Biomax film

Manufactured by Kodak

Sourced in United States

BioMax film is a high-performance, fine-grain photographic film designed for use in scientific and medical imaging applications. It is well-suited for capturing high-resolution images from gel electrophoresis, autoradiography, and other lab-based imaging techniques.

Automatically generated - may contain errors

Lab products found in correlation

Supersignal west pico chemiluminescent substrate, by Thermo Fisher Scientific (8 mentions) Quantity one software, by Bio-Rad (6 mentions) Supersignal west pico, by Thermo Fisher Scientific (6 mentions) Detector block buffer, by LGC (5 mentions) Pierce bca protein assay kit, by Thermo Fisher Scientific (5 mentions) Nupage gel, by Thermo Fisher Scientific (4 mentions) M per mammalian protein extraction reagent, by Thermo Fisher Scientific (4 mentions) Bis tris gradient gel, by Thermo Fisher Scientific (4 mentions) Nitrocellulose membrane, by Merck Group (4 mentions) Nylon membrane, by Bio-Rad (3 mentions) Versadoc imaging system, by Bio-Rad (3 mentions) Nitrocellulose membrane, by Cytiva (3 mentions) Secondary antibody peroxidase conjugate, by Merck Group (3 mentions) Iblot, by Thermo Fisher Scientific (3 mentions) Enhanced chemi luminescence (ecl), by Cytiva (3 mentions) Hrp conjugated secondary antibody, by Santa Cruz Biotechnology (3 mentions) Nitrocellulose membrane, by Bio-Rad (3 mentions) Horseradish peroxidase conjugated secondary antibody, by Santa Cruz Biotechnology (3 mentions) Pvdf membrane, by Merck Group (3 mentions) Bicinchoninic acid protein assay, by Avantor (2 mentions)

89 protocols using biomax film

Western Blot Quantification of Neuronal Signaling Proteins

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

PCAs were harvested in a lysis buffer [50 mM Tris HCl (pH 7.4), 150 mM NaCl, 1% Triton X-100 and protease inhibitors (Sigma-Aldrich)]. The total amount of protein was determined by the bicinchoninic acid protein assay (Amresco, Solon, OH, USA). Samples (50 μg protein) were separated by 10% SDS-PAGE and electroblotted to polyvinylidene fluoride membranes, which were blocked by incubation in 5% non-fat milk powder dissolved in TBS-T (150 mM NaCl, 50 mM Tris and 0.05% Tween-20). Following transfer, proteins were probed using a primary antibody; NMDAR1 (1:1000; Cell Signaling Technology, Inc.), CaM (1:1000; Abcam), nNOS (1:1500; Abcam), sGC (1:1000; Abcam) and cGMP (1:200, Santa Cruz Biotechnology). Then, horseradish peroxidase-conjugated secondary antibody was used. Following extensive washing, protein bands detected by antibodies were visualized by enhanced chemiluminescence reagent (Pierce Biotechnology, Inc., Rockford, IL, USA) following exposure on Kodak BioMax film (Kodak, Rochester, NY, USA). The films were subsequently scanned and the band intensities were quantified using Quantity One software (Bio-Rad Laboratories, Inc., Hercules, CA, USA).

DING S., HUANG W., YE Y., YANG J., HU J., WANG X., LIU L., LU Q, & LIN Y. (2014). Elevated intracranial dopamine impairs the glutamate-nitric oxide-cyclic guanosine monophosphate pathway in cortical astrocytes in rats with minimal hepatic encephalopathy. Molecular Medicine Reports, 10(3), 1215-1224.

+ Open protocol

+ Expand

Detection of sflt-1 mRNA Expression

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

For the detection of sflt-1 mRNA expression, total RNA was isolated from HUVEC or excised mammary tumors using the TRIZOL Reagent (Gibco BRL, Paisley, Scotland). The RNA concentration was determined spectrophotometrically and normalized by ethidium bromide staining of agarose gels. Twenty five μg of total RNA was separated on 1% agarose-formaldehyde gels, transferred onto nylon membranes (Sartorius, Göttingen, Germany) and hybridized with ³²P-labeled 450-bp sflt-1 cDNA probe. The sflt-1 probe was generated by polymerase chain reaction using the 5′ flt-1 (nt 1808-1827; 5′-GCACCTTGGTTGTGGCTGAC-3′) [29 (link)] and 3′ sflt-5 (nt 2238-2258; 5′-GAGATCCGAGAGAAAACAGCC-3′) primers and Adsflt DNA as template. Membranes were hybridized with 1 × 10⁶ cpm/mL of QuikHyb solution (Stratagene, La Jolla, CA, USA), washed once with 2X SSC/0.1% SDS for 15 min at 23 °C, then twice with 2X SSC/0.1% SDS for 30 min at 63 °C and exposed to Kodak Bio-Max film (Eastman Kodak, Rochester, NY) at −80 °C with intensifying screens overnight (HUVEC RNA analysis) or for 2 days (tumor RNA analysis).

