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> Chemicals & Drugs > Inorganic Chemical > Hydroxylamine

Hydroxylamine

Hydroxylamine is a chemical compound with the formula NH2OH.
It is a colorless, crystalline solid that is commonly used in organic synthesis, biochemistry, and as a reducing agent.
Hydroxylamine plays a key role in various biological processes, including the metabolism of certain amino acids and the production of nitric oxide.
Researchers can utilize PubCompare.ai to optimize their hydroxylamine-related studies by locating and comparing protocols from literature, preprints, and patents, ensuring reproducibility and accuracy.
This AI-driven platform enhances research by providing a comprehensive, SEO-optimized resource for hydroxylamine-focused investigations.

Most cited protocols related to «Hydroxylamine»

1
Quantitative Proteomics with Tandem Mass Tags
Cited 39 times
Protein content was measured using a BCA assay (Thermo Scientific); disulfide bonds were reduced with DTT and cysteine residues alkylated with iodoacetamide as previously described.10 (link) Protein lysates were cleaned up by methanol-chloroform precipitation and digested overnight with Lys-C (Wako) in a 1/100 enzyme/protein ratio in 4 M urea and 50 mM Tris-HCl, pH 8.8. The digest was acidified with formic acid (FA) to a pH of ~ 2–3 and subjected to C18 solid-phase extraction (SPE) (Sep-Pak, Waters).
Isobaric labeling of the peptides was accomplished with 6-plex TMT reagents (Thermo Scientific). Reagents, 0.8 mg, were dissolved in 40 μl acetonitrile (ACN), and 10 μl of the solution was added to 100 μg of peptides dissolved in 100 μl of 50 mM HEPES, pH 8.5. We found that the generation of unidentified and unwanted side reaction products – singly charged ions with m/z of 303.26, 317.26, and 331.29 – was prevented by using a 200 mM HEPES pH 8.5 buffer instead of the triethylammonium bicarbonate (TEAB) buffer recommended by the manufacturer. After 1 h at room temperature, the reaction was quenched by adding 8 μl of 5% hydroxylamine. Yeast peptides were labeled with all six reagents (126–131), human peptides were labeled with reagents 126, 127, and 128. Labeled peptides from yeast and human were separately mixed in the ratios described in the main manuscript and subjected to C18 SPE on Sep-Pak cartridges. After individual LC-MS2 analysis of both samples (Supplementary Fig. 5), they were mixed to generate the final multi-proteome digest mixture. Two samples were prepared using the ratios presented in Fig. 1: one was used to study the influence of isolation specificity and precursor ion isolation width on the interference effect (see below and main manuscript), while all other experiments used the second sample. One sample was prepared using the ratios given in Supplementary Fig. 1.
Ting L., Rad R., Gygi S.P, & Haas W. (2011). MS3 eliminates ratio distortion in isobaric labeling-based multiplexed quantitative proteomics. Nature methods, 8(11), 937-940.
Publication 2011
acetonitrile Biological Assay Buffers Chloroform Cysteine Disulfides Enzymes formic acid HEPES Homo sapiens Hydroxylamine Iodoacetamide isolation link protein Methanol M protein, multiple myeloma Peptides Proteins Proteome Solid Phase Extraction triethylammonium bicarbonate Tromethamine Urea Yeast, Dried
2
Quantitative Proteome Interference Analysis
Cited 33 times
The two-proteome interference
model was prepared as previously.14 (link),16 (link) HeLa S3 cells
were grown in suspension to 1 × 106 cells/mL. Yeast
cells were grown to an OD of 1.0. Cells were lysed in 6 M guanidiumthiocyanate,
50 mM Hepes (pH 8.5, HCl). Protein content was measured using a BCA
assay (Thermo Scientific), disulfide bonds were reduced with dithiothreitol
(DