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Ammonium phosphate

Ammonium phosphate is a chemical compound composed of ammonium (NH4+) and phosphate (PO4^3-) ions.
It is widely used in fertilizers, flame retardants, and as a food additive.
Ammonium phosphate plays a key role in plant nutrition, soil amendment, and fire safety applications.
Researchers studying ammonium phosphate can leverage PubCompare.ai to optimaize their research process, easily locate relevant protocols, and identify the best products and methods through intelligent comparisons.
This AI-powered platform enhaces reproducibility and accuracy in ammonium phosphate studies, making it the ultimate tool for researchrs in this field.

Most cited protocols related to «Ammonium phosphate»

Comprehensive Antioxidant and Enzyme Inhibitory Assays

Antioxidant (DPPH and ABTS radical scavenging, reducing power (CUPRAC and FRAP), phosphomolybdenum, and metal chelating (ferrozine method)) and enzyme inhibitory activities [cholinesterase (ChE) Elmann’s method], tyrosinase (dopachrome method), α-amylase (iodine/potassium iodide method), and α -glucosidase (chromogenic PNPG method)) were determined using the methods previously described by Zengin et al. (2014) (link) and Dezsi et al. (2015) (link).
For the DPPH (1,1-diphenyl-2-picrylhydrazyl) radical scavenging assay: Sample solution (1 mg/mL; 1 mL) was added to 4 mL of a 0.004% methanol solution of DPPH. The sample absorbance was read at 517 nm after a 30 min incubation at room temperature in the dark. DPPH radical scavenging activity was expressed as millimoles of trolox equivalents (mg TE/g extract).
For ABTS (2,2′-azino-bis(3-ethylbenzothiazoline) 6-sulfonic acid) radical scavenging assay: Briefly, ABTS+ was produced directly by reacting 7 mM ABTS solution with 2.45 mM potassium persulfate and allowing the mixture to stand for 12–16 in the dark at room temperature. Prior to beginning the assay, ABTS solution was diluted with methanol to an absorbance of 0.700 ± 0.02 at 734 nm. Sample solution (1 mg/mL; 1 mL) was added to ABTS solution (2 mL) and mixed. The sample absorbance was read at 734 nm after a 30 min incubation at room temperature. The ABTS radical scavenging activity was expressed as millimoles of trolox equivalents (mmol TE/g extract) (Mocan et al., 2016a (link)).
For CUPRAC (cupric ion reducing activity) activity assay: Sample solution (1 mg/mL; 0.5 mL) was added to premixed reaction mixture containing CuCl₂ (1 mL, 10 mM), neocuproine (1 mL, 7.5 mM) and NH₄Ac buffer (1 mL, 1 M, pH 7.0). Similarly, a blank was prepared by adding sample solution (0.5 mL) to premixed reaction mixture (3 mL) without CuCl₂. Then, the sample and blank absorbances were read at 450 nm after a 30 min incubation at room temperature. The absorbance of the blank was subtracted from that of the sample. CUPRAC activity was expressed as milligrams of trolox equivalents (mg TE/g extract).
For FRAP (ferric reducing antioxidant power) activity assay: Sample solution (1 mg/mL; 0.1 mL) was added to premixed FRAP reagent (2 mL) containing acetate buffer (0.3 M, pH 3.6), 2,4,6-tris(2-pyridyl)-S-triazine (TPTZ) (10 mM) in 40 mM HCl and ferric chloride (20 mM) in a ratio of 10:1:1 (v/v/v). Then, the sample absorbance was read at 593 nm after a 30 min incubation at room temperature. FRAP activity was expressed as milligrams of trolox equivalents (mg TE/g extract).
For phosphomolybdenum method: Sample solution (1 mg/mL; 0.3 mL) was combined with 3 mL of reagent solution (0.6 M sulfuric acid, 28 mM sodium phosphate and 4 mM ammonium molybdate). The sample absorbance was read at 695 nm after a 90 min incubation at 95°C. The total antioxidant capacity was expressed as millimoles of trolox equivalents (mmol TE/g extract) (Mocan et al., 2016c (link)).
