Typhoon 9400 variable mode imager

Manufactured by Cytiva

Sourced in United Kingdom

The Typhoon 9400 is a variable mode imager designed for the detection and analysis of fluorescent and chemiluminescent signals in a variety of sample types, including gels, blots, and microplates. The instrument uses a laser-based detection system to capture high-resolution images with a wide dynamic range.

Automatically generated - may contain errors

Lab products found in correlation

Bca kit, by Thermo Fisher Scientific (3 mentions) Imagequant tl software, by Cytiva (2 mentions) Pvdf membrane, by Bio-Rad (2 mentions) Myecl imager, by Thermo Fisher Scientific (1 mentions) Ecl plu, by Cytiva (1 mentions) Myimageanalysis software, by Thermo Fisher Scientific (1 mentions) Polyvinylidine difluoride pvdf membrane, by Bio-Rad (1 mentions) Ecl plus substrate, by Thermo Fisher Scientific (1 mentions) Anti hdac1, by Cell Signaling Technology (1 mentions) Anti atf3, by Santa Cruz Biotechnology (1 mentions) Ne per nuclear and cytoplasmic extraction kit, by Thermo Fisher Scientific (1 mentions) Luminata forte western hrp substrate, by Merck Group (1 mentions) Phosphatase inhibitor, by Merck Group (1 mentions) Ecl plus reagent, by Cytiva (1 mentions)

Close spelling variants of this product

Typhoon Variable Mode Imager Typhoon 9400 imager Typhoon 9400 Typhoon imager

9 protocols using typhoon 9400 variable mode imager

Gel-Based Protein-DNA Interaction Analysis

Check if the same lab product or an alternative is used in the 5 most similar protocols

Samples of FAM-labeled
dsDNAs and DBD⁶⁰¹ were incubated for 10 min at room temperature
in buffer HN₅₀ and then loaded on 8% acrylamide/bisacrylamide
1× TBE mini gels with running buffer prechilled at 4 °C.
Electrophoretic migration was conducted at a constant voltage of 80
V for 70 min at 4 °C. Gels were scanned using a Typhoon 9400
Variable Mode Imager (Amersham BioSciences, GE Healthcare Bio Sciences)
after excitation of the fluorophore with the blue laser (488 nm) setting.
EMSAs involving unlabeled DNA were subjected to identical incubation
and electrophoresis treatments, stained in 1× TBE buffer with
GelRed (Phenix Research, Candler, NC) for 15 min, and scanned on an
Alpha Imager HP imager (Protein Simple, Santa Clara, CA).

Feldmann E.A, & Galletto R. (2014). The DNA-Binding Domain of Yeast Rap1 Interacts with Double-Stranded DNA in Multiple Binding Modes. Biochemistry, 53(48), 7471-7483.

+ Open protocol

+ Expand

Vascular Signaling Pathway Analysis

Cited 4 times

Check if the same lab product or an alternative is used in the 5 most similar protocols

Aortic inflammation and vascular insulin and VEGF signaling were analyzed by performing Western blots to examine IκBα degradation, a marker of NF-κBα activation, and insulin or VEGF-induced Akt phosphorylation (17 (link)–20 (link), 31 (link)). In addition, IκBα degradation was examined to test for the activation of the NF-κBα pathway by FFA in HUVECs. As described before (17 (link)–20 (link), 30 (link), 31 (link)), tissue and cells were lysed, and proteins were separated by SDS-PAGE, transferred to PVDF membranes (Bio-Rad, Hercules, CA), and probed with antibodies against IκBα and actin or phospho-Akt (Ser473) and Akt. Antibodies against IκBα, phospho-Akt (Ser473), and Akt (1:1,000) were obtained from Cell Signaling Technology (Danvers, MA), and the actin (1:2,000) antibody was purchased from Sigma-Aldrich. The blots were developed with ECL plus (Amersham Biosciences, Piscataway, NJ; or Pierce, Thermo Fisher, Waltham, MA), and band intensities (Typhoon 9400 variable mode imager Amersham Biosciences; or myECL Imager, Thermo Fisher) were quantified using Image Quant TL software (Amersham Biosciences, Piscataway, NJ; or myImageAnalysis Software, Thermo Fisher).

