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Barbital

Barbital is a sedative-hypnotic drug that was commonly used as a sleeping aid in the early 20th century.
It belongs to the class of barbiturates and has a depressant effect on the central nervous system.
Researchers can leverage PubCompare.ai to optimize their Barbital research by locating and comparing experimental protocols from literature, pre-prints, and patents.
The AI-driven comparisons help identify the most accurate and reproducible proceedures, enhancing research outcomes.
Experince the power of PubCompare.ai today to advance your Barbital studies.

Most cited protocols related to «Barbital»

1
Analyzing fH-Dependent Complement Regulation
NHS was sequentially depleted of fB and fH (NHSΔBΔH) by flowing over immobilised anti-Bb (JC1 mAb; in house) and immobilised anti-fH (35H9; in house) affinity columns in complement fixation diluent (CFD; Oxoid), undiluted depleted serum was pooled and used in haemolysis assays as described below. Antibody-coated sheep erythrocytes (EA) were prepared by incubating sheep E (2% v/v) with Amboceptor (1/1000 dilution; Behring Diagnostics) in complement fixation diluent (CFD; Oxoid) for 30 minutes at 37°C, EA were washed and resuspended at 2% (v/v) in CFD. To deposit C3b on the E surface (E-C3b), equal volumes of EA and NHSΔBΔH (8% v/v) were incubated at 37°C for 10 minutes, the C5 inhibitor (OmCI; 6μg/ml; (28 (link)) was added to block the terminal pathway).
To test fH dependent decay accelerating activity, washed E-C3b cells were resuspended to 2% (v/v) in AP buffer (5 mM sodium barbitone pH 7.4, 150 mM NaCl, 7 mM MgCl2, 10 mM EGTA) and AP convertase was formed on the cell surface by incubating with fB 42μg/ml (0.46μM) and fD (0.4μg/ml) at 37°C for 15 minutes. 1/25 volume of PBS/0.25M EDTA was added to prevent further enzyme formation and cells (50μl) were mixed and incubated with 50μl of fH (serial dilution from 15.4μg/ml (99nM)) in PBS/10mM EDTA for 12 minutes. Lysis was developed by adding 50μl NHSΔBΔH (4%, v/v) in PBS/EDTA and incubating at 37°C for 20 minutes. To calculate lysis, cells were pelleted by centrifugation, and hemoglobin release was measured by absorbance at 415 nm. Control incubations included 0%lysis (buffer only) and 100%lysis (0.1% Nonidet-P40). Percentage lysis 100*(A415 test sample-A415 0% control)/(A415 100% control-A415 0% control).
To test fH cofactor activity, washed EA-C3b cells were resuspended to 2% in AP buffer and incubated with an equal volume of different concentrations of fH as indicated and constant fI (2.5μg/mL) for 7 minutes at 22°C. After three washes in AP buffer, 50μl cells (2%) were mixed with 50μl of 70μg/ml fB (0.75μM; fB32R or fB32Q) and fD (0.4μg/ml) and incubated for 10 minutes at 22°C to form convertase on residual C3b (EA-C3bBb). Lysis was developed by adding 50μl NHSΔBΔH (4%, v/v) in PBS/EDTA and incubating at 37°C for 20 minutes. Percentage lysis was calculated as described above. To assess the effect on lysis by combining different polymorphic variants of fB and fH, the above two assays were combined and modified as follows. EA-C3b cells were incubated with 80ng/ml (0.5nM) fH-Ile62 or fH-Val62 variant and 2.5μg/ml fI for 7 minutes at 22°C. Washed cells were incubated as described above with different concentrations of fBArg32 or fBGln32, fD and properdin (1μg/ml) and lysis was developed using NHSΔBΔH.
Tortajada A., Montes T., Martinez-Barricarte R., Morgan B.P., Harris C.L, & de Córdoba S.R. (2009). The disease-protective complement factor H allotypic variant Ile62 shows increased binding affinity for C3b and enhanced cofactor activity. Human molecular genetics, 18(18), 3452-3461.
Publication 2009
Barbital Biological Assay Buffers Cardiac Arrest Cells Centrifugation Diagnosis Domestic Sheep Edetic Acid Egtazic Acid Enzymes Erythrocytes Hemoglobin Hemolysis Immunoglobulins Magnesium Chloride Neutrophil nonidet Properdin Serum Sodium Sodium Chloride Technique, Dilution
2
