Odyssey nitrocellulose membrane

Manufactured by LI COR

Sourced in United States, Niger

The Odyssey Nitrocellulose Membrane is a product designed for use in Western blot analysis. It is a thin, porous membrane made of nitrocellulose material that allows for the efficient transfer and immobilization of proteins from a gel to the membrane surface. The membrane facilitates the detection and quantification of specific proteins using fluorescent-based detection methods.

Automatically generated - may contain errors

Lab products found in correlation

Odyssey blocking buffer, by LI COR (11 mentions) Odyssey infrared imager, by LI COR (5 mentions) Mini protean tgx 4 20 gel, by Bio-Rad (4 mentions) Image studio software, by LI COR (4 mentions) Odyssey infrared imaging system, by LI COR (4 mentions) Odyssey blocking buffer tbs, by LI COR (4 mentions) Nupage novex 4 12 bis tris gel, by Thermo Fisher Scientific (3 mentions) Ripa buffer, by Thermo Fisher Scientific (3 mentions) Pageruler plus prestained protein ladder, by Thermo Fisher Scientific (3 mentions) Intercept pbs blocking buffer, by LI COR (3 mentions) Irdye conjugated secondary antibody, by LI COR (3 mentions) Restore western blot stripping buffer, by Thermo Fisher Scientific (3 mentions) Sapphire biomolecular imager, by Azure Biosystems (3 mentions) Nupage bis tris precast polyacrylamide gels, by Thermo Fisher Scientific (3 mentions) Sapphire capture software, by Azure Biosystems (3 mentions) Irdye secondary antibody, by LI COR (3 mentions) Bradford method, by Bioworld Technology (2 mentions) Irdye 800cw conjugated goat anti rabbit igg, by LI COR (2 mentions) Anti gapdh, by Santa Cruz Biotechnology (2 mentions) Seeblue plus2 pre stained standard, by Thermo Fisher Scientific (2 mentions)

Close spelling variants of this product

Nitrocellulose membranes (100 citations) Nitrocellulose (10 citations)

47 protocols using odyssey nitrocellulose membrane

Immunoblotting Analysis of Sigma-1 Receptor and IP3R3 in Rat and Mouse Cells

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

Whole-cell lysates obtained from rat nucleus accumbens and NG108-15 cells (mouse neuroblastoma x rat glioma) were separated on Mini-PROTEAN TGX 4–20% gels (Bio-Rad, Hercules, CA) by SDS-PAGE followed by immunoblotting. Proteins were transferred to an Odyssey nitrocellulose membrane (Li-Cor Biosciences; Lincoln, NE). After blocking with Odyssey blocking buffer, the membranes were incubated overnight with primary antibody against σ₁R (rabbit polyclonal, 1:100, OriGene Technologies, Rockville, MD), or IP₃R3 (mouse monoclonal, 1:1,000, BD Biosciences, San Jose, CA). An antibody against β-actin (mouse monoclonal, 1:10,000; Sigma Aldrich) was used to confirm equal protein loading. Membranes were washed with Tris-buffered saline-Tween 20 (TBST) and incubated with the secondary antibodies: IRDye 800CW conjugated goat anti-rabbit IgG, and IRDye 680 conjugated goat anti-mouse IgG (1:10,000, 1 h at room temperature). Membranes were then washed in TBST and scanned using Li-Cor Odyssey Infrared and Odyssey V.3 software.

Barr J.L., Deliu E., Brailoiu G.C., Zhao P., Yan G., Abood M.E., Unterwald E.M, & Brailoiu E. (2015). Mechanisms of Activation of Nucleus Accumbens Neurons by Cocaine via Sigma-1 Receptor - Inositol 1,4,5-Trisphosphate - Transient Receptor Potential Canonical Channel Pathways. Cell calcium, 58(2), 196-207.

+ Open protocol

+ Expand

Dot-blot Quantification of ATX3 and PNPase

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

The 5 μL of TE samples were diluted in 100 μL final volume of Sample Buffer, and then were boiled for 10 min and vacuum filtered in 48-well dot-blot apparatus through Odyssey nitrocellulose membrane (LI-COR, Lincoln, NE, USA). ATX3 variants and PNPase proteins were revealed using anti-AT3 Z46 (1:5000) rabbit polyclonal and anti-PNPase (1:150,000) rabbit polyclonal antibodies. Dot density was quantified using Image Studio™ software (LI-COR, Lincoln, NE, USA).