Felici A., Bottaro D.P., Mangoni A., Reusch P., Marmé D., Kovesdi I., De Silva D.M., Lee Y.H., Capogrossi M.C, & Mühlhauser J. (2022). Regression of Human Breast Carcinoma in Nude Mice after Adsflt Gene Therapy Is Mediated by Tumor Vascular Endothelial Cell Apoptosis. Cancers, 14(24), 6175.

+ Open protocol

+ Expand

Glycosylation Analysis of Rhodopsin

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

Neuroretinae from wt and D190N animals were collected and homogenized. Protein concentrations were measured by BCA protein assay. For glycosylation analyses, 5 μg of protein were treated with Endoglycosidase H (Endo-H, New England Labs, Ipswich, MA) or Peptide: N-Glycosidase F (PNGase F, New England Labs), according to the manufacturer’s protocol. Consequently, proteins were separated by SDS-PAGE in 12% acrylamide gels and transferred to PVDF membranes. Membranes were then blocked in dry skim milk and PBS Tween 0.1%. Later, membranes were incubated with mouse anti-Rhodopsin antibody (ID4, 1:5000, Santa Cruz Biotech) overnight at 4 °C. On the following day, membranes were incubated in goat anti-mouse secondary antibody (1:10,000, Santa Cruz Biotech) for 1 h at RT. Antibody complexes were visualized by chemiluminescence detection (Immobilon Western, Millipore Corporation, Billerica MA) using Kodak Biomax film (Kodak, Rochester, NY).

Sancho-Pelluz J., Cui X., Lee W., Tsai Y.T., Wu W.H., Justus S., Washington I., Hsu C.W., Park K.S., Koch S., Velez G., Bassuk A.G., Mahajan V.B., Lin C.S, & Tsang S.H. (2019). Mechanisms of neurodegeneration in a preclinical autosomal dominant retinitis pigmentosa knock-in model with a RhoD190N mutation. Cellular and molecular life sciences : CMLS, 76(18), 3657-3665.

+ Open protocol

+ Expand

Protein Separation and Detection by SDS-PAGE and Western Blot

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

SDS–PAGE analysis was used to separate proteins that were then electroblotted onto Westran-S PVDF membrane (Whatman; 310413096) for 1 h in chilled transfer buffer. Membranes were blocked in 5% nonfat dry milk (NFDM) for 1 h at 4°C and incubated with primary antibody in 3% NFDM overnight at 4°C. Membranes were washed in wash buffer and HRP-conjugated secondary antibodies were incubated at 4°C for 2 h. ECL2 (Thermo Scientific; #PI80196) was used for chemiluminescence detection with Kodak Bio-Max film (Kodak).

Mageeney C.M, & Ware V.C. (2019). Specialized eRpL22 paralogue-specific ribosomes regulate specific mRNA translation in spermatogenesis in Drosophila melanogaster. Molecular Biology of the Cell, 30(17), 2240-2253.

+ Open protocol

+ Expand

Quantitative Western Blot Analysis

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

PHNs or hippocampal tissues were harvested in lysis buffer (Sigma-Aldrich). The total protein was measured with a bicinchoninic acid protein assay (Amresco). Samples of 50 μg of protein were separated by SDS-PAGE and then were electroblotted to PVDF membranes. The membranes were blocked by incubation in 5% non-fat dry milk dissolved in TBS-T (150 mM NaCl, 0.05% Tween, and 2050 mM Tris). Proteins were probed using a primary antibody following electroblotting: pERK1/2 (ERK1 (pThr202/pTyr204) + ERK2 (pThr185/pTyr187)) (monoclonal/polyclonal, 1:1000), ERK1/2 (monoclonal/polyclonal, 1:1000), pnNOS Ser847 (monoclonal, 1:1000), pnNOS Ser1417 (monoclonal, 1:1000), nNOS (monoclonal, 1:2000), PSD95 (monoclonal, 1:2000), β-actin (monoclonal, 1:1000; Abcam), pRSK Ser369 (monoclonal, 1:1500; Biorbyt), or RSK (monoclonal, 1:5000; Biorbyt). Horseradish peroxidase-conjugated anti-rabbit secondary antibody (Abcam) was then used. Protein bands detected by antibodies were visualized by ECL reagent (Pierce) after extensive washing and were then exposed on Kodak BioMax film (Kodak). The films were scanned and the band intensities were quantified using Quantity One software. Densitometrical measurements were expressed as folds of proteins relative to GAPDH expression levels.

