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> Phenomena > Natural Phenomenon or Process > Chemiluminescence

Chemiluminescence

Chemiluminescence is a form of luminescence where light is emitted from a chemical reaction.
This process occurs when a molecule in an excited state relaxes to a lower energy state, releasing a photon.
Chemiluminescence has a wide range of applications in various fields, including analytical chemistry, biomedical research, and environmental monitoring.
It is often used as a detection method in assays and imaging techniques, providing sensitive and quantitative measurements.
Chemiluminescence can be a valuable tool for researchers, offering insight into biological processes, chemical reactions, and the presence of specific analytes.
Understanding the principles and applications of chemiluminescence is crucial for optimizing experimental workflows and obtaining reproducible, data-driven insights.

Most cited protocols related to «Chemiluminescence»

1
Transient Luciferase Assay in Tobacco
Tobacco leaves were harvested approximately 70 hours after infiltration with Agrobacterium containing the plasmid encoding the respective genes under control of the 35S promoter. Tissue was frozen in liquid nitrogen, protein was extracted as described by [30 ] and assayed as described by [18 (link),17 (link)].
Firefly Luciferase and Renillia luciferase were assayed using the dual luciferase assay reagents (Promega, Madison, USA). After inoculation and a transient incubation of 2–4 days, 2 cm leaf discs were harvested and ground in 500 μl of Passive Lysis Buffer. Five μl of a 1/100 dilution of this crude extract was assayed in 40 μl of Luciferase Assay Buffer, and the chemiluminescence measured. 40 μl of Stop and Glow™ buffer was then added and a second chemiluminescence measurement made. Absolute RLU were measured in a Turner 20/20 luminometer, with a 5 second delay and 15-second measurement. Data was collected as ratio or, for multiple data points (e.g. several leaves of different ages were infiltrated), the regression-gradient and regression-standard-error were used as a measure of relative promoter strength. Ratios are without units as both the light measurement and protein concentrations are identical. Background controls were run with only the promoter-LUC, 35S-REN reporter plasmid (no TF). In some cases, positive controls were run using a TF with known activity.
Hellens R.P., Allan A.C., Friel E.N., Bolitho K., Grafton K., Templeton M.D., Karunairetnam S., Gleave A.P, & Laing W.A. (2005). Transient expression vectors for functional genomics, quantification of promoter activity and RNA silencing in plants. Plant Methods, 1, 13.
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Publication 2005
Agrobacterium Biological Assay Buffers Chemiluminescence Chemiluminescent Assays Complex Extracts Freezing Gene Expression Regulation Light Luciferases Luciferases, Firefly Nicotiana Nitrogen Plasmids Promega Proteins Technique, Dilution Tissues Transients Vaccination
2
Protein Extraction and Immunoblot Analysis
Total proteins were extracted from 100 mg of sample using extraction buffer (100 mM Tris-Cl pH8, 150 mM NaCl, 0.6% IGEPAL, 1 mM EDTA, 3 mM DTT with protease inhibitors, PMSF, leupeptin, aprotinin, pepstatin, antipain, chymostatin, Na2VO3, NaF, MG132, and MG115. Proteins were separated on a 10% polyacrylamide gel. Immunoblot analysis was carried out using mouse α-GFP (1:2000; Invitrogen) for TuMV GFP and rat α-HA (1:500) antibody for pCas13a. The antigens were detected by chemiluminescence using an ECL-detecting reagent (Thermo Scientific).
Aman R., Ali Z., Butt H., Mahas A., Aljedaani F., Khan M.Z., Ding S, & Mahfouz M. (2018). RNA virus interference via CRISPR/Cas13a system in plants. Genome Biology, 19, 1.
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Publication 2018
Antigens Antipain Aprotinin Buffers Chemiluminescence chymostatin Edetic Acid Elafin Immunoblotting Immunoglobulins leupeptin MG 115 MG 132 Mice, House pepstatin polyacrylamide gels Proteins Sodium Chloride Tromethamine
3
SDS-PAGE and Western Blot Analysis
Protein samples were treated for 30 min at 50°C in a sample-treating solution containing 2% SDS and 5% β-mercaptoethanol. The samples were then loaded onto a 12% or 15% SDS-polyacrylamide gel (7.0×8.3 cm ×0.75 mm) and electrophoresed using Mini-Protean Tetra system (Bio-Rad) at 15 mA (current constant). After electrophoresis, proteins separated on the gel were transferred onto a methanol-activated PVDF membrane (Immobilon-P, pore size 0.45 µm, Millipore) or a nitrocellulose membrane (Protran BA85, pore size 0.45 µm, Whatman) for 2 h using TE22 Mighty Small Transfer system (Hoefer Scientific) at 100 V (voltage constant). The membrane was then treated with or without phosphate-buffered saline (PBS) containing 0.4% PFA for 30 min at room temperature, followed by blocking for 1 h with 5% skim milk (Carnation) in Tris-buffered saline containing 0.1% Tween-20 (TBS-T). The membrane was then incubated for 1 h with a primary antibody in TBS-T containing 1% skim milk. As primary antibody, mouse monoclonal anti-α-syn antibodies 4D6 and LB509 (Santa Cruz Biotechnology) and rabbit monoclonal anti-phospho α-syn antibody EP1536Y (Epitomics, Burlingame, CA) were used at a dilution 1∶1,000, and rabbit polyclonal anti-actin antibody (Sigma) was also used at a dilution 1∶5,000. After washing with TBS-T containing 1% skim milk for 5 min three times, the membrane was incubated for 1 h with a secondary antibody, horseradish peroxidase-conjugated anti-mouse IgG or anti-rabbit IgG antibody (Santa Cruz Biotechnology), in TBS-T containing 1% skim milk. After washing with TBS-T for 10 min three times, protein bands on the membrane were detected by chemiluminescence method using ECL-Plus immunoblotting detection system (GE Healthcare).
Lee B.R, & Kamitani T. (2011). Improved Immunodetection of Endogenous α-Synuclein. PLoS ONE, 6(8), e23939.
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Publication 2011
2-Mercaptoethanol Actins Anti-Antibodies anti-IgG Antibodies, Anti-Idiotypic Carnation Chemiluminescence Electrophoresis Horseradish Peroxidase Immobilon P Immunoglobulins Membrane Proteins Methanol Mice, House Milk, Cow's Nitrocellulose Phosphates polyacrylamide gels polyvinylidene fluoride Proteins Rabbits Saline Solution Technique, Dilution Tetragonopterus Tissue, Membrane Tween 20
4
Western Blot Analysis of Transgene Expression
M-PER mammalian protein extraction reagent (Thermo Scientific, USA) was used to
lyse the human cell lines 24 hr post-transfection, zebrafish embryos at 24 hour
post-fertilization (hpf) and mouse liver 3 day post-injection (dpi). Each lysate
was separated by 12% sodium dodecyl sulfate polyacrylamide gel
electrophoresis (SDS-PAGE) and transferred to nitrocellulose membrane (Pall
Corporation; NY, USA). Subsequently, the membrane was probed with the indicated
primary antibody (anti-EGFP [1∶1000, Santa Cruz Biotechnology,
catalog # sc-9996] and anti-DsRed [1∶1000, Clontech, catalog #
632393]), washed with TBST (0.2 M Tris, 1.37 M NaCl,0.1% Tween-20,
pH7.6), probed with HRP-conjugated goat anti-mouse antibody (1∶4000, Santa
Cruz Biotechnology, catalog # sc-2005). The bound antibody was detected by
enhanced chemiluminescence (AniGen, Korea) and then exposed to X-ray film (AGFA,
Belgium).
Because anti-DsRed antibody has been successfully used to decorate mCherry
protein [12] (link),
anti-DsRed antibody was used to visualize the mCherry protein.
Kim J.H., Lee S.R., Li L.H., Park H.J., Park J.H., Lee K.Y., Kim M.K., Shin B.A, & Choi S.Y. (2011). High Cleavage Efficiency of a 2A Peptide Derived from Porcine Teschovirus-1 in Human Cell Lines, Zebrafish and Mice. PLoS ONE, 6(4), e18556.
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Publication 2011
Antibodies, Anti-Idiotypic Cell Lines Chemiluminescence Embryo Fertilization Goat Homo sapiens Immunoglobulins Liver Mammals Mus Nitrocellulose Proteins SDS-PAGE Sodium Chloride Tissue, Membrane Transfection Tromethamine Tween 20 X-Ray Film Zebrafish
5
Stevia Transgenic Plant Molecular Analysis
Genomic DNA (gDNA) was extracted from approximately 600 mg of Stevia leaves using cetyltrimethylammonium bromide (CTAB)-based extraction method [45 ]. The final gDNA pellet was washed with ice-cold 75% ethanol and dissolved in water.
PCR amplification was carried out from 100 ng of gDNA extracted from each line of transgenic Stevia to check for the presence of T-DNA using forward primers specific to the CaMV 35S promoter and reverse primers specific to the 3′-end of SrDXS1 or SrKAH (Additional file 9: Table S1).
Southern blot analysis for detection of transgene integrations and number of integration sites was performed using a DIG-labelled probe specific to the full-length nptII (Roche). The purity of the synthesized probes was checked by electrophoresis on a 1% agarose gel. gDNAs extracted from the SrDXS1-OE and SrKAH-OE lines were digested with HindIII and XbaI, respectively. After digestion, the fragments were resolved on a 0.8% agarose gel together with DIG-labelled DNA molecular weight marker II (Roche). The agarose gel was treated with 0.2 M HCl followed by denaturation solution (0.5 M NaOH, 1.5 M NaCl) and neutralization solution (1 M Tris-Cl pH 7.4, 1.5 M NaCl) and transferred to a positively charged nylon membrane (Hybond-N+, GE healthcare life sciences) in 20x SSC (3.0 M NaCl, 0.3 M sodium citrate, pH 7.0). After the transfer, UV-crosslinking was carried out using Stratalinker 2400 (Stratagene, USA). Then, DIG-based Southern blot hybridization was performed according to manufacturer’s instructions (Roche). Chemiluminescence from the membrane was acquired with the ChemiDoc Touch Imaging System (Bio-Rad, USA).
Zheng J., Zhuang Y., Mao H.Z, & Jang I.C. (2019). Overexpression of SrDXS1 and SrKAH enhances steviol glycosides content in transgenic Stevia plants. BMC Plant Biology, 19, 1.
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Publication 2019
Animals, Transgenic Cetrimonium Bromide Chemiluminescence Cold Temperature Digestion Electrophoresis Ethanol Genome Markers, DNA Nylons Oligonucleotide Primers Sepharose Sodium Chloride Sodium Citrate Southern Blotting Stevia Tissue, Membrane Touch Transgenes Tromethamine

Most recents protocols related to «Chemiluminescence»

1
EV Protein Isolation and Western Blot
Total protein was isolated from EVs using Pierce RIPA lysis buffer with Halt protease and phosphatase inhibitor cocktail (Thermo Fisher, Waltham, MA), and protein concentration was determined using the Pierce BCA protein assay kit (Thermo Fisher). For Western blotting, samples were prepared in Laemmli buffer, boiled at 95 °C for 5 min, and 5 μg protein was loaded. Proteins were separated by SDS-PAGE using 4–15% TGX Gels (Criterion, Bio-Rad, Hercules, CA) by running at 200 V at room temperature. Proteins were transferred for 60 min at 100 V on ice onto a nitrocellulose membrane in 20% methanol Tris-glycine buffer. The Revert Total Protein Stain Kit (Li-Cor Biosciences, Lincoln, NE) or Ponceau S solution (Thermo Fisher) was used to stain total protein, and the membranes were imaged to verify transfer efficiency and loading. The membranes were subsequently blocked in 5% nonfat dry milk in Tris-buffered saline-Tween (TBS-T, 0.1% Tween-20) for 1 h at room temperature, then incubated overnight at 4 °C in primary antibody (anti-CD63, EXOAB-CD63A-1; System Biosciences, Palo Alto, CA and anti-Apolipoprotein A1 (ApoA1, 701239; Thermo Fisher) at a 1:1000 dilution in 5% nonfat dry milk in TBS-T. The membranes were then washed before incubation in goat anti-rabbit secondary antibodies (EXOAB-CD63A-1; System Biosciences) (1:10,000 dilution) for 1 h at room temperature. Blots were developed with enhanced chemiluminescence (Clarity Western ECL Substrate, Bio-Rad), imaged, and quantified with ImageJ (National Institutes of Health).
Ismaeel A., Van Pelt D.W., Hettinger Z.R., Fu X., Richards C.I., Butterfield T.A., Petrocelli J.J., Vechetti I.J., Confides A.L., Drummond M.J, & Dupont-Versteegden E.E. (2023). Extracellular vesicle distribution and localization in skeletal muscle at rest and following disuse atrophy. Skeletal Muscle, 13, 6.
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Publication 2023
Anti-Antibodies APOA1 protein, human Biological Assay Buffers Chemiluminescence Gels Glycine Goat Immunoglobulins Laemmli buffer Methanol Milk, Cow's Nitrocellulose Peptide Hydrolases Phosphoric Monoester Hydrolases ponceau S Proteins Rabbits Radioimmunoprecipitation Assay Saline Solution SDS-PAGE Stains Technique, Dilution Tissue, Membrane Tween 20 Tweens
2
Western Blot Analysis of Apoptosis and MAPK Signaling
Total proteins from BC cells were extracted with radioimmunoprecipitation assay (RIPA) lysis buffer containing phenylmethyl sulfonylfluoride (PMSF), followed by SDS-PAGE, and transferred to polyvinylidene difluoride (PVDF) membranes (Millipore, Billerica, MA, USA). After that, the PVDF membranes were blocked with 5% skimmed milk and incubated with the corresponding primary antibody: Bax (1:1000, Abcam, Cambridge, UK), Bcl-2 (1:1000, Abcam), MAPK6 (1:1000, Abcam), p-MAPK6 (1:1000, Abcam), p38 (1:1000, Cell Signaling Technology, Danvers, MA, USA), p-p38 (1:1000, Cell Signaling Technology), ERK (1:1000, Cell Signaling Technology), p-ERK (1:1000, Cell Signaling Technology), and β-actin (1:5000, Cell Signaling Technology). Next, the membranes were incubated at 4℃ for 14 h, and subsequently, the membranes were incubated with the corresponding secondary antibody (1:6000, Cell Signaling Technology) for 1.5 h at room temperature. Lastly, the band signal was visualized using an enhanced chemiluminescence (ECL) detection system (Millipore).
Wang B., Chen H., Deng Y., Chen H., Xing L., Guo Y., Wang M, & Chen J. (2023). CircDNAJC11 interacts with TAF15 to promote breast cancer progression via enhancing MAPK6 expression and activating the MAPK signaling pathway. Journal of Translational Medicine, 21, 186.
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Publication 2023
Actins BCL2 protein, human Buffers Cells Chemiluminescence Immunoglobulins Milk, Cow's Mitogen-Activated Protein Kinase 3 polyvinylidene fluoride Proteins Radioimmunoprecipitation Assay SDS-PAGE sulfuryl fluoride Tissue, Membrane
3
Protein Expression Analysis by Western Blot
Total protein was isolated from RIPA lysate and quantified using the BCA method. Next, 30 μg of total protein was separated by 8% sodium dodecyl sulfate polyacrylamide gel electrophoresis and transferred onto a polyvinylidene fluoride membrane. After blocking with 5% skim milk at 37 °C for 2 h, the membrane was incubated with primary antibodies against LDHA (1:1 000), CD47 (1:1 000), PDIA3 (1:1 000), SLC16A1 (1: 200), and the internal reference β-actin (1:1 000) overnight at 4 °C. The next day, the membrane was incubated with secondary antibodies at 37 °C for 1 h. The bands were detected by adding the chemiluminescence substrate, and proteins were quantified by densitometry using Image Lab 5.2 software, with β-actin as the internal reference. The experiment was performed three times.
Zhang H., Wang X., Li Y., Bai Y., Li Q., Wang S., Wei Y., Li J., Wen S, & Zhao W. (2023). The hsa_circ_0000276-ceRNA regulatory network and immune infiltration in cervical cancer. BMC Cancer, 23, 222.
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Publication 2023
Actins Antibodies CD47 protein, human Chemiluminescence Densitometry LDH 5 Milk, Cow's PDIA3 protein, human polyvinylidene fluoride Proteins Radioimmunoprecipitation Assay SDS-PAGE Tissue, Membrane
4
Proteasome Inhibitor Effects on Protein Regulation
HMC-1 and ROSAKIT D816V cells maintained in control medium or after 24 h-incubation with 10 nM bortezomib, 5 nM carfilzomib, 50 nM ixazomib and 5 µM SP141 were lysed to extract total cellular proteins. WB, co-immunoprecipitation and immunoblotting were performed as described in the Supplementary methods. The following primary antibodies were used for Co-IP/immunoblotting and WB: anti-SETD2 (goat polyclonal antibody, cat. PAB7385, Abnova), anti-H3K36Me3 (rabbit monoclonal antibody, clone D5A7 cat. 4909) anti-p53 (rabbit monoclonal antibody, clone 7F5 cat.2527), anti-Mdm2 (rabbit monoclonal antibody, cloneD1V2Z, cat. 86,934), anti-ubiquitin (rabbit monoclonal antibody, clone E6K4Y, cat. 20,326), anti-Aurora kinase A (rabbit monoclonal antibody, clone D3V7T, cod. 91,590, anti-phospho-Aurora kinase A(T288) (rabbit monoclonal antibody, clone C39D8, cod. 3079), anti-Plk1 (rabbit monoclonal antibody, clone208G4, cod. 4513), anti phospho-Plk1(T210) (rabbit polyclonal antibody, cat. 5472), anti-phospho-Ser/Thr (rabbit polyclonal antibody, cat. 9631)(all from Cell Signaling Technology). Beta-actin (mouse monoclonal antibody, clone AC-15, cod. SC-69879 Santa Cruz biotechnology) or beta-tubulin (rabbit monoclonal antibody, clone 3F7, cod. 2128 Cell Signaling Technology) were used as loading control. Immunoreactive proteins were visualized by probing with horseradish peroxidase-conjugated secondary antibodies and then by enhanced chemiluminescence (ECL, Thermo Fisher Scientific). Signal intensities in single blots obtained from three individual experiments were quantified with the ImageJ software, which attributes a numerical value to signals of chemiluminescent substrates, thereby allowing a comparative analysis of protein levels across different samples.
Mancini M., Monaldi C., De Santis S., Papayannidis C., Rondoni M., Sartor C., Bruno S., Pagano L., Criscuolo M., Zanotti R., Bonifacio M., Tosi P., Arock M., Valent P., Cavo M, & Soverini S. (2023). SETD2 non genomic loss of function in advanced systemic mastocytosis is mediated by an Aurora kinase A/MDM2 axis and can be therapeutically targeted. Biomarker Research, 11, 29.