Ami D., Sciandrone B., Mereghetti P., Falvo J., Catelani T., Visentin C., Tortora P., Ventura S., Natalello A, & Regonesi M.E. (2021). Pathological ATX3 Expression Induces Cell Perturbations in E. coli as Revealed by Biochemical and Biophysical Investigations. International Journal of Molecular Sciences, 22(2), 943.

+ Open protocol

+ Expand

Western Blot Analysis of Bag Proteins

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

Cells were washed with PBS (Sigma-Aldrich, St. Louis MO) twice and lysed in RIPA buffer. Cells were then passed through a 26 gauge needle to break them up completely. Unbroken cells and cell debris were removed by centrifugation and supernatant was used as total cell lysate for Western blots. Protein concentration was determined by the Bradford method (bioWorld, Columbus OH). Equal amounts of proteins were separated on SDS-PAGE and transferred to Odyssey Nitrocellulose membrane (Li-Cor, Lincoln NE) by wet transfer (Bio-Rad, Philadelphia PA). Membranes were blocked with Odyssey blocking buffer (Li-Cor) for 1h at room temperature and probed with primary antibody for overnight at 4°C with rocking. The membranes were further washed thrice with PBST and then probed with respective secondary antibody for 1h at room temperature. Signal was detected by an Odyssey scanner after washing twice with PBST. The following primary antibodies were used for Western blotting: Bag1, Bag2, Bag4 (Novus Biologicals, Littleton CO), Bag3 (Protein Tech, Chicago IL), Bag6 (R&D system, Minneapolis MN), CHOP, GRP78, Bag5 (Abcam, Cambridge MA) PDI, pELFα, ELFα (Cell Signaling, Danvers MA).

Gupta M.K., Tahrir F.G., Knezevic T., White M.K., Gordon J., Cheung J.Y., Khalili K, & Feldman A.M. (2016). GRP78 Interacting Partner Bag5 Responds to ER Stress and Protects Cardiomyocytes from ER Stress-Induced Apoptosis. Journal of cellular biochemistry, 117(8), 1813-1821.

+ Open protocol

+ Expand

GPR55 Protein Expression Analysis

Cited 2 times

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

Whole-cell lysates of RBMVEC and rat cerebral cortex were separated on Mini-PROTEAN TGX 4–20% gels (Bio-Rad, Hercules, CA) by SDS-PAGE followed by immunoblotting as previously described (Altmann et al., 2015 (link), Brailoiu et al., 2016 (link)). Proteins were transferred to an Odyssey nitrocellulose membrane (LI-COR Biosciences, Lincoln, NE). After incubation with blocking buffer, membranes were incubated overnight with primary antibody against GPR55 (rabbit polyclonal against the N-terminus of rat GPR55 (1:1000, cat # ADI-905-900; Enzo Life Sciences, Inc., Farmingdale, NY). An antibody against β-actin (mouse monoclonal, 1:10,000; cat # A5441, Sigma-Aldrich) was used to confirm equal protein loading. Membranes were washed with Tris-buffered saline-Tween 20 (TBST) and incubated with the secondary antibodies: IRDye 800CW conjugated goat anti-rabbit IgG (1:10,000, Cat # 926-32211, LI-COR) and IRDye 680 conjugated goat anti-mouse IgG (1:10,000, Cat # 926-32220, LI-COR) for 1 h at room temperature. Membranes were then washed in TBST and scanned using a LI-COR Odyssey Infrared Imager. Densitometric analysis was performed using Odyssey V.3 software (LI-COR).

Leo L.M., Familusi B., Hoang M., Smith R., Lindenau K., Sporici K.T., Brailoiu E., Abood M.E, & Brailoiu G.C. (2019). GPR55-mediated effects on brain microvascular endothelial cells and the blood-brain barrier. Neuroscience, 414, 88-98.

+ Open protocol

+ Expand

Western Blot Analysis of Neuronal Proteins

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

Neurons in culture were washed with PBS twice and lysed in RIPA buffer (50 mM Tris–HCl, pH 7.5, 150 mM NaCl, 0.5% NP40, 1:100 protease inhibitor cocktail (Calbiochem, San Diego, CA), plus mammalian protease inhibitor cocktail (Sigma-Aldrich, MO, USA). The protein concentration was determined by the Bradford method (BioWorld, Columbus, OH). Equal amounts of proteins were separated on SDS-PAGE and transferred to Odyssey nitrocellulose membrane (Li-Cor, Lincoln, NE) by wet transfer (Bio-Rad, Philadelphia, PA). The following primary antibodies were used for western blotting: anti-GPCR GPR7 antibody for NPBWR1 detection (1:1,000, Abcam, Cambridge, MA), anti-GAPDH (1:2,000, Santa Cruz, sc-32233), anti-BCL-2 antibody (1:1000, Santa Cruz, sc-7382), anti-BAG3 antibody (1:1000, Proteintech, 10599-1-AP), anti-p62 antibody (1:1000, Proteintech, 18420-I-AP), anti-LC3 antibody (1:1000, Cell signaling, 3868), anti-ß3 tubulin antibody (1:1000, Santa Cruz,), anti-cleaved-caspase-3 antibody (1:1000, Cell signaling, 9661), anti-MCU (1:1000, abcam, ab121499).