Non-denaturing PAGE for Hydrogenase Activity
Non-denaturing PAGE was performed using a discontinuous system with 7.5% (w/v) polyacrylamide separating gels in 250 mM Tris/HCl buffer, pH 8.5 including 0.1% (w/v) Triton X-100 [18 (link)]. As running buffer 0.1 M Tris/0.1 M glycine buffer was used. After reaching mid-exponential phase of growth cells were harvested from cultures by centrifugation at 10,000 x g for 15 min at 4 °C and after washing once in the same volume of 50 mM MOPS buffer pH 7.0, cells were resuspended in a tenth of their volume of 50 mM MOPS buffer pH 7.0, broken by sonification and cell debris and unbroken cells removed as described [20 (link)]. Samples of crude extract were resuspended at a protein concentration of 10 mg ml-1 in 50 mM MOPS buffer pH 7.0 and incubated with a final concentration of 5% (w/v) Triton X-100 prior to application of the solubilized sample (usually 25 μg of protein) to the gels. Alternatively, for neutral pH analyses the barbitone gel system was used. This system uses final concentrations of 34 mM Tris-phosphate buffered stacking gel, pH 5.5 and 62.5 mM Tris-HCl resolving gel pH 7.5. The running buffer consists of 82.5 mM Tris and 26.8 mM diethylbarbituric acid, pH 7.0. Hydrogenase activity-staining was done as described in [18 (link)] with 0.5 mM benzyl viologen (BV) and 1 mM 2,3,5,-triphenyltetrazolium chloride (TTC) and continuous flushing with highly pure hydrogen gas until the activity bands appeared except that the buffer used was 50 mM MOPS pH 7.0. Alternatively, staining was done in hydrogen-flushed buffer using 0.3 mM phenazine methosulfate (PMS) as mediator and 0.2 mM nitroblue tetrazolium (NBT) as electron acceptor [52 (link)]. When formate was added as substrate to the buffer, a final concentration of 50 mM was used. When used in native-PAGE molecular mass standard proteins from a gel filtration markers kit 29-700 kDa (Sigma) were mixed in equal amounts and 6 μg of each were loaded on the gel.
Pinske C., Jaroschinsky M., Sargent F, & Sawers G. (2012). Zymographic differentiation of [NiFe]-Hydrogenases 1, 2 and 3 of Escherichia coli K-12. BMC Microbiology, 12, 134.
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Publication 2012
Acids ATP8A2 protein, human Barbital Benzyl Viologen Buffers Cells Centrifugation Complex Extracts Formates Gel Chromatography Glycine Hydrogen Hydrogenase Methylphenazonium Methosulfate morpholinopropane sulfonic acid Native Polyacrylamide Gel Electrophoresis Nitroblue Tetrazolium Oxidants Phosphates polyacrylamide gels Proteins Proto-Oncogene Mas triphenyltetrazolium chloride Triton X-100 Tromethamine
3
Evaluating Complement Activation in Serum
Microtiter plates were coated with 5 µg/ml acBSA in PBS-buffer overnight at 4°C. Plates were blocked for 1 h with barbital-T and subsequently washed thrice in barbital-T. Serum diluted in barbital-T was added to the wells and incubated for 30 min at 37°C (45 min at 37°C for the detection of TCC). In order to evaluate whether the binding was dependent on calcium 10 mM EDTA or 10 mM EGTA with 5 mM Mg2+ was added to the serum. Plates were washed in barbital-T and subsequently incubated with anti-C4c (0.13 µg/ml), anti-C4c-biotin (2 µg/ml), anti-C3c (0.32 µg/ml) or anti-C5b-C9 (TCC) (1 µg/ml) for 2 h, shaking at room temperature. Plates were washed in barbital-T and incubated with HRP-conjugated streptavidin, anti-rabbit or anti-mouse IgG antibodies (all diluted 1:2000 in barbital-T) for 1 h at room temperature, shaking. Plates were washed and developed as described above.
Hein E., Honoré C., Skjoedt M.O., Munthe-Fog L., Hummelshøj T, & Garred P. (2010). Functional Analysis of Ficolin-3 Mediated Complement Activation. PLoS ONE, 5(11), e15443.
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Publication 2010
anti-IgG Antibodies Barbital Biotin Buffers Edetate, Calcium Disodium Egtazic Acid Mus Rabbits Serum Streptavidin
4
Quantifying Residual Lectin Pathway Activity
A LP specific C3 deposition ELISA was performed to measure residual LP functional activity in patient plasma (38 (link)). A Maxisorp ELISA plate (NUNC™) was coated with 10 μg/mL mannan to test LP activation by MBL (38 (link), 39 (link)), or 25 μg/mL acetylated bovine serum albumin (acBSA) to test LP activation by ficolins (21 (link), 40 (link)) diluted in coating buffer (15 mM Na2CO3, 35 mM NaHCO3, pH 9.6) and incubated overnight at 4°C. Residual protein binding sites were saturated by incubating the plate with 1% BSA-TBS blocking buffer (0.1% (w/v) BSA in 10 mM Tris–CL, 140 mM NaCl, 1.5 mM NaN3, pH 7.4) overnight at 4°C. The plate was then washed with washing buffer (TBS with 0.05% Tween 20 and 5 mM CaCl2). EDTA-plasma samples were thawed on ice and suspended in barbital buffered saline (BBS; 4 mM barbital, 145 mM NaCl, 2 mM CaCl2, 1 mM MgCl2, pH 7.4), to a final plasma concentration of 6%. Wells receiving only BBS buffer were used as negative controls. Plasma solutions were incubated on the coated plate at 37°C for 1 h 30 min (40 μL/well). The plate was washed and incubated for 1 h 30 min at RT with a polyclonal anti-human C3c antibody (Dako, A0062) diluted 1:5,000 in washing buffer. After washing, the plate was incubated with an alkaline-phosphatase labeled goat anti-rabbit IgG antibody (Sigma A-3812) diluted 1:5,000 in washing buffer for 1 h 30 min at RT. Following washing, the assay was developed by adding 100 μL substrate solution (Sigma Fast p-Nitrophenyl Phosphate tablets, Sigma). The absorption at OD405 nm was then measured using the Infinite M200 spectrofluorimeter managed by Magellan software (Tecan, CH).
Fumagalli S., Perego C., Zangari R., De Blasio D., Oggioni M., De Nigris F., Snider F., Garred P., Ferrante A.M, & De Simoni M.G. (2017). Lectin Pathway of Complement Activation Is Associated with Vulnerability of Atherosclerotic Plaques. Frontiers in Immunology, 8, 288.
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Publication 2017
Alkaline Phosphatase anti-IgG Antibodies, Anti-Idiotypic Barbital Bicarbonate, Sodium Biological Assay Buffers Cardiac Arrest Edetic Acid Enzyme-Linked Immunosorbent Assay ficolin Goat Homo sapiens Immunoglobulins M-200 Magnesium Chloride Mannans nitrophenylphosphate Patients Plasma Rabbits Saline Solution Serum Albumin, Bovine Sodium Azide Sodium Chloride Tromethamine Tween 20
5
Muscle Fiber Typing with Histochemistry
Routine H&E, NADH-TR, and ATPase staining were performed as described previously [30] (link). Briefly, the various fiber types were determined by NADH-TR staining and differential ATPase staining at different preincubation pHs. ATPase at pH 10.8 distinguishes type I (light staining) from type II (dark staining) fibers; pH 4.5 distinguishes type I (dark staining) from IIA (light staining) and IIB (medium staining) fibers; and pH 4.2 distinguishes IID/X (medium staining) from IIA or IIB (light staining) fibers. The three preincubation reagents were (1) 20 mM sodium barbital, 36 mM CaCI2, pH 10.8, (2) 50 mM sodium acetate, 30 mM sodium barbital brought to pH 4.5 with HCI, and (3) the same as (2) but adjusted to pH 4.2. The sections were preincubated for 15 min at pH 10.8 and 5 min at the acid pHs. After preincubation, the sections were incubated for 45 min in 20 mM sodium barbital, pH 9.5, containing 9 mM CaCl2 and 2.7 mM ATP; rinsed in 2 changes of 1% CaCl2 (1 min each); immersed for 2 min in 2% CaCl2; and rinsed with several changes of tap water. After staining with 1% (NH4)2S, the sections were washed with several changes of tap water, dehydrated with ethanol, cleared in xylene, and mounted in balsam.
Suga T., Kimura E., Morioka Y., Ikawa M., Li S., Uchino K., Uchida Y., Yamashita S., Maeda Y., Chamberlain J.S, & Uchino M. (2011). Muscle Fiber Type-Predominant Promoter Activity in Lentiviral-Mediated Transgenic Mouse. PLoS ONE, 6(3), e16908.
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Publication 2011
Acids Adenosine Triphosphatases Barbital Ethanol Fibrosis Light NADH Sodium Sodium Acetate Xylene