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Publication 2023
Antibodies Aurora Kinase A beta-Actin beta-Tubulin Bortezomib carfilzomib Cells Chemiluminescence Clone Cells Co-Immunoprecipitation Goat Horseradish Peroxidase hSet2 protein, human Immunoglobulins ixazomib MDM2 protein, human Monoclonal Antibodies Mus PLK1 protein, human Proteins Rabbits Staphylococcal Protein A Ubiquitin
5
Pancreatic Cancer Cell Culture Protocols
Pancreatic cancer cell lines (AsPC-1 and BxPC-3) were cultured in RPMI-1640 (Corning, NY, USA) with 10% fetal bovine serum (FBS) and 1% penicillin–streptomycin. Two additional pancreatic cancer cell lines (PANC-1, MIA Paca-2) were cultured in DMEM (Dulbecco’ modified eagle medium) (Gibco, Grand Island, NY, USA) supplemented with 10% FBS and 1% penicillin–streptomycin. Human pancreatic ductal epithelium (hTERT-HPNE) cells were cultured in Medium D with mixtures of M3 and DMEM medium containing one volume of medium M3TM Base F culture media (InCell Corp., San Antonio, TX, USA), three volumes of glucose-free DMEM, 5% FBS, 5.5 mM glucose, 10 ng/ml EGF, and 50 µg/ml gentamycin [26 (link)]. All these cells were cultured at 37 °C in a humidified atmosphere containing 5% CO2. RNA was extracted from tissues using the TRIzol reagent (Invitrogen, Carlsbad, CA, USA) and was reverse-transcribed into cDNA using the PrimeScript RT Master Mix (Takara, Otsu, Shiga, Japan). RT-qPCR analyses were quantified with PowerUp™ SYBR® Green Master Mix (Applied Biosystems, Austin, TX, USA), and expression levels were normalized to GAPDH levels. Proteins were extracted in RIPA buffer supplemented with a complete, EDTA-free protease and phosphatase inhibitor single-use cocktail (Thermo Scientific). Proteins were separated by SDS-PAGE and blotted onto a PVDF membrane. Anti-TSC22D2 (1:1000 dilution, #25,418–1-AP, Proteintech) was used as primary antibodies for immunoblotting. Reacted antibodies were detected using an enhanced chemiluminescence detection system.
Liu Q., Li R., Wu H, & Liang Z. (2023). A novel cuproptosis-related gene model predicts outcomes and treatment responses in pancreatic adenocarcinoma. BMC Cancer, 23, 226.
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Publication 2023
Antibodies Atmosphere austin Buffers Cell Lines Cells Chemiluminescence Culture Media DNA, Complementary Eagle Edetic Acid Epithelium Fetal Bovine Serum GAPDH protein, human Gentamicin Glucose Homo sapiens Pancreatic Cancer Pancreatic Duct Penicillins Peptide Hydrolases Phosphoric Monoester Hydrolases polyvinylidene fluoride Proteins Radioimmunoprecipitation Assay SDS-PAGE Streptomycin SYBR Green I Technique, Dilution Tissue, Membrane Tissues trizol

Top products related to «Chemiluminescence»

1
Pvdf membrane by Merck Group
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PVDF membranes are a type of laboratory equipment used for a variety of applications. They are made from polyvinylidene fluoride (PVDF), a durable and chemically resistant material. PVDF membranes are known for their high mechanical strength, thermal stability, and resistance to a wide range of chemicals. They are commonly used in various filtration, separation, and analysis processes in scientific and research settings.
2
Ripa lysis buffer by Beyotime
Sourced in China, United States, Switzerland, Germany, Japan, United Kingdom
RIPA lysis buffer is a detergent-based buffer solution designed for the extraction and solubilization of proteins from cells and tissues. It contains a mixture of ionic and non-ionic detergents that disrupt cell membranes and solubilize cellular proteins. The buffer also includes additional components that help to maintain the stability and activity of the extracted proteins.