Hill B.G., Rood B., Ribble A, & Haberzettl P. (2021). Fine particulate matter (PM2.5) inhalation-induced alterations in the plasma lipidome as promoters of vascular inflammation and insulin resistance. American Journal of Physiology - Heart and Circulatory Physiology, 320(5), H1836-H1850.

+ Open protocol

+ Expand

Ethidium Bromide Fluorescence Imaging

Check if the same lab product or an alternative is used in the 5 most similar protocols

Samples were 15 µM in nucleotides or ~ 0.8 µM in duplex concentration; the individual samples were incubated in 1 µg/mL ethidium bromide concentrations in 100 mM sodium chloride, 10 mM sodium phosphate, and 0.1 mM EDTA at pH 6.5 in PCR tubes. The tubes were imaged on a Typhoon 9400 Variable Mode Imager from Amersham Biosciences. Excitation for imaging occurred at 532 nm and emission was measured at 610 nm.

Thompson R.A., Spring A.M., Sheng J., Huang Z, & Germann M.W. (2014). The Importance of Fitting In: Conformational Preference of Selenium 2’ Modifications in Nucleosides and Helical Structures. Journal of biomolecular structure & dynamics, 33(2), 289-297.

+ Open protocol

+ Expand

Western Blot Analysis of α7-nAChR Signaling

Check if the same lab product or an alternative is used in the 5 most similar protocols

After pre-treatment with MLA or ACB or si-RNA of α7-nAChR or corynoxenine for 12 h, cells were infected for 24 h with either rL-RVG,NDV or PBS and then washed with ice-cold PBS for 3 times and lysed by using the lysis buffer RIPA containing 1 mM PMSF for 30 min on ice. Next the lysates were collected and the protein concentrations were quantified using a BCA kit (Thermo Fisher Scientific, USA). Equal quantities of protein were separated by using a 10% SDS-PAGE and the proteins were then transferred to polyvinylidinedifluoride (PVDF) membranes (Bio-Rad Laboratories). The membranes were then blocked with 5% BSA in Tris-buffered saline containing 0.1% Tween 20 (TBST, at pH 7.5) for about 2 h at room temperature before washing them with TBST for 15 min for 3 times. Next the membranes were incubated with antibodies at 4 °C overnight with the following antibodies: anti-α7 nAChR, anti-P-MEK, anti-MEK, anti-P-ERK, anti-ERK, anti-E-cadherin, anti-N-cadherin and anti-Vementin. Proteins were detected with HRP-conjugated secondary antibodies for 1 h at room temperature. The protein bands were visualized with a Typhoon 9400 variable mode imager (Amersham Biosciences, UK) using chemiluminescence (ECL Plus Substrate, Thermo Fisher Scientific, USA).

Bu X., Zhang A., Chen Z., Zhang X., Zhang R., Yin C., Zhang J., Zhang Y, & Yan Y. (2019). Migration of gastric cancer is suppressed by recombinant Newcastle disease virus (rL-RVG) via regulating α7-nicotinic acetylcholine receptors/ERK- EMT. BMC Cancer, 19, 976.

+ Open protocol

+ Expand

Biophysical Characterization of Rap1-DNA Interactions

Check if the same lab product or an alternative is used in the 5 most similar protocols

All fluorescence titrations were performed with an L-format PC1 spectrofluorimeter (ISS, Champaign, IL) equipped with Glenn-Thompson polarizers. Measurements of the anisotropy and total fluorescence intensity of FAM-labeled DNA were recorded using excitation and emission wavelengths of 480 nm and 530 nm respectively, as described (25 ). Electrophoretic Mobility Shift Assays (EMSA) of Rap1^DBD with labeled or unlabeled dsDNAs were performed on 8% acrylamide/bisacrylamide 1X TBE mini gels with running buffer pre-chilled at 4 °C. Gels were scanned using a Typhoon 9400 Variable Mode Imager (Amersham BioSciences, GE Healthcare Bio Sciences, Piscataway, NJ) or for unlabeled DNAs stained with GelRed (Phenix Research, Candler, NC) and scanned on an Alpha Imager HP imager (Protein Simple, Santa Clara, CA).

Feldmann E.A., Koc K.N, & Galletto R. (2015). Alternative Arrangements of Telomeric Recognition Sites Regulate the Binding Mode of the DNA-Binding Domain of Yeast Rap1. Biophysical chemistry, 198, 1-8.

