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Ammonium bicarbonate

Ammonium bicarbonate is a chemical compound with the chemical formula (NH4)HCO3.
It is a white, crystalline solid that is soluble in water and used in various applications, such as a food additive, leavening agent, and in the production of fertilizers and other chemicals.
Ammonium bicarbonate is an important compound in biochemistry and has various uses in research and industry.
It is an important component of the carbon cycle and plays a role in regulating pH levels in biological systems.
Researchers can optimize their ammonium bicarbonate studies with PubCompare.ai, the leading AI platform for comparing and enhancing research protocols.
This powerful tool can help identify the most effective methods and products to advance your research in this area.

Most cited protocols related to «Ammonium bicarbonate»

1
Fractionation of Colorectal Peptides
Cited 118 times
Human colorectal peptides
were subjected to basic-pH reverse-phase
HPLC fractionation. Mixed and labeled peptides were solubilized in
buffer A (5% ACN, 10 mM ammonium bicarbonate, pH 8.0) and separated
on an Agilent 300 Extend C18 column (5 μm particles, 4.6 mm
i.d., and 20 cm in length). Using an Agilent 1100 binary pump equipped
with a degasser and a photodiode array (PDA) detector, a 50 min linear
gradient from 18% to 45% acetonitrile in 10 mM ammonium bicarbonate
pH 8 (flow rate of 0.8 mL/min) separated the peptide mixture into
a total of 96 fractions. The 96 fractions were consolidated into 24
samples, acidified with 10% formic acid, and vacuum-dried. Each sample
was redissolved with 5% formic acid/5% ACN, desalted via StageTip,
dried via vacuum centrifugation, and reconstituted for LC–MS/MS
analysis.
All LC–MS experiments were performed on a Velos-Orbitrap
Elite mass spectrometer (Thermo Fischer Scientific) coupled to a Proxeon
nLC-1000 (Thermo Fisher Scientific) ultra high-pressure liquid chromatography
(UPLC) pump. Peptides were separated on a 75 μm inner diameter
microcapillary column. The tip for the column was pulled in-house
and the column was packed with approximately 0.5 cm of Magic C4 resin
(5 μm, 100 Å, Michrom Bioresources) followed by 25 cm of
Sepax Technologies GP-C18 resin (1.8 μm, 120 Å). Separation
was achieved by applying a 3–22% ACN gradient in 0.125% formic
acid over 165 min at ∼300 nL/min. Electrospray ionization was
enabled by applying a voltage of 2.0 kV through an IDEX high-pressure
fitting at the inlet of the microcapillary column. In the case of
the two-proteome mixture, the linear gradient was shortened to 70
min.
McAlister G.C., Nusinow D.P., Jedrychowski M.P., Wühr M., Huttlin E.L., Erickson B.K., Rad R., Haas W, & Gygi S.P. (2014). MultiNotch MS3 Enables Accurate, Sensitive, and Multiplexed Detection of Differential Expression across Cancer Cell Line Proteomes. Analytical Chemistry, 86(14), 7150-7158.
Publication 2014
acetonitrile Ammonium ammonium bicarbonate Centrifugation formic acid Fractionation, Chemical High-Performance Liquid Chromatographies Homo sapiens Peptides Proteome Resins, Plant Vacuum
2
Fractionation of Breast Epithelial Cell Proteome
Cited 65 times
Human breast epithelial cells (MCF10A) were transfected with a pQCXIH vector and were cultured in DMEM/F12 (Invitrogen, Carlsbad, CA) supplemented with 5% horse serum (Invitrogen), 20 ng/mL EGF, 0.5 μg/mL hydro-cortisone, 100 ng/mL cholera toxin, 10 μg/mL insulin, and 50 μg/mL penicillin/streptomycin until 70–80% confluence was reached. The cells were then lysed in a buffer containing 8 M urea, 2.5 mM sodium pyrophosphate, 1 mM β-glycerophosphate, 50 mM ammonium bicarbonate, one-third tablet of protease inhibitor, and 2 mM sodium ortho-vanadate. Proteins were denatured, reduced, and alkylated after which tryptic digestions were performed at an enzyme/substrate ratio of 1:50. For method comparison between SCX and RP, digested peptides were cleaned by flowing through a 1 mL solid-phase extraction C18 column (Discovery DSC-18, SUPELCO, Bellefonte, PA). Samples were concentrated using a Speed-Vac SC 250 Express (Thermo Savant, Holbrook, NY) and stored at −80°C until time for analysis. A 300.0 μg desalted peptide sample was used for each SCX, low-pH RPLC, and high-pH RPLC fractionation. A 300.0 μg nondesalted protein digest was used to evaluate the potential of high-pH approach for desalting.
Wang Y., Yang F., Gritsenko M.A., Wang Y., Clauss T., Liu T., Shen Y., Monroe M.E., Lopez-Ferrer D., Reno T., Moore R.J., Klemke R.L., Camp DG I.I, & Smith R.D. (2011). Reversed-phase chromatography with multiple fraction concatenation strategy for proteome profiling of human MCF10A cells. Proteomics, 11(10), 2019-2026.
Publication 2011
ammonium bicarbonate beta-glycerol phosphate Breast Buffers Cells Cholera Toxin Cloning Vectors Cortisone Digestion Enzymes Epithelial Cells Equus caballus Fractionation, Chemical Homo sapiens Insulin Penicillins Peptides Protease Inhibitors Proteins Serum sodium pyrophosphate Sodium Vanadate Solid Phase Extraction Streptomycin Tablet Trypsin Urea
3
Lipid Extraction from Diluted Plasma
Cited 53 times
The lipid extraction (adapted from Matyash et al. 23 (link)) was carried out in high grade polypropylene deep well plates. Fifty microliters of diluted plasma (50×) (equivalent of 1 μL of undiluted plasma) was mixed with 130 μL of ammonium bicarbonate solution and 810 μL of methyl tert-butyl ether/methanol (7:2, v/v) solution was added. Twenty-one microliters of internal standard mixture was pre-mixed with the organic solvents mixture. The internal standard mixture contained: 50 pmol of lysophasphatidylglycerol (LPG) 17:1, 50 pmol of lysophosphatic acid (LPA) 17:0, 500 pmol of phosphatidylcholine (PC) 17:0/17:0, 30 pmol of hexosylceramide (HexCer) 18:1;2/12:0, 50 pmol of phosphatidylserine (PS) 17:0/17:0, 50 pmol of phosphatidylglycerol (PG) 17:0/17:0, 50 pmol of phosphatic acid (PA) 17:0/17:0, 50 pmol of lysophposphatidylinositol (LPI 17:1), 50 pmol of lysophosphatidylserine (LPS) 17:1, 1 nmol cholesterol (Chol) D6, 100 pmol of diacylglycerol (DAG) 17:0/17:0, 50 pmol of triacylglycerol (TAG) 17:0/17:0/17:0, 50 pmol of ceramide (Cer) 18:1;2/17:0, 200 pmol of sphingomyelin (SM) 18:1;2/12:0, 50 pmol of lysophosphatidylcholine (LPC) 12:0, 30 pmol of lysophosphatidylethanolamine (LPE) 17:1, 50 pmol of phosphatidylethanolamine (PE) 17:0/17:0, 100 pmol of cholesterol ester (CE) 20:0, 50 pmol of phosphatidylinositol (PI) 16:0/16:0. The plate was then sealed with a teflon-coated lid, shaken at 4°C for 15 min, and spun down (3000 g, 5 min) to facilitate separation of the liquid phases and clean-up of the upper organic phase. Hundred microliters of the organic phase was transferred to an infusion plate and dried in a speed vacuum concentrator. Dried lipids were re-suspended in 40 μL of 7.5 mM ammonium acetate in chloroform/methanol/propanol (1:2:4, v/v/v) and the wells were sealed with an aluminum foil to avoid evaporation and contamination during infusion. All liquid handling steps were performed using Hamilton STARlet robotic platform with the Anti Droplet Control feature for organic solvents pipetting.
Surma M.A., Herzog R., Vasilj A., Klose C., Christinat N., Morin-Rivron D., Simons K., Masoodi M, & Sampaio J.L. (2015). An automated shotgun lipidomics platform for high throughput, comprehensive, and quantitative analysis of blood plasma intact lipids. European Journal of Lipid Science and Technology, 117(10), 1540-1549.