Ding S., Zhuge W., Wang X., Yang J., Lin Y., Wang C., Hu J, & Zhuge Q. (2017). DA Negatively Regulates IGF-I Actions Implicated in Cognitive Function via Interaction of PSD95 and nNOS in Minimal Hepatic Encephalopathy. Frontiers in Cellular Neuroscience, 11, 258.

+ Open protocol

+ Expand

Autoradiographic Mapping of Cerebral Blood Flow

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

Brains were flash frozen and serially sectioned (20-μm coronal slices, 300-μm interslice distance). Sections were exposed to Kodak Biomax film along with 16 radioactive ¹⁴C standards (GE Healthcare, Chicago, IL, USA). Autoradiograms of brain slices were digitized and CBF-related tissue radioactivity was measured by the classic [¹⁴C]-iodoantipyrine method [12 (link)]. In this method, there is a strict linear proportionality between tissue radioactivity and CBF when data is captured within a brief interval (~10 sec.) after the tracer injection [13 (link)].

Guo Y., Wang Z., Prathap S, & Holschneider D.P. (2017). Recruitment of Prefrontal-Striatal Circuit in Response to Skilled Motor Challenge. Neuroreport, 28(18), 1187-1194.

+ Open protocol

+ Expand

Autoradiographic Quantification of KOR Activation

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

Brains were collected from saline or CFA injected rats 48h post-injection and were snap-frozen with isopentane at −30 °C, and stored in −80 °C until fu rther processing. The brains were then coronal-sectioned via cryostat (20 μm thick) at −20 °C, and thaw-mounted on SuperFrost charged slides. Sections were pre-incubated in assay buffer (50mM Tris-HCl, 3mM MgCl2, 0.2mM EGTA, 100 mM NaCl, 2 mM GDP, 1 μM DPCPX, pH=7.4) for 15 min. Agonist-stimulated KOR activity was determined by incubating brain sections in [³⁵S] GTPγS (40 pM) with U69,593 (10 μM) +/− JdTic (10 μM) for 1 hour at RT. After incubation, slides were washed 2x in ice-cold wash buffer (50 mm Tris-HCl, pH 7.4) followed by a brief wash in ice-cold deionized water (30 sec). Slides were air-dried and exposed to Kodak Biomax film together with [¹⁴C] standards for 2 days. Films were developed using Kodak GBX Developer and RapidFix solutions. Films were digitally analyzed and quantified using MicroComputer Image Device (MCID) normalized to the [¹⁴C] standard curve, measured in dpm/mg (MCID Imaging Research, St. Catherine, Ontario, Canada). The resulting agonist-stimulated samples were compared to non-agonist-treated brain samples to determine the percent activation of KOR above basal.

Massaly N., Copits B.A., Wilson-Poe A.R., Hipólito L., Markovic T., Yoon H.J., Liu S., Walicki M.C., Bhatti D.L., Sirohi S., Klaas A., Walker B.M., Neve R., Cahill C.M., Shoghi K.I., Gereau RW I.V., McCall J.G., Al-Hasani R., Bruchas M.R, & Morón J.A. (2019). Pain-Induced Negative Affect Is Mediated Via Recruitment Of The Nucleus Accumbens Kappa Opioid System. Neuron, 102(3), 564-573.e6.