+ Open protocol

+ Expand

Zymosan-induced Atf3 and Hdac1 in RAW 264.7 Macrophages

Check if the same lab product or an alternative is used in the 5 most similar protocols

RAW 264.7 (ATCC) macrophages were incubated with zymosan (50µg/ml) for 6h. The NE-PER Nuclear and Cytoplasmic Extraction kit (Thermo Scientific) was used to obtain nuclear extracts that were analyzed by immunoblotting with anti-Atf3 (Santa Cruz) and anti-Hdac1 (Cell Signaling) antibodies. Immunoblots were developed using Luminata Forte Western HRP Substrate (Millipore), detected using a Typhoon 9400 variable mode imager (Amersham Biosciences), and quantified with ImageQuant TL.

Hellmann J., Tang Y., Zhang M.J., Hai T., Bhatnagar A., Srivastava S, & Spite M. (2015). Atf3 negatively regulates Ptgs2/Cox2 expression during acute inflammation. Prostaglandins & other lipid mediators, 0, 49-56.

+ Open protocol

+ Expand

Quantitative Western Blot Analysis of Aorta and PVAT

Cited 1 time

Check if the same lab product or an alternative is used in the 5 most similar protocols

Western blot analysis was performed with lysates of aorta and PVAT as described (Conklin et al., 2015 (link); Haberzettl, McCracken, et al., 2016 (link)). Briefly, collected tissues were lysed in RIPA buffer (50 mM Tris•HCl, pH 7.4; 150 mM NaCl; 1 mM EDTA; 0.25% sodium desoxycholate; 1% NP‐40; 1:100 protease inhibitor cocktail, Pierce, Rockford, IL; 1:100 phosphatase inhibitor, Sigma‐Aldrich) and proteins were separated by SDS‐PAGE and transferred to PVDF membranes (Bio‐Rad, Hercules, CA). Membranes were probed with antibodies against phospho‐Akt (Ser473) and Akt (1:1000; Cell Signaling Technology, Danvers, MA), or protein–acrolein adducts, and then developed using ECL® plus reagent (Amersham Biosciences, Piscataway, NJ). Detected band intensities (Typhoon 9400 variable mode imager, Amersham Biosciences) were quantified using Image Quant TL software (Amersham Biosciences) and normalized either to appropriate loading controls or total protein staining (amido black).

Haberzettl P., Jin L., Riggs D.W., Zhao J., O’Toole T.E, & Conklin D.J. (2021). Fine particulate matter air pollution and aortic perivascular adipose tissue: Oxidative stress, leptin, and vascular dysfunction. Physiological Reports, 9(15), e14980.

+ Open protocol

+ Expand

Mapping Nucleotide Cleavage Sites in mRNA

Check if the same lab product or an alternative is used in the 5 most similar protocols

2-dimensional thin layer chromatography was performed as previously described 43 . In brief, twice-purified polyadenylated mRNA was digested with T1 ribonuclease. This results in mRNA cleavage immediately following guanosine residues. The RNA mixture is then labeled with [γ-32 P]ATP using T4 PNK , so that all nucleotides following a guanosine are labelled with 32 P on the 5' end. Excess [γ-32 P]ATP is removed by apyrase. RNA is then digested into single nucleotides using P1 nuclease. The digested RNA was then spotted on PEI-cellullose plates and developed as previously described 43 . Radioactively labelled nucleotides were detected using a phosphor storage screen and Amersham Biosciences Typhoon 9400 Variable Mode Imager.

Ries R.J., Pickering B.F., Poh H.X., Namkoong S, & Jaffrey S.R. (2023). m⁶A governs length-dependent enrichment of mRNAs in stress granules. Nature structural & molecular biology, 30(10).

+ Open protocol

+ Expand

Mapping Nucleotide Cleavage Sites in mRNA

Check if the same lab product or an alternative is used in the 5 most similar protocols

Ries R.J., Pickering B.F., Poh H.X., Namkoong S., & Jaffrey S.R. (2022). m⁶A governs length-dependent enrichment of mRNAs in stress granules.

+ Open protocol

+ Expand

About PubCompare

Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.

We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.

However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.

Ready to get started?

Revolutionizing how scientists
search and build protocols!