Most recents protocols related to «Barbital»

1
In Vitro SGSH-Fc Fusion Protein Activity Assay
Not available on PMC !

Example 8

This example provides an alternative in vitro activity assay for SGSH-Fc fusion proteins. The assay is adapted from Karpova et al., J. Inherit. Metab. Dis., 19:278-285 (1996).

The standard reaction mixtures consisted of 10-15 μg of protein and 20 μL MU-α-GlcNS (5 or 10 mmol/L, respectively) in Michaelis' barbital sodium acetate buffer, pH 6.5 (29 mmol/L sodium barbital, 29 mmol/L sodium acetate, 0.68% (w/v) NaCl, 0.02% (w/v) sodium azide; adjusted to pH 6.5 with HCl) and the reaction mixtures were incubated for 17 h at 37° C. MU-α-GcNS is available from Moscerdam Substrates. After the first incubation, 6 μl twice-concentrated McIlvain's phosphate/citrate buffer, pH 6.7, containing 0.02% sodium azide and 10 μl (0.1 U) yeast a-glucosidase (Sigma) in water were added and a second incubation of 24 h at 37° C. was carried out. Long incubations at 37° C. (17-24 h) were carried out in 96-well plates which were sealed airtight with broad sticky tape, limiting evaporation to <15%. Next, 200 μL 0.5 mol/L Na2CO3/NaHCO3, pH 10.7, was added, and the fluorescence of the released 4-methylumbelliferone (MU) was measured on a Fluoroskan (Titertek) fluorimeter. Protein was determined as described previously (van Diggelen et al., Clin. Chim. Acta., 187:131-139 (1990)).