Full text: Click here
Publication 2015
1-Propanol Acids Aluminum ammonium acetate ammonium bicarbonate Ceramides Chloroform Cholesterol Cholesterol Esters Diacylglycerol Lipids Lysophosphatidylcholines lysophosphatidylethanolamine lysophosphatidylserine Methanol methyl tert-butyl ether Phosphates Phosphatidylcholines phosphatidylethanolamine Phosphatidyl Glycerol Phosphatidylinositols Phosphatidylserines Plasma Polypropylenes Solvents Sphingomyelins Teflon Triglycerides Vacuum
4
Cross-linking and Enrichment of E. coli Proteins
Cited 51 times
Leiker bAL222 was used to cross-link the E. coli MG1655 whole-cell lysates. MG1655 was cultured in unlabeled or 15N-labeled M9 medium and collected at OD600 0.6–0.8. Pellets of 40 OD*ml E. coli cells was resuspended in 0.4 ml lysis buffer (50 mM HEPES, pH 7.5, 150 mM NaCl). Cell lysates were prepared using a FastPrep homogenizer (6.5 m/s, 20 s, repeat 5 times). After measuring protein concentration, 1 mg of unlabeled and 15N-labeled lysate was cross-linked separately with 0.33 mg [d0]-bAL2 for 0.5 h at room temperature. Cross-linking reactions were quenched with 20 mM ammonium bicarbonate. The two reactions were mixed together and then precipitated by trichloroacetic acid (TCA) followed by Trypsin digestion. After filtering with a 50 kDa cutoff Amicon Ultra-0.5 Centrifugal Filter Unit, the digested peptides were brought to a volume of 3 mL with 2% ACN, 20 mM HEPES, pH 8.2; the pH was adjusted to 10.0 with ammonia. High-pH reverse-phase separation was used for fractionation. The peptides were eluted with buffer B (80% ACN, 5 mM NH4COOH, pH 10) gradient. A total of 39 two-minute fractions were collected and then combined into five fractions of similar shades of color (bAL2-linked peptides are bright yellow before cleavage of the biotin tag). Each pooled sample was evaporated to 200–300 µl before enrichment of bAL2-linked peptides on 50 µl high-capacity streptavidin beads. After release of beads and desalting through a C18 column, the five fractions of bAL2-linked peptides were analyzed by liquid chromatography–tandem mass spectrometry (LC-MS/MS) using a Q-Exactive HF mass spectrometer coupled with an EASY-nLC 1000 system (both from Thermo Fisher Scientific). Precursors of the + 1, + 2, + 8, or above, or unassigned charge states were rejected and dynamic exclusion was set to 20 s.
Chen Z.L., Meng J.M., Cao Y., Yin J.L., Fang R.Q., Fan S.B., Liu C., Zeng W.F., Ding Y.H., Tan D., Wu L., Zhou W.J., Chi H., Sun R.X., Dong M.Q, & He S.M. (2019). A high-speed search engine pLink 2 with systematic evaluation for proteome-scale identification of cross-linked peptides. Nature Communications, 10, 3404.
Full text: Click here
Publication 2019
Ammonia ammonium bicarbonate Biotin Buffers Cells Cytokinesis Digestion Escherichia coli Fractionation, Chemical HEPES Liquid Chromatography Pellets, Drug Peptides Proteins Sodium Chloride Streptavidin Tandem Mass Spectrometry Trichloroacetic Acid Trypsin
5
Quantitative Proteomics Workflow for E. coli
Cited 46 times
The E. coli K12 strain was grown in standard LB medium, harvested, washed in PBS, and lysed in 4% SDS, 100 mm Tris, pH 8.5. Lysates were briefly boiled and DNA sheared using a Sonifier (Branson Model 250). Lysates were cleared by centrifugation at 15,000 × g for 15 min and precipitated with acetone. Proteins were resuspended in 8 m urea, 25 mm Tris, pH 8.5, 10 mm DTT. After 30 min of incubation, 20 mm iodoacetamide was added for alkylation. The sample was then diluted 1:3 with 50 mm ammonium bicarbonate buffer, and the protein concentration was estimated via tryptophan fluorescence emission assay. After 5 h of digestion with LysC (Wako Chemicals) at room temperature, the sample was further diluted 1:3 with ammonium bicarbonate buffer, and trypsin (Promega) digestion was performed overnight (protein-to-enzyme ratio of 60:1 in each case). E. coli peptides were then purified by using a C18 Sep Pak cartridge (Waters, Milford, MA) according to the manufacturer's instructions. UPS1 and UPS2 standards (Sigma-Aldrich) were resuspended in 30 μl of 8 m urea, 25 mm Tris, pH 8.5, 10 mm DTT and reduced, alkylated, and digested in an analogous manner, but with a lower protein-to-enzyme ratio (12:1 for UPS1 and 10:1 for UPS2, both LysC and trypsin). UPS peptides were then purified using C18 StageTips. E. coli and UPS peptides were quantified based on absorbance at 280 nm using a NanoDrop spectrophotometer (Fisher Scientific). For each run, 2 μg of E. coli peptides were then spiked with 0.15 μg of either UPS1 or UPS2 peptides, and about 1.6 μg of the mix was then analyzed via liquid chromatography combined with mass spectrometry on a Q Exactive (Thermo Fisher). Data were analyzed with MaxQuant as described above for the proteome dataset. All files were searched against the E. coli complete proteome sequences plus those of the UPS proteins and common contaminants.