Torkzaban B., Natarajaseenivasan K., Mohseni Ahooyi T., Shekarabi M., Amini S., Langford T.D, & Khalili K. (2020). The lncRNA LOC102549805 (U1) modulates neurotoxicity of HIV-1 Tat protein. Cell Death & Disease, 11(10), 835.

+ Open protocol

+ Expand

Western Blot Analysis of Pax6 Protein

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

Cells were lysed directly in the NuPAGE® LDS Sample Buffer (NP0007, Life Technologies) with DTT. Samples were run on NuPAGE Novex 4–12% Bis-Tris gels (NP0322, Life Technologies), and blotted onto the Odyssey nitrocellulose membrane (LI-COR Biosciences, Lincoln, NE). Membranes were blocked for 1 hour in room temperature using Odyssey blocking buffer (LI-COR Biosciences). Primary and secondary antibodies were diluted in the blocking buffer, and membranes were incubated at room temperature for at least 1 hour. Washing was done after each antibody incubation 5 times for 5 minutes in TBS containing 0.1% Tween-20. Membranes were incubated with IRDye Coupled secondary antibodies, and images were acquired with the Odyssey Sa Infrared Imaging System (LI-COR Biosciences).
Antibodies used were rabbit polyclonal anti-Pax6 antibody 1:1200 (AB2237, Merck Millipore), rabbit anti-Actin 1:2000 (A2066, Sigma-Aldrich), anti-rabbit 800 CW 1:10 000 (#926-32214 and #926-32213, LI-COR Biosciences). Molecular weight markers used were SeeBlue Plus2 Prestained Standard (Invitrogen) and MagicMark XP Western Protein Standard (Invitrogen).

Kiselev Y., Andersen S., Johannessen C., Fjukstad B., Standahl Olsen K., Stenvold H., Al-Saad S., Donnem T., Richardsen E., Bremnes R.M, & Rasmussen Busund L.T. (2018). Transcription factor PAX6 as a novel prognostic factor and putative tumour suppressor in non-small cell lung cancer. Scientific Reports, 8, 5059.

+ Open protocol

+ Expand

Quantification of Feline Cerebral Cortex Proteins

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

Samples of feline cerebral cortex (5–10 mg) were homogenized in 400 μl of RIPA buffer (PIERCE, ThermoFisher, Waltham, MA, USA) with a hand-held micro-pestle for 30 sec, followed by passage through a 25G needle and kept on ice for 20 min. After centrifugation at 16,200 ×g for 30 min at 4°C, the soluble fraction was transferred to a new tube and total protein concentration was determined by DC protein assay (Bio-Rad, Hercules, CA, USA). Following quantification, 33 μg of protein sample were mixed with 4× Laemmli sample buffer (Bio-Rad) containing 400mM Dithiothreitol. Protein fractions were separated with 18% sodium dodecyl sulfate polyacrylamide gel electrophoresis, and transferred to Odyssey® nitrocellulose membrane (Li-Cor, Lincoln, NE, USA), blocked in LI-COR Odyssey blocking buffer (Lincoln, NE) for 1 h, and incubated with rabbit polyclonal anti-PEA-15 (C-terminal amino acids 93–123 of Human PEA15) antibody ab135694 (Abcam, Cambridge, UK) at a concentration of 1:100 and anti-GAPDH antibody (MAB374, EMD Millipore, Burlington, MA, USA) at a concentration of 1:500. Secondary antibodies (1:15,000) were IRDye®680RD Goat anti-Rabbit IgG (H+L, Li-Cor) and IRDye®800CW Goat anti-Mouse IgG (H+L, Li-Cor), respectively. The fluorescent signal was detected using Odyssey® Infrared imaging system (Li-Cor).

Graff E.C., Cochran J.N., Kaelin C.B., Day K., Gray-Edwards H.L., Watanabe R., Koehler J.W., Falgoust R.A., Prokop J.W., Myers R.M., Cox N.R., Barsh G.S, & Martin D.R. (2020). PEA15 loss of function and defective cerebral development in the domestic cat. PLoS Genetics, 16(12), e1008671.