For metal chelating activity assay: Briefly, sample solution (1 mg/mL; 2 mL) was added to FeCl₂ solution (0.05 mL, 2 mM). The reaction was initiated by the addition of 5 mM ferrozine (0.2 mL). Similarly, a blank was prepared by adding sample solution (2 mL) to FeCl₂ solution (0.05 mL, 2 mM) and water (0.2 mL) without ferrozine. Then, the sample and blank absorbances were read at 562 nm after 10 min incubation at room temperature. The absorbance of the blank was sub-tracted from that of the sample. The metal chelating activity was expressed as milligrams of EDTA (disodium edetate) equivalents (mg EDTAE/g extract).
For ChE inhibitory activity assay: Sample solution (1 mg/mL; 50 μL) was mixed with DTNB (5,5-dithio-bis(2-nitrobenzoic) acid, Sigma, St. Louis, MO, United States) (125 μL) and AChE [acetylcholines-terase (Electric ell AChE, Type-VI-S, EC 3.1.1.7, Sigma)], or BChE [BChE (horse serum BChE, EC 3.1.1.8, Sigma)] solution (25 μL) in Tris–HCl buffer (pH 8.0) in a 96-well microplate and incubated for 15 min at 25°C. The reaction was then initiated with the addition of acetylthiocholine iodide (ATCI, Sigma) or butyrylthiocholine chloride (BTCl, Sigma) (25 μL). Similarly, a blank was prepared by adding sample solution to all reaction reagents without enzyme (AChE or BChE) solution. The sample and blank absorbances were read at 405 nm after 10 min incubation at 25°C. The absorbance of the blank was subtracted from that of the sample and the cholinesterase inhibitory activity was expressed as galanthamine equivalents (mgGALAE/g extract) (Mocan et al., 2016b (link)).
For Tyrosinase inhibitory activity assay: Sample solution (1 mg/mL; 25 μL) was mixed with tyrosinase solution (40 μL, Sigma) and phosphate buffer (100 μL, pH 6.8) in a 96-well microplate and incubated for 15 min at 25°C. The reaction was then initiated with the addition of L-DOPA (40 μL, Sigma). Similarly, a blank was prepared by adding sample solution to all reaction reagents without enzyme (tyrosinase) solution. The sample and blank absorbances were read at 492 nm after a 10 min incubation at 25°C. The absorbance of the blank was subtracted from that of the sample and the tyrosinase inhibitory activity was expressed as kojic acid equivalents (mgKAE/g extract) (Mocan et al., 2017 (link)).
For α-amylase inhibitory activity assay: Sample solution (1 mg/mL; 25 μL) was mixed with α-amylase solution (ex-porcine pancreas, EC 3.2.1.1, Sigma) (50 μL) in phosphate buffer (pH 6.9 with 6 mM sodium chloride) in a 96-well microplate and incubated for 10 min at 37°C. After pre-incubation, the reaction was initiated with the addition of starch solution (50 μL, 0.05%). Similarly, a blank was prepared by adding sample solution to all reaction reagents without enzyme (α-amylase) solution. The reaction mixture was incubated 10 min at 37°C. The reaction was then stopped with the addition of HCl (25 μL, 1 M). This was followed by addition of the iodine-potassium iodide solution (100 μL). The sample and blank absorbances were read at 630 nm. The absorbance of the blank was subtracted from that of the sample and the α-amylase inhibitory activity was expressed as acarbose equivalents (mmol ACE/g extract) (Savran et al., 2016 (link)).
For α-glucosidase inhibitory activity assay: Sample solution (1 mg/mL; 50 μL) was mixed with glutathione (50 μL), α-glucosidase solution (from Saccharomyces cerevisiae, EC 3.2.1.20, Sigma) (50 μL) in phosphate buffer (pH 6.8) and PNPG (4-N-trophenyl-α-D-glucopyranoside, Sigma) (50 μL) in a 96-well microplate and incubated for 15 min at 37°C. Similarly, a blank was prepared by adding sample solution to all reaction reagents without enzyme (α-glucosidase) solution. The reaction was then stopped with the addition of sodium carbonate (50 μL, 0.2 M). The sample and blank absorbances were read at 400 nm. The absorbance of the blank was subtracted from that of the sample and the α-glucosidase inhibitory activity was expressed as acarbose equivalents (mmol ACE/g extract) (Llorent-Martínez et al., 2016 (link)).
All the assays were carried out in triplicate. The results are expressed as mean values and standard deviation (SD). The differences between the different extracts were analyzed using one-way analysis of variance (ANOVA) followed by Tukey’s honestly significant difference post hoc test with α = 0.05. This treatment was carried out using SPSS v. 14.0 program.