Cox J., Hein M.Y., Luber C.A., Paron I., Nagaraj N, & Mann M. (2014). Accurate Proteome-wide Label-free Quantification by Delayed Normalization and Maximal Peptide Ratio Extraction, Termed MaxLFQ. Molecular & Cellular Proteomics : MCP, 13(9), 2513-2526.
Publication 2014
Acetone Alkylation ammonium bicarbonate Biological Assay Buffers Centrifugation Digestion Enzymes Escherichia coli Escherichia coli K12 Fluorescence Iodoacetamide Liquid Chromatography Mass Spectrometry peptide E (adrenal medulla) Peptides Promega Proteins Proteome Staphylococcal Protein A Strains Tromethamine Trypsin Tryptophan Urea

Most recents protocols related to «Ammonium bicarbonate»

1
Soil Fumigation Techniques for Chinese Cabbage
Field experiment was conducted during the growing season from June to August 2021 under four different situations: NB; soil fumigation with lime (0.15 kg/m2), N; soil fumigation with ammonium bicarbonate (0.15 kg/m2), LNB; soil fumigation with combined lime (0.15 kg/m2) and ammonium bicarbonate (0.15 kg/m2), and GZ; no soil fumigation as control. After soil amendments with ammonium bicarbonate and lime, the field was divided into plots (3 m × 9 m) and covered with 0.08 mm film for 15 days for anaerobic soil fumigation. The experiment was performed using a randomized complete block design and repeated three times with 3 plots/treatment (in total 12 plots), and each plot contained 120 plants of Chinese cabbage. The Di, DI, CE, and soil pH from each treatment were recorded at the completion of the trial as described above using the methodology of Zhang et al. (2022a) (link).
Zhang J., Zhou X., Zhang Y., Dai Z., He Z., Qiu Y., Alharbi S.A., Wei F., Wei L., Ahmed W, & Ji G. (2024). Pre-soil fumigation with ammonium bicarbonate and lime modulates the rhizosphere microbiome to mitigate clubroot disease in Chinese cabbage. Frontiers in Microbiology, 15, 1376579.
Full text: Click here
Publication 2024
2
Clubroot Control in Chinese Cabbage
The greenhouse experiment was performed from March to May 2021 under controlled conditions: 30/18°C day/night temperature and 10/14 h light/dark photoperiod (Zhang et al., 2022b (link)). The pots (24 × 18 cm diameter) were filled with 3.5 kg/pot of diseased soil heavily infected with clubroot pathogen collected from the field (Xiadabai County, Kunming, China). Lime and ammonium bicarbonate were added to each pot at the ratio 1:1,300 (m/m), mixed thoroughly with the diseased soil, covered with plastic film (0.08 mm), and placed in a greenhouse at >35°C. The experiment was performed under four different conditions: NB; soil fumigation with lime (2.69 g/pot), N; soil fumigation with ammonium bicarbonate (2.69 g/pot), LNB; soil fumigation with combined ammonium bicarbonate (2.69 g/pot) and lime (2.69 g/pot), and GZ; no soil fumigation as control. After 15 days of anaerobic soil fumigation, Chinese cabbage seedlings were transplanted in pots (5 plants/pots). In addition, fertilizer was applied in each pot before the transplantation of seedlings to overcome the nutrient deficiency (Wei et al., 2021 (link)). The experiment was repeated three times with 15 plants per replication (in total, 45 plants/treatment) and was accomplished using a completely randomized design.
Zhang J., Zhou X., Zhang Y., Dai Z., He Z., Qiu Y., Alharbi S.A., Wei F., Wei L., Ahmed W, & Ji G. (2024). Pre-soil fumigation with ammonium bicarbonate and lime modulates the rhizosphere microbiome to mitigate clubroot disease in Chinese cabbage. Frontiers in Microbiology, 15, 1376579.
