, MN). Anti-CUG-BP1, anti-HuR, and anti-GAPDH antibodies were purchased from Santa Cruz Biotechnology (Dallas, TX). All primary anti-bodies were used at a dilution of 1:2000 and all secondary antibodies were used at a dilution of 1:4000. Signal intensity was quantified using Image Lab quantification software (Bio-Rad, Hercules, CA).
Phatak P., Byrnes K.A., Mansour D., Liu L., Cao S., Li R., Rao J.N., Turner D.J., Wang J.Y, & Donahue J.M. (2015). Overexpression of miR-214-3p in Esophageal Squamous Cancer Cells Enhances Sensitivity to Cisplatin by Targeting Survivin Directly and Indirectly Through CUG-BP1. Oncogene, 35(16), 2087-2097.
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6

Immunofluorescence analysis of cell adhesion and cytokine expression

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Cells adhered to glass coated with BD Cell-Tak Cell and Tissue Adhesive (BD PharMingen, San Jose, CA) were fixed with 4% paraformaldehyde (40 min, room temperature), stained with the following antibodies: anti-CUGBP1 (Santa Cruz Biotechnology, SC-20003, 1: 100), α-SMA (Santa Cruz Biotechnology, SC-32251, 1: 50), anti-IFN-γ (Abcam, ab133566, 1: 200)and detected with secondary antibodies: goat anti-mouse IgG2a conjugated to Alexa Fluor 594 (Invitrogen, A-21135, 1: 1,000), goat anti-mouse IgG1 conjugated to Alexa Fluor 647 (Invitrogen, A-21240, 1: 1,000), goat anti-rabbit IgG conjugated to Alexa Fluor 488 (Invitrogen, A-11008, 1: 1000). The coverslips were counterstained with DAPI and imaged with a confocal laser scanning microscope (Olympus, Lake Success, NY). Examination was blindly carried out.
Wu X., Wu X., Ma Y., Shao F., Tan Y., Tan T., Gu L., Zhou Y., Sun B., Sun Y., Wu X, & Xu Q. (2016). CUG-binding protein 1 regulates HSC activation and liver fibrogenesis. Nature Communications, 7, 13498.
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7

Antibody Detection in Cell Lines

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The antibodies used were anti-DDX3 (Bethyl Laboratories/Cederlane, Burlington, Canada), anti-TIA1 and anti-CUGBP1 (Santa Cruz Biotechnology, Santa Cruz, CA), anti-PABP1 (Cell Signalling/New England Biolabs, Whitby, Canada), anti-Staufen1 and anti–glyceraldehyde-3-phosphate dehydrogenase (GAPDH; Abcam/Cederlane), and anti-MyHC (MF20; Developmental Studies Hybridoma Bank, Iowa City, IA).
Ravel-Chapuis A., Klein Gunnewiek A., Bélanger G., Crawford Parks T.E., Côté J, & Jasmin B.J. (2016). Staufen1 impairs stress granule formation in skeletal muscle cells from myotonic dystrophy type 1 patients. Molecular Biology of the Cell, 27(11), 1728-1739.
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