Uysal S., Zengin G., Locatelli M., Bahadori M.B., Mocan A., Bellagamba G., De Luca E., Mollica A, & Aktumsek A. (2017). Cytotoxic and Enzyme Inhibitory Potential of Two Potentilla species (P. speciosa L. and P. reptans Willd.) and Their Chemical Composition. Frontiers in Pharmacology, 8, 290.

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Publication 2017

Crystallization of H1R-T4L in Pichia pastoris

H₁R-T4L was expressed in yeast Pichia pastoris. Ligand binding assays were performed as described in Methods. Pichia pastoris membranes were solubilized using 1% (w/v) n-dodecyl-β-D-maltopyranoside and 0.2% (w/v) cholesteryl hemisuccinate, and purified by immobilized metal ion affinity chromatography (IMAC). After IMAC, the C-terminal GFP was cleaved by Tobacco Etch virus (TEV) protease. Then the sample mixture was passed through IMAC to remove the cleaved His-tagged GFP and TEV protease. Receptor crystallization was performed by lipidic cubic phase (LCP) method. The protein-LCP mixture contained 40% (w/w) receptor solution, 54% (w/w) monoolein, and 6% (w/w) cholesterol. Crystals were grown in 40-50 nl protein-laden LCP boluses overlaid by 0.8 μl of precipitant solution (26-30% (v/v) PEG400, 300 mM ammonium phosphate, 10 mM MgCl₂, 100 mM Na-citrate pH 4.5 and 1 mM doxepin) at 20 °C. Crystals were harvested directly from LCP matrix and flash frozen in liquid nitrogen. X-ray diffraction data were collected at 100 K with a beam size of 10 × 10 microns on the microfocus beamline I24 at the Diamond Light Source (UK). Data collection, processing, structure solution and refinement are described in Methods.

Shimamura T., Shiroishi M., Weyand S., Tsujimoto H., Winter G., Katritch V., Abagyan R., Cherezov V., Liu W., Han G.W., Kobayashi T., Stevens R.C, & Iwata S. (2011). Structure of the human histamine H1 receptor complex with doxepin. Nature, 475(7354), 65-70.

Publication 2011

ammonium phosphate Biological Assay Cholesterol cholesterol-hemisuccinate Chromatography, Affinity Citrate Crystallization Cuboid Bone Diamond Doxepin Freezing Komagataella pastoris Ligands Lipids Magnesium Chloride Metals monoolein Nitrogen polyethylene glycol 400 Proteins Saccharomyces cerevisiae TEV protease Tissue, Membrane TNFSF14 protein, human X-Ray Diffraction