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Publication 2024
3
Improving Wheat Root Growth under Ammonium
Seeds of wheat (cultivar Jimai 22) were surface-sterilized using 70% ethanol for 45 s and washed 5 times with distilled water. The sterilized seeds were then germinated on moist filter paper placed inside Petri dishes at 23 °C. After 3 days, the uniform-sized seedlings were transferred to black plastic pots with dimensions of 10 cm × 8 cm × 5 cm (length, width, height) containing distilled water and grown in a growth chamber at 25 °C/21 °C (day/night) under 14 h/10 h (light/dark) for 5 days under the following conditions: light intensity 450 µmol m−2 s−1 and humidity 70 ± 5%. Each pot contained 15 plants and the distilled water was renewed every 2 days.
In our preliminary experiment, we found that the roots of 8-day-old seedlings grew best in half-strength Hoagland nutrient solution containing 7.5 mM NO3− (Table S1), and 7.5 mM NH4+ showed significant inhibition of root growth compared with 7.5 mM NO3−. An experiment using gradient concentrations showed that 3 mM HCO3− significantly improved the root growth of wheat seedlings fed 7.5 mM NH4+. Therefore, the following experiment was conducted using 8-day-old seedlings that were fixed on polystyrene plates and hydroponically cultured in half-strength Hoagland nutrient solution containing 7.5 mM NO3− (CK, applied as KNO3 and Ca(NO3)2), 7.5 mM NH4+ (sole ammonium (SA), applied as 7.5 mM NH4Cl), or 7.5 mM NH4+ + 3 mM HCO3− (ammonium and bicarbonate (AC), applied as 7.5 mM NH4Cl and 3 mM KHCO3). The solutions were renewed every 2 days. Each treatment was repeated in triplicate. Potassium in the nutrient solution was balanced by the addition of K2SO4.
Liu X., Zhang Y., Tang C., Li H., Xia H., Fan S, & Kong L. (2024). Bicarbonate-Dependent Detoxification by Mitigating Ammonium-Induced Hypoxic Stress in Triticum aestivum Root. Biology, 13(2), 101.
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Publication 2024
4
Nitrogen Fertilizer and Soil Moisture Effects
A soil sample bag with a height of 30 cm and an inner diameter of 10 cm was adopted. The soil required to fill a 21 cm soil column was calculated as 850 g, and the air-dried soil treated in the early stage was weighed and evenly filled to form a soil column. The soil was treated with water injection to ensure that the water content in the bag was 30%, 40%, and flooded, respectively, and stood for 24 h. Each soil water content was treated as follows: local farmers commonly use urea, ammonium bicarbonate, ammonium bicarbonate, and ammonium sulfate. Four nitrogen fertilizers (i.e., ammonium bicarbonate, ammonium sulfate, ammonium chloride, and urea) were treated with oxalic acid, DMPP, and NBPT, respectively (A1 ammonium bicarbonate, A2 ammonium bicarbonate + oxalic acid, A3 ammonium bicarbonate +DMPP, A4 ammonium bicarbonate +NBPT, collectively referred to as A treatment; B1 ammonium sulfate, B2 ammonium sulfate + oxalic acid, B3 ammonium sulfate +DMPP, B4 ammonium sulfate +NBPT, collectively referred to as B treatment; C1 ammonium chloride, C2 ammonium chloride + oxalic acid, C3 ammonium chloride +DMPP, C4 ammonium chloride +NBPT, collectively referred to as C treatment; D1 urea, D2 urea + oxalic acid, D3 urea +DMPP, D4 urea +NBPT, collectively referred to as D treatment). Each treatment was replicated three times. The mixture was applied to the surface of the soil column after resting. Then, the soil was covered at 135 g, the height was 3 cm, and the specific amount of water injected was calculated according to the quality of the covering soil. The mouth of the soil column was wrapped and sealed with a rope, and five small holes with a diameter of about 1 cm were pricked with needles to ensure ventilation, avoid an anaerobic environment, reduce water loss, and maintain soil water content during cultivation. Then, the soil column was placed horizontally indoors for 30 days.
Jiafeng W, & Qiuliang C. (2024). Nitrogen migration and transformation characteristics of the soil in karst areas under the combined application of oxalic acid and urea inhibitors. Frontiers in Plant Science, 15, 1386912.