3
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Polyvinylidene difluoride (PVDF) membranes are a type of lab equipment used for various applications. PVDF membranes are known for their chemical resistance, thermal stability, and mechanical strength. They are commonly used in filtration, separation, and transfer processes in laboratory settings.
4
Bca protein assay kit by Beyotime
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The BCA protein assay kit is a colorimetric-based method for the quantitative determination of total protein concentration in a sample. It uses bicinchoninic acid (BCA) to detect and quantify the presence of protein.
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Polyvinylidene fluoride membrane by Merck Group
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Polyvinylidene fluoride (PVDF) membranes are a type of lab equipment used for a variety of filtration and separation applications. They are made from a thermoplastic fluoropolymer material and offer high chemical and thermal resistance. PVDF membranes are commonly used in processes such as microfiltration, ultrafiltration, and sample preparation.
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Bca protein assay kit by Thermo Fisher Scientific
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The BCA Protein Assay Kit is a colorimetric detection and quantification method for total protein concentration. It utilizes bicinchoninic acid (BCA) for the colorimetric detection and quantification of total protein. The assay is based on the reduction of Cu2+ to Cu1+ by protein in an alkaline medium, with the chelation of BCA with the Cu1+ ion resulting in a purple-colored reaction product that exhibits a strong absorbance at 562 nm, which is proportional to the amount of protein present in the sample.
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Pvdf membrane by Bio-Rad
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PVDF membranes are a type of laboratory equipment used for protein transfer and detection in Western blot analysis. They provide a stable and durable surface for the immobilization of proteins, enabling effective identification and quantification of target proteins in complex biological samples.
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Nitrocellulose membrane by Bio-Rad
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Nitrocellulose membranes are a type of laboratory equipment designed for use in protein detection and analysis techniques. These membranes serve as a support matrix for the immobilization of proteins, enabling various downstream applications such as Western blotting, dot blotting, and immunodetection.
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Protease inhibitor cocktail by Roche
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Protease inhibitor cocktail is a laboratory reagent used to inhibit the activity of proteases, which are enzymes that break down proteins. It is commonly used in protein extraction and purification procedures to prevent protein degradation.
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Protease inhibitor cocktail by Merck Group
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The Protease Inhibitor Cocktail is a laboratory product designed to inhibit the activity of proteases, which are enzymes that can degrade proteins. It is a combination of various chemical compounds that work to prevent the breakdown of proteins in biological samples, allowing for more accurate analysis and preservation of protein integrity.

More about "Chemiluminescence"

Chemiluminescence is a fascinating phenomenon where light is emitted from a chemical reaction.
This process occurs when a molecule in an excited state relaxes to a lower energy level, releasing a photon.
This versatile technique has a wide range of applications, from analytical chemistry and biomedical research to environmental monitoring.
Chemiluminescence is often used as a detection method in various assays and imaging techniques, providing sensitive and quantitative measurements.
It's a valuable tool for researchers, offering insights into biological processes, chemical reactions, and the presence of specific analytes.
Understanding the principles and applications of chemiluminescence is crucial for optimizing experimental workflows and obtaining reproducible, data-driven insights.
Chemiluminescence can be used in conjunction with techniques like PVDF membranes, RIPA lysis buffer, and BCA protein assay kits to unlock a deeper understanding of biological systems and chemical processes.
Polyvinylidene fluoride (PVDF) membranes and nitrocellulose membranes are commonly used in conjunction with chemiluminescence-based assays, such as Western blotting, to detect and quantify specific proteins.
Protease inhibitor cocktails can also be used to preserve the integrity of these proteins during sample preparation.
Whether you're studying signaling pathways, environmental pollutants, or conducting medical diagnostics, the insights gained from chemiluminescence can be transformative.
Explore the latest advancements and optimize your research workflow with the power of this versatile, light-emitting technique.