Isolating White Blood Cells from Whole Blood

To generate white blood cells (WBC), red blood cells were lysed from whole human blood, which was collected using either ethylenediaminetetraacetic acid (EDTA) or acid citrate dextrose (ACD) as a coagulant. Blood was mixed at a 1:10 ratio with ammonium-chloride‑potassium (ACK) lysis buffer (150 mM NH₄Cl, 10 mM KHCO₃, 0.1 mM Na₂EDTA, pH 7.4) and incubated for 5 min at room temperature. The WBCs were pelleted by centrifugation (500 ×g, 5 min) at room temperature and then washed with cold phosphate-buffered saline (PBS). For the isolation of human neutrophils, whole blood was mixed with hetasep (Stemcell) in a 1:5 ratio and incubated for 30 min to separate leukocytes from erythrocytes. Subsequently, the straw-colored layer of leukocytes was transferred to a fresh tube and neutrophils were isolated using the direct human neutrophil isolation kit (Stemcell) according to manufacturer's instructions. Both WBCs and purified neutrophils were finally diluted in complete R10 media (RPMI-1640 media (Sigma) with 10% FBS, 2 mM L-Gluthamine and 100 U/ml penicillin/streptomycin) for each assay.

Karsten C.B., Mehta N., Shin S.A., Diefenbach T.J., Slein M.D., Karpinski W., Irvine E.B., Broge T., Suscovich T.J, & Alter G. (2019). A versatile high-throughput assay to characterize antibody-mediated neutrophil phagocytosis. Journal of Immunological Methods, 471, 46-56.

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Publication 2019

acid citrate dextrose Ammonium Biological Assay Blood Centrifugation Chloride, Ammonium Coagulants Cold Temperature Edetic Acid Erythrocytes Homo sapiens isolation Leukocytes Neutrophil Penicillins Phosphates Potassium potassium bicarbonate Potassium Chloride Saline Solution Stem Cells Streptomycin

Investigating Glyoxalase 1 (GLO1) Depletion in Melanoma and Prostate Carcinoma

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Publication 2020

Nanobody Conjugation and Affinity Isolation

Recombinant nanobodies were conjugated to epoxy-activated magnetic Dynabeads (Life Technologies), with minor modifications to published IgG coupling conditions^{57 (link)}. 10 μg recombinant protein was used per 1 mg of Dynabeads, with conjugations carried out in 0.1 M sodium phosphate, pH 8.0 and 1 M ammonium sulfate, with an 18–20 hour incubation at 30°C. Affinity isolations of yeast Nup84-GFP were carried out as previously described, using binding buffer consisting of 20 mM HEPES, pH 7.4, 500 mM NaCl, 2 mM MgCl₂, 0.1% CHAPS, 0.1 M PMSF, and 3 μg/ml pepstatin A^{57 (link)}. For each experiment, 50 μl of bead slurry was used with 0.5 g of yeast cells. Similar conditions were used for HTB2-mCherry isolations (from yeast with HTB2 genomically tagged at the C-terminus with mCherry^{58 (link)}), except lysate was sonicated 4 times for 10 s before centrifugation, and the binding buffer consisted of 20 mM HEPES, pH 8.0, 300 mM NaCl, 110 mM KOAc, 0.1% Tween-20, 0.1% Triton X-100, 0.1 M PMSF, and 3 μg/ml pepstatin A. Isolations of RBM7-GFP from HeLa cells were performed as previously described^{4 (link)}. 10 μl of bead slurry was used with 100 mg of cells, using a binding buffer of 20 mM HEPES, pH 7.4, 300 mM NaCl, 0.5% Triton X-100, with cOmplete Protease Inhibitor, EDTA-free (Roche).
To determine affinity isolation yields, samples of resuspended lysate were taken before and after Dynabead binding. These were run on a 4–12% Novex Bis-Tris gel in MES running buffer (Life Technologies), and probed by Western blotting using mouse anti-GFP antibody (Roche, cat. no. 11 814 460 001) diluted 1:1,000 in TBST/2% dry milk and an anti-mouse, HRP-conjugated secondary (GE Healthcare, cat. no. NA931V) diluted 1:3,000 in TBST/2% dry milk. Signals were quantified using ImageJ software.

Fridy P.C., Li Y., Keegan S., Thompson M.K., Nudelman I., Scheid J.F., Oeffinger M., Nussenzweig M.C., Fenyö D., Chait B.T, & Rout M.P. (2014). A robust pipeline for rapid production of versatile nanobody repertoires. Nature methods, 11(12), 1253-1260.