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Publication 2024
5
Quantification of cAMP in CNBD Proteins
Determination of the cAMP content of purified CNBD proteins performed following the procedure previously described13 (link). Endogenous cAMP bound to His6-MBP tagged HCN1/2 CNBDs purified from Escherichiacoli Rosetta strain (EMD Millipore) was released by boiling the protein sample (∼1 mg) for 2 min. The boiled protein samples were centrifuged at maximum speed for 10 min, at room temperature, and the supernatant was diluted in 5 mM ammonium bicarbonate. The sample was loaded onto an anion exchange chromatography column (HiTrapQ (1 ml), GE Healthcare), previously equilibrated with 5 mM ammonium bicarbonate. After a washing step (7 column volumes) with 5 mM ammonium bicarbonate, cAMP was eluted with a linear gradient of ammonium bicarbonate (5–1000 mM) in 20 column volumes. Calibration curves were performed by loading in the HiTrapQ column 5, 10 and 20 nmoles of cAMP diluted in 5 mM ammonium bicarbonate. Chromatographies were performed at 4 °C and monitored using the AKTApurifier UPC 10 fast protein liquid system (GE Healthcare). Calculation of the area of the peaks of cAMP eluted from the HiTrapQ column was performed by using the software UNICORN5.11.
Porro A., Saponaro A., Castelli R., Introini B., Hafez Alkotob A., Ranjbari G., Enke U., Kusch J., Benndorf K., Santoro B., DiFrancesco D., Thiel G, & Moroni A. (2024). A high affinity switch for cAMP in the HCN pacemaker channels. Nature Communications, 15, 843.
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Publication 2024

Top products related to «Ammonium bicarbonate»

1
Trypsin by Promega
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Trypsin is a serine protease enzyme that is commonly used in cell culture and molecular biology applications. It functions by cleaving peptide bonds at the carboxyl side of arginine and lysine residues, which facilitates the dissociation of adherent cells from cell culture surfaces and the digestion of proteins.
2
Ammonium bicarbonate by Merck Group
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Ammonium bicarbonate is a chemical compound with the formula (NH4)HCO3. It is a white crystalline solid that is commonly used as a leavening agent in baking and as a source of carbon dioxide in certain industrial processes.
3
Iodoacetamide by Merck Group
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Iodoacetamide is a chemical compound commonly used in biochemistry and molecular biology laboratories. It is a reactive compound that selectively modifies cysteine residues in proteins, thereby allowing for the study of protein structure and function. Iodoacetamide is often used in sample preparation procedures for mass spectrometry and other analytical techniques.
4
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Dithiothreitol (DTT) is a reducing agent commonly used in biochemical and molecular biology applications. It is a small, water-soluble compound that helps maintain reducing conditions and prevent oxidation of sulfhydryl groups in proteins and other biomolecules.
5
Formic acid by Merck Group
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Formic acid is a colorless, pungent-smelling liquid chemical compound. It is the simplest carboxylic acid, with the chemical formula HCOOH. Formic acid is widely used in various industrial and laboratory applications.
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Sequencing grade trypsin is a proteolytic enzyme used to cleave peptide bonds in protein samples, primarily for use in protein sequencing applications. It is purified to ensure high-quality, consistent performance for analytical processes.
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Sequencing grade modified trypsin is a protease enzyme used for the digestion of proteins prior to mass spectrometry analysis. It is designed to provide consistent, high-quality peptide digestion for protein identification and characterization.
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Acetonitrile is a colorless, volatile, flammable liquid. It is a commonly used solvent in various analytical and chemical applications, including liquid chromatography, gas chromatography, and other laboratory procedures. Acetonitrile is known for its high polarity and ability to dissolve a wide range of organic compounds.

More about "Ammonium bicarbonate"

Ammonium bicarbonate, also known as ammonium hydrogen carbonate or bicarbonate of ammonia, is a versatile chemical compound with the formula (NH4)HCO3.
This white, crystalline solid is soluble in water and has a wide range of applications, including use as a food additive, leavening agent, and in the production of fertilizers and other chemicals.
Ammonium bicarbonate plays a crucial role in biochemistry and the carbon cycle, helping to regulate pH levels in biological systems.
Researchers can optimize their studies on ammonium bicarbonate, as well as related compounds like trypsin, iodoacetamide, dithiothreitol, formic acid, and sequencing-grade trypsin, by utilizing PubCompare.ai - the leading AI platform for comparing and enhancing research protocols.
This powerful tool can help identify the most effective methods and products to advance your research in these areas, allowing you to stay ahead of the curve and drive scientific progress forward.
Whether you're investigating the role of ammonium bicarbonate in the carbon cycle, exploring its use as a food additive or leavening agent, or studying its interactions with other biochemical compounds, PubCompare.ai can provide valuable insights and guidance to optimize your research workflow.
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