+ 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

The total amount of protein in the lysates was determined by BCA protein assay (AMRESCO). Samples (50 μg protein) were separated by 10% SDS-PAGE and electroblotted to PVDF membranes, which were blocked by incubation in 5% non-fat dry milk dissolved in TBS-T (150 mM NaCl, 50 mM Tris, 0.05% Tween 20). Following transfer, proteins were probed using the following primary antibodies: D₁R, DARPP32, GABA_ARβ1, GABA_ARβ3, TrkB, pAKT, AKT, synaptotagmin, synapsin I, PSD95, spinophilin, and β-actin (Abcam). Then, horseradish peroxidase-conjugated secondary antibody was used. After extensive washing, protein bands detected by antibodies were visualized by ECL reagent (Thermo) after exposure on Kodak BioMax film (Kodak).

Ding S., Zhuge W., Hu J., Yang J., Wang X., Wen F., Wang C, & Zhuge Q. (2018). Baicalin reverses the impairment of synaptogenesis induced by dopamine burden via the stimulation of GABAAR–TrkB interaction in minimal hepatic encephalopathy. Psychopharmacology, 235(4), 1163-1178.

+ Open protocol

+ Expand

Protein Expression Analysis by Western Blot

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

Cells were washed 2x with sterile PBS and lysed at approximately 500,000 cells/mL of ice-cold lysis buffer (80mM Tris-HCL pH 6.8, 15% glycerol, 2% SDS and 10 uL/mL commercial protease/phosphatase inhibitor cocktail). Cell lysis was followed by 1 minute of sonication and then centrifugation at 17,500rpm for 15 minutes. The protein content of cell lysate was determined using a bicinchoninic acid (BCA) protein assay kit (Pierce Chemical, Rockford, IL). Proteins were separated by SDS–PAGE using a mini-Protean system (Bio-Rad, Hercules, CA) and wet-transferred to a PVDF membrane (Amersham Biosciences, Uppsala, Sweden), followed by blocking with 3% BSA in 1x-TBST (0.1% Tween-20) overnight. Membranes were incubated with primary antibody (in 3% BSA) specific to iNOS & FBXW7 (Abcam; 1:1000, 1 hr at RT); p-STAT3 & STAT3 (Santa Cruz Biotechnology; 1:500, overnight at 4°C); TLR4 (Novus Biologicals NB100-56580; 1:1,000, 2hr at RT) and β-actin (Cell Signaling Technologies; 1:3000, 1 hr at RT). After washing with 1X TBST, blots were incubated with the appropriate HRP-conjugated secondary antibody for 1 hr at room temperature (RT). Blots were washed before addition of ECL plus^™ (Amersham Biosciences) and detection of bands with Kodak Biomax^™ film.

Deiuliis J.A., Syed R., Duggineni D., Rutsky J., Rengasamy P., Zhang J., Huang K., Needleman B., Mikami D., Perry K., Hazey J, & Rajagopalan S. (2016). Visceral Adipose MicroRNA 223 Is Upregulated in Human and Murine Obesity and Modulates the Inflammatory Phenotype of Macrophages. PLoS ONE, 11(11), e0165962.

+ Open protocol

+ Expand

Lapatinib Treatment Induces EGFR Expression

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

Cells were treated with 10 μM lapatinib for the indicated (0-24 h) times. After each treatment, cells were washed with cold phosphate-buffered saline (PBS), and were lysed with Laemmli sample buffer for protein extraction. The lysates were centrifuged, and the supernatant was recovered. Western blot analysis was performed as described previously [17] . In brief, whole cell lysates were heated, and proteins were separated on a 2-15% gradient polyacrylamide gel and transferred to a polyvinylidene fluoride membrane (Daiichi Kagaku, Tokyo, Japan). Membranes blocked with Detector Block ® buffer (Kirkegaard & Perry Laboratories, Gaithersburg, MD, USA) were incubated for 1 h with an anti-EGFR antibody (1:1,000 dilution) (Boster Biological Technology, Pleasanton, CA, USA) and anti-β-actin antibody (1:10,000 dilution) (ab8227, Abcam, Cambridge, MA). After washes with PBS containing 0.05% Tween 20, the membrane was incubated with horseradish peroxidaselabeled anti-rabbit immunoglobulin G (Daiichi Kagaku). Hybridization signals were detected by the chemiluminescent substrate SuperSignal West Pico (Pierce Chemical Co., Rockford, IL, USA), and the membrane was exposed to BioMax film (Eastman Kodak Co., Rochester, NY, USA).

Asari Y., Kageyama K., Sugiyama A., Kogawa H., Niioka K, & Daimon M. (2019). Lapatinib decreases the ACTH production and proliferation of corticotroph tumor cells. Endocrine journal, 66(6).

+ 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!