Publication 2014

Most recents protocols related to «Ammonium phosphate»

Synthesis of AZP@GO-Cs Composite

To prepare AZP (zinc ammonium phosphate), a 0.3 M solution of Zn(NO₃)₂ (zinc nitrate) was added to a 0.3 M solution of (NH₄)₂HPO₄ (diammonium phosphate) at room temperature (RT). The pH of the solution was adjusted to about nine by adding NH₄OH 28%, and the reaction was allowed to proceed for 12 h at RT under vigorous stirring. Then, it was left for another 24 h, then the illiquid material was dried in a vacuum oven^{23 (link)}. After that, 0.50 g of GO was dispersed in DW using an ultrasonic bath for 20 min and added dropwise to a clear solution containing 5 g of Cs in 50 ml of 10% AA, and mixed slowly for 12 h to obtain the GO-Cs coating material. In the end, 5 g of AZP was mixed with 500 mg of GO-Cs, and after that, the AZP@GO-Cs were dried at RT.

Raiesi Ardali T., Ma’mani L., Chorom M., Motamedi E, & Fathi Gharebaba M. (2024). A biocompatible NPK+Fe+Zn slow release fertilizer: synthesis and its evaluation in tomato plant growth improvement. Scientific Reports, 14, 4640.

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Publication 2024

Phosphate Adsorption on Biochar

All
chemicals were purchased
from Aladdin Industrial Corporation except for humic acid (HA) that
was provided by Aldrich-Sigma. These chemicals were analytical reagent
grade (AR) or better and directly used without any pretreatment. A
1000 mg/L phosphate stock solution was obtained by dissolving KH₂PO₄ into ultrapure water with resistivity higher
than 18.25 MΩ·cm. It was subjected to a stepwise dilution
for further experimental uses. Corn stalk (CS) was used as the precursor
for biochar and acquired from the farmland in Huangshan City, China.
The compared adsorbent D201, a commercial phosphate adsorbent, was
derived from Zhejiang Zheng Guang. Co., Ltd. D201 was covalently bound
with abundant quaternary ammonium groups, i.e., −N⁺(CH₃)₃, with a BET surface area of ∼10.5
m²/g and an average pore diameter of 24.8 nm.

Li Y., Dong L., Ren X., Liu H., Zhang C, & Wan S. (2024). Remarkably Enhanced Phosphate Sequestration from Waters by Biochar with High-Density Quaternary Ammonium Groups. ACS Omega, 9(18), 20119-20128.

Publication 2024

Amino Acid and Nitrogen Balance in Pigs

Not available on PMC !

A total of 90 growing barrows (Camborough Plus × C3378; PIC Canada, Ltd., Winnipeg, MB) with an initial body weight (BW) of 20.4 ± 0.5 kg were used in an N-balance experiment at the Prairie Swine Centre, Inc. (Saskatoon, Canada) . Pigs were housed individually in metabolism crates (1.4 m × 1.5 m) in a temperature-controlled room (22 ± 1 • C) and were randomly assigned to 1 of 10 dietary treatments arranged as a 2 × 5 factorial in a randomized complete block design over nine blocks (n = 9 pigs/treatment). The factors were NPN inclusion (no ammonium phosphate (NAP) or supplemented with ammonium phosphate at 1.7% (AP)) and graded levels of standardized ileal digestible (SID) Lys content (0.8%, 0.9%, 1.0%, 1.1%, or 1.2%). The NAP diet was formulated to have an E:T ratio of 0.36 (considered to be relatively deficient in N) and the AP diet to have a ratio of 0.33 (N supplemented). While these ratios are lower than the suggested optimum in swine (Heger et al. 1998) (link), previous ratios were calculated using total AAs and only considering AA-N, ignoring the contribution of NPN (Heger et al. 1998; (link)Heger 2003) . As in our previous study (Camiré et al. 2023) (link), the E:T ratio in the current study was calculated using SID EAA-N to the requirement (NRC 2012) and total dietary N content. As such, all excess EAA-N and all other sources of N are considered as potentially contributing to N supply. Lysine was chosen as the test EAA based on our previous study (Camiré et al. 2023 (link)) and as it is generally first-limiting in diets for swine and is first limiting for lean gain. Diets were formulated to meet or exceed nutrient requirements according to NRC (2012), except for Lys, and contained titanium dioxide as an indigestible marker (Table 1). Only the diets containing the lowest and highest Lys content were milled under standard commercial conditions and then mixed in appropriate proportions to obtain the 0.9%, 1.0%, and 1.1% SID Lys diets (Canadian Feed Research Centre, North Battleford, SK, Canada). Daily feed allowance was provided at 2.8× metabolizable energy requirements for maintenance (determined as 110 × BW 0.75 ) and was adjusted to BW at the start of adaptation and collection periods. Diets were fed in two equal meals per day at 0800 and 1500 h with ad libitum access to water. Feed refusals were collected for each pig daily and weighed to determine daily feed intake.