+ Open protocol

+ Expand

Quantifying Cellular Protein Levels

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

3D Matrigel samples were dissolved in Lysis Buffer 6 (R&D Systems, Minneapolis, MN) with protease & phosphatase inhibitors (Thermo Scientific, Rockford, IL). One Pl of each sample was spotted onto a LI-COR Biosciences Odyssey Nitrocellulose Membrane (LI-COR Biosciences, Lincoln, NE). The dot blot was then stained for Monoclonal Anti-β-Actin-Peroxidase antibody produced in mouse (Sigma Aldrich, St. Louis, MO) overnight at a dilution ratio of 1:50,000. Then, after sufficient washing the following day, the blot was coated with 2 ml of Pierce ECL Western Blotting Substrate (Thermo Scientific, Rockford, IL). Chemiluminescent detection imaging was then conducted using the Chemi exposure setting on a Li-Cor Odyssey FC machine (LI-COR Biosciences, Lincoln, NE) and then quantified using Image Studio software (LI-COR Biosciences, Lincoln, NE).

Choi S.H., Bylykbashi E., Chatila Z.K., Lee S.W., Pulli B., Clemenson G.D., Kim E., Rompala A., Oram M.K., Asselin C., Aronson J., Zhang C., Miller S.J., Lesinski A., Chen J.W., Kim D.Y., van Praag H., Spiegelman B.M., Gage F.H, & Tanzi R.E. (2018). Induced Adult Neurogenesis plus BDNF Mimicks the Effects of Exercise on Cognition in an Alzheimer’s Mouse Model. Science (New York, N.Y.), 361(6406), eaan8821.

+ Open protocol

+ Expand

Monitoring ATX3-Q55 Protein Production by Western Blot

Cited 1 time

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

The production of ATX3-Q55 was monitored by WB analysis. Crude extracts were obtained from aliquots of OD₆₀₀ ~ 4 of cells collected at different growth times according to the procedure previously described [28 (link)] and denatured in the Laemmli buffer as previously described. A preliminary SDS-PAGE analysis was carried out to determine the amount of crude extracts used for WB analysis. Comparable amount of crude extracts (~ OD₆₀₀: 0.20) was loaded on 12% SDS-PAGE and then blotted on Odyssey nitrocellulose membrane (LI-COR Biosciences, Lincoln, NE, USA) using the Mini Protean electroblotting system (Bio-Rad, Hercules, CA, USA) and Towbin transfer buffer (25 mM Tris, 192 mM glycine, 20% (v/v) methanol, pH 8.3) (constant current 400 mA for 2 h at 4 °C). Rabbit polyclonal primary anti-AT3 Z46 (1:5000) and anti-PNPase (1:150,000) antibodies were diluted in 5% milk and incubated overnight; anti-rabbit fluorescent IRDye^® 800CW (LI-COR Biosciences, Lincoln, NE, USA) was used as a secondary antibody for both primary antibodies. Signal quantification was carried out using Image Studio software (LI-COR Biosciences, Lincoln, NE, USA). The experiment was performed in triplicate.

de Divitiis M., Ami D., Pessina A., Palmioli A., Sciandrone B., Airoldi C., Regonesi M.E., Brambilla L., Lotti M., Natalello A., Brocca S, & Mangiagalli M. (2023). Cheese-whey permeate improves the fitness of Escherichia coli cells during recombinant protein production. Biotechnology for Biofuels and Bioproducts, 16, 30.

+ Open protocol

+ Expand

Phospho-Erk1/2 Detection in CTLL2 Cells

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

Protein lysate from CTLL2 cells (ATCC) cells was prepared using RIPA buffer (Thermo Fisher Scientific) and 20 μg of protein per sample were separated on a NuPAGE 4–12% Bis-Tris Protein gel (Thermo Fisher Scientific) and blotted onto a 0.22 μm Odyssey nitrocellulose membrane (LI-COR). Phospho Erk1/2 was detected using a pErk antibody Thr202/204 #9101 (Cell Signaling Technology).

Koliesnik I.O., Kuipers H.F., Medina C.O., Zihsler S., Liu D., Van Belleghem J.D, & Bollyky P.L. (2020). The Heparan Sulfate Mimetic PG545 Modulates T Cell Responses and Prevents Delayed-Type Hypersensitivity. Frontiers in Immunology, 11, 132.

+ 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!