US11866742B2. Fusion proteins comprising enzyme replacement therapy enzymes (2024-01-09). Denali Therapeutics Inc. [US]. Inventors: Anastasia Henry [US], Mihalis S. Kariolis [US], Cathal S. Mahon [US], Adam P. Silverman [US], Ankita Srivastava [US], Julie Ullman [US].
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Patent 2024
Barbital Bicarbonate, Sodium Biological Assay Buffers Citrate Fluorescence Glucosidase Hymecromone Phosphates Proteins Sodium Sodium Acetate Sodium Azide Sodium Chloride Yeast, Dried
2
Optimal pH, Temperature, and Thermostability of Xylanase
The optimal pH of xylanase was measured at 37 °C using 50.00 mM buffer with pH values ranging from 2.0 to 12.0, including Glycine-HCl (Gly-HCl) buffer (pH 2.0–3.0), citrate buffer (pH 3.0–6.5), phosphate buffer (pH 6.5–8.0), barbital sodium buffer (pH 8.0–9.5), Glycine-NaOH (Gly-NaOH) buffer (pH 9.5–10.5), 3-(cyclohexylamino)-1-propanesulfonic acid (CAPS) buffer (pH 10.5–11.0), and NaH2PO4-NaOH buffer (pH 11.0–12.0). The pH stability of xylanase was determined by incubating the enzyme in buffers with pH ranging from 2.0 to 12.0 for 30 min at 37 °C, and then measuring the residual enzyme activity. The optimal temperature of xylanase was detected for the enzyme activity in 50 mM citrate buffer at temperatures ranging from 30 °C to 80 °C. The thermostability of xylanase was determined by incubating the enzyme at temperatures ranging from 30 °C to 70 °C for 30 min in 50.00 mM citrate buffer.
The protein concentration of the pure enzyme solution was diluted to 0.50 mg/mL using citrate buffer at pH 6.0, and the diluted enzyme solutions of the mutant enzyme and XynA were kept at 60 °C for 0, 15, 30, 60, 90, 120 and 180 min, respectively, and cooled rapidly in an ice water bath. The activity of untreated xylanase was defined as 100%, and the residual enzyme activity was calculated using the formula y = Ae−kt (A is the initial enzyme activity, t is time, k is the decay constant). The half-life t1/2 is equal to ln2/k. The half-lives of mutants and XynA at 60 °C were calculated separately according to the formula [49 (link)]. The Protein Thermal Shift ™ dye kit was used to determine the thermal denaturation temperature of mutants and XynA [50 (link)]. Quantitative real-time PCR was performed using the CFX Touch 96-well system (Bio-Rad, California, CA, USA). Samples were heated on a 0.05 °C/s gradient from 4 to 95 °C and protein unfolding at each temperature was monitored by measurement of fluorescence at 580/623 nm (excitation/emission) [51 (link)].
Substrate specificity of the enzymes was investigated using the standard assay procedure with one of the following substrates (1%, w/v), beechwood xylan, birchwood xylan, or oat-spelt xylan. The liberated reducing sugars’ concentrations were determined by the DNS method, as described in Section 2.4. The kinetic parameters of xylanase were measured with different concentrations (2.50–30.00 mg/mL) of beechwood xylan in optimal reaction conditions. The values of Km and Vmax of the enzyme were calculated according to the Michaelis-Menten equation using GraphPad Prism software [40 (link),52 (link)].