Buchinski M.J., Wellington M.O., Camiré C.M., Panisson J.C., Shoveller A.K., & Columbus D.A. (2024). Effect of dietary nitrogen content and ammonium phosphate inclusion on lysine requirement for nitrogen retention in growing pigs. Canadian Journal of Animal Science, 104(2), 241-250.

Publication 2024

Stone Composition Analysis and Classification

This study classified stone composition into mixed stones, calcium oxalate monohydrate (COM), anhydrous uric acid (UAA), magnesium ammonium phosphate hexahydrate (MAPH), dicalcium phosphate dihydrate (DCDP), carbonate apatite (CA), L-cystine, ammonium uric acid (AUA), and other stones, based on the results of stone composition analysis. Stones with more than one component were defined as mixed components. Stones with less than 3 cases of single-component stones are known as other types of stones. Other types of calculi in this study included 2 patients with xanthine stones, 2 patients with magnesium ammonium phosphate monohydrate (MAPM) stones, 2 patients with sodium urate monohydrate stones, and 1 patient with calcite stones. Infected stones were defined as stones containing magnesium ammonium phosphate and carbonate apatite.^{[9 (link)]}

Yin K., Yin Z., Liu Z., Yao J., Wu Y, & Su S. (2024). Exploring the association between multiple factors and urolithiasis: A retrospective study and Mendelian randomization analysis. Medicine, 103(18), e37968.

Publication 2024

Inorganic Chemical Synthesis Protocol

Calcium hydroxide, ammonium dihydrogen phosphate, Calcium nitrate tetrahydrate, citric acid, and sodium hydroxide were all purchased from Sigma-Aldrich (Korea). Diammonium hydrogen phosphate was purchased from Junsei (Japan). Ammonium hydroxide and hydrochloric acid were purchased from Daejung (Korea).

Jang W.Y., Pyun J.C, & Chang J.H. (2024). Comparative In Vitro Dissolution Assessment of Calcined and Uncalcined Hydroxyapatite Using Differences in Bioresorbability and Biomineralization. International Journal of Molecular Sciences, 25(1), 621.

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Publication 2024

Top products related to «Ammonium phosphate»

Sodium hydroxide (naoh) by Merck Group

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Sodium hydroxide is a chemical compound with the formula NaOH. It is a white, odorless, crystalline solid that is highly soluble in water and is a strong base. It is commonly used in various laboratory applications as a reagent.

Methanol by Merck Group

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Methanol is a clear, colorless, and flammable liquid that is widely used in various industrial and laboratory applications. It serves as a solvent, fuel, and chemical intermediate. Methanol has a simple chemical formula of CH3OH and a boiling point of 64.7°C. It is a versatile compound that is widely used in the production of other chemicals, as well as in the fuel industry.

Hydrochloric acid (hcl) by Merck Group

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Hydrochloric acid is a commonly used laboratory reagent. It is a clear, colorless, and highly corrosive liquid with a pungent odor. Hydrochloric acid is an aqueous solution of hydrogen chloride gas.

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NaCl is a chemical compound commonly known as sodium chloride. It is a white, crystalline solid that is widely used in various industries, including pharmaceutical and laboratory settings. NaCl's core function is to serve as a basic, inorganic salt that can be used for a variety of applications in the lab environment.

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Ammonium acetate by Merck Group

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Ammonium acetate is a chemical compound with the formula CH3COONH4. It is a colorless, crystalline solid that is soluble in water and alcohol. Ammonium acetate is commonly used in various laboratory applications, such as pH adjustment, buffer preparation, and as a mobile phase component in chromatography.

Bovine serum albumin (bsa) by Merck Group

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Bovine serum albumin (BSA) is a common laboratory reagent derived from bovine blood plasma. It is a protein that serves as a stabilizer and blocking agent in various biochemical and immunological applications. BSA is widely used to maintain the activity and solubility of enzymes, proteins, and other biomolecules in experimental settings.

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PBS (Phosphate-Buffered Saline) is a widely used buffer solution in biological and medical research. It is a balanced salt solution that maintains a stable pH and osmotic pressure, making it suitable for a variety of applications. PBS is primarily used for washing, diluting, and suspending cells and biological samples.

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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.

What are the different types or variations of ammonium phosphate?

Ammonium phosphate exists in several forms, including monoammonium phosphate (MAP), diammonium phosphate (DAP), and ammonium polyphosphate. Each type has slightly different chemical properties and applications. For example, MAP is commonly used as a fertilizer, while DAP is often used in fire retardants and as a food additive. Understanding the specific characteristics of each form can help researchers select the most appropriate type for their ammonium phosphate studies.

What are the key applications of ammonium phosphate?

Ammonium phosphate has a wide range of applications, including: 1. Fertilizer: Ammonium phosphate is a primary ingredient in many commercial fertilizers, as it provides both nitrogen and phosphorus, which are essential nutrients for plant growth. 2. Fire retardant: The thermal stability and flame-retarding properties of ammonium phosphate make it a common component in fire-resistant coatings and materials. 3. Food additive: Certain forms of ammonium phosphate, such as diammonium phosphate, are approved for use as food additives to enhance acidity, act as a leavening agent, or serve as a nutritional supplement. 4. Water treatment: Ammonium phosphate can be used in the treatment of wastewater to remove phosphates and prevent eutrophication.

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More about "Ammonium phosphate"

Ammonium phosphate (NH4)3PO4 is a versatile chemical compound composed of ammonium (NH4+) and phosphate (PO4^3-) ions.
This inorganic salt is widely used in a variety of applications, including fertilizers, flame retardants, and food additives.
As a key component in plant nutrition, ammonium phosphate plays a crucial role in soil amendment, helping to enrich the soil and support plant growth.
Its fire-retardant properties also make it an essential ingredient in various safety products, contributing to fire prevention and control.
Researchers studying ammonium phosphate can leverage advanced tools like PubCompare.ai to optimize their research process.
This AI-powered platform enables researchers to easily locate relevant protocols from literature, preprints, and patents, while utilizing intelligent comparisons to identify the best protocols and products.
By enhancing reproducibility and accuracy, PubCompare.ai becomes the ultimate tool for researchers in this field.
In addition to ammonium phosphate, researchers may also encounter related compounds and chemicals such as sodium hydroxide (NaOH), methanol (CH3OH), hydrochloric acid (HCl), sodium chloride (NaCl), formic acid (HCOOH), ammonium acetate (CH3COO-NH4+), bovine serum albumin (BSA), phosphate-buffered saline (PBS), dimethyl sulfoxide (DMSO), and acetonitrile (CH3CN).
Understanding the properties and applications of these substances can further enhance the research process and provide a more comprehensive understanding of the related topics.
By incorporating these insights, researchers can optimize their ammonium phosphate studies, leveraging the power of AI-driven tools and exploring the broader context of related compounds and chemicals.
This approach ensures that their research is both informative and impactful, driving progress in the field of ammonium phosphate and related areas of study.