Zhu W., Qin L., Xu Y., Lu H., Wu Q., Li W., Zhang C, & Li X. (2023). Three Molecular Modification Strategies to Improve the Thermostability of Xylanase XynA from Streptomyces rameus L2001. Foods, 12(4), 879.
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Publication 2023
Acids Adjustment Disorders Barbital Bath Biological Assay Buffers Citrate enzyme activity Enzymes Fluorescence Glycine Ice Kinetics Phosphates prisma Proteins Real-Time Polymerase Chain Reaction Sodium Sugars Touch Triticum spelta Xylans
3
ELISA Assays for Complement Pathways
ELISAs were performed as described by Dekkers et al.75 For the alternative pathway ELISA, Nunc Polysorp flat‐bottom plates (Thermo Scientific, Rockland, IL, USA) were coated overnight with 40 μg mL−1 lipopolysaccharide from Salmonella typhosa (LPS, Sigma‐Aldrich, St. Louis, MI, USA) in phosphate‐buffered saline (PBS) at room temperature (RT). Plates were washed and incubated for 1 h at 37°C with 20% (v/v) NHS or FB‐or FD‐depleted serum, with or without purified FB (162.5 μg mL−1) or FD (1.05 μg mL−1) supplementation in Veronal Buffer (1.8 mm sodium barbital and 3.1 mm barbituric acid, pH 7.3–7.4; VB) with 0.1% (w/v) Tween‐20, 0.3% (w/v) BSA, 5 mm MgCl2 and 10 mm EDTA. For the CP ELISA, Nunc Maxisorp flat‐bottom plates (ThermoFisher Scientific, Whaltam, MA, USA) were coated overnight with 5 or 0.5 μg mL−1 agglutinated human IgG (AHG, Sanquin Reagents) in PBS at RT. Plates were washed and incubated for 1 h at RT with 25% (v/v) NHS with or without anti‐FB (202 μg mL−1), anti‐FD (1.3 μg mL−1) or anti‐C1q (31.75 μg mL−1) in VB with 0.1% (w/v) Tween‐20, 0.3% (w/v) BSA, 1 mm CaCl2 and 0.5 mm MgCl2. ELISA was performed as described above. Biotinylated anti‐C3.19 was used as conjugate and ELISA was developed as described by Dekkers et al.,75 with the exception of the usage of streptavidin‐HRP for the classical pathway ELISA.
de Boer E.C., Thielen A.J., Langereis J.D., Kamp A., Brouwer M.C., Oskam N., Jongsma M.L., Baral A.J., Spaapen R.M., Zeerleder S., Vidarsson G., Rispens T., Wouters D., Pouw R.B, & Jongerius I. (2023). The contribution of the alternative pathway in complement activation on cell surfaces depends on the strength of classical pathway initiation. Clinical & Translational Immunology, 12(1), e1436.
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Publication 2023
Barbital barbituric acid Edetic Acid Enzyme-Linked Immunosorbent Assay Homo sapiens Magnesium Chloride Phosphates Saline Solution Salmonella typhi Serum Sodium Streptavidin Tween 20
4
Histopathological Effects of B. caeruleus Venom

Protocol full text hidden due to copyright restrictions

Open the protocol to access the free full text link

Publication 2023
Albinism Autopsy Barbital Brain Eosin Ethanol Formaldehyde Heart Intestines Kidney Light Microscopy Liver Lung Mice, House Microtomy Mouse, Swiss Tissues Venoms
5
Humane Euthanasia of Experimental Animals
This study was approved by the Experimental Animal Management and Use Committee of the Hubei Provincial Center for Disease Control and Prevention (project approval number 202120134).
Euthanasia was performed by cervical dislocation after anesthesia via intraperitoneal injection of 1% barbital sodium.
Xu L., Zhan Z.C., Du S., Wang S., Zhang Q., Wang C., Yang W., Deng X., Zhan Z., Li Y., Zhou Y, & Chen X. (2023). Isolation, functional evaluation, and fermentation process optimization of probiotic Bacillus coagulans. PLOS ONE, 18(11), e0286944.
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Publication 2023
Anesthesia Animals, Laboratory Barbital Euthanasia Injections, Intraperitoneal Joint Dislocations Neck Sodium

Top products related to «Barbital»

1
Barbital buffer by Merck Group
Sourced in United States, Sao Tome and Principe, Italy
Barbital buffer is a laboratory buffer solution used to maintain a specific pH level for various analytical and experimental procedures. It is commonly used in biochemical and immunological applications. The buffer solution contains sodium barbital and barbital as the primary components, which work to stabilize the pH within the desired range.
2
Barbital sodium by Merck Group
Sourced in United States
Barbital sodium is a laboratory reagent used in the analysis and testing of various chemical and biological samples. It functions as a buffer substance, maintaining a stable pH environment during the analytical process. This product is commonly utilized in various scientific applications, including clinical diagnostics and pharmaceutical research and development.
3
Hydragel 15 30 lipoprotein e agarose gels by Sebia
The Sebia Hydragel 15/30 lipoprotein (e) agarose gels are laboratory equipment designed for the electrophoretic separation and analysis of lipoproteins in human serum or plasma samples. The gels provide a standardized platform for the separation and visualization of different lipoprotein fractions, including low-density lipoproteins (LDL), high-density lipoproteins (HDL), and very low-density lipoproteins (VLDL).
4
Titan gel electrophoresis chamber by Helena Laboratories
The Titan gel electrophoresis chamber is a laboratory equipment designed for the separation and analysis of macromolecules, such as proteins and nucleic acids, using the technique of gel electrophoresis. It provides a controlled environment for the migration of charged molecules through a gel matrix under the influence of an electric field.
5
Yeast α glucosidase by Merck Group
Sourced in United States, Germany
Yeast α-glucosidase is an enzyme that catalyzes the hydrolysis of terminal, non-reducing α-D-glucose residues in α-D-glucosides. It is commonly used in laboratory settings for various biochemical and enzymatic analyses.
6
S1389 by Merck Group
Sourced in United States
S1389 is a laboratory equipment product manufactured by Merck Group. It is a precision instrument designed for scientific research and analysis. The core function of S1389 is to perform accurate measurements and data collection, without further extrapolation on its intended use.
7
Pentobarbital sodium by Merck Group
Sourced in United States, Germany, China, Sao Tome and Principe, United Kingdom, Japan, Italy, Canada, Hungary, Macao
Pentobarbital sodium is a laboratory chemical compound. It is a barbiturate drug that acts as a central nervous system depressant. Pentobarbital sodium is commonly used in research and scientific applications.
8
Acetonitrile by Thermo Fisher Scientific
Sourced in United States, United Kingdom, China, Belgium, Germany, Canada, Portugal, France, Australia, Spain, Switzerland, India, Ireland, New Zealand, Sweden, Italy, Japan, Mexico, Denmark
Acetonitrile is a highly polar, aprotic organic solvent commonly used in analytical and synthetic chemistry applications. It has a low boiling point and is miscible with water and many organic solvents. Acetonitrile is a versatile solvent that can be utilized in various laboratory procedures, such as HPLC, GC, and extraction processes.
9
Sudan black by Merck Group
Sourced in United States, Germany
Sudan Black is a lipophilic dye that is commonly used for staining lipids and lipid-containing structures in biological samples. It has the ability to bind to and stain neutral lipids, phospholipids, and glycolipids, making it a useful tool for visualizing these components in microscopy and histological applications.
10
Infinite m200 spectrofluorimeter by Tecan
The Infinite M200 spectrofluorimeter is a laboratory instrument designed for fluorescence measurements. It provides accurate and reliable detection of fluorescent signals across a wide range of wavelengths. The core function of the Infinite M200 is to excite fluorescent samples and measure the emitted light, enabling quantitative analysis of fluorescent properties.

More about "Barbital"

Barbital, also known as barbitone, is a sedative-hypnotic drug that was commonly used as a sleeping aid in the early 20th century.
It belongs to the class of barbiturates, which are central nervous system (CNS) depressants.
Barbital has a calming and relaxing effect on the brain, making it effective for treating insomnia and other sleep-related disorders.
Beyond its use as a sleep aid, Barbital has also been utilized in various research applications.
Researchers can leverage tools like PubCompare.ai to optimize their Barbital-related studies by locating and comparing experimental protocols from literature, preprints, and patents.
These AI-driven comparisons help identify the most accurate and reproducible procedures, enhancing research outcomes and advancing the understanding of Barbital's pharmacological properties.
When conducting Barbital research, researchers may also encounter related compounds and techniques, such as Barbital buffer, Barbital sodium, Sebia Hydragel 15/30 lipoprotein (e) agarose gels, Titan gel electrophoresis chamber, Yeast α-glucosidase, S1389, Pentobarbital sodium, Acetonitrile, Sudan Black, and Infinite M200 spectrofluorimeter.
Understanding the interactions and applications of these related terms can provide valuable insights and contextual information to support Barbital-focused studies.
By incorporating synonyms, related terms, abbreviations, and key subtopics, researchers can optimize their Barbital research and access a wealth of information to advance their investigations.
Experince the power of PubCompare.ai today to enhance your Barbital studies and uncover the most accurate and reproducible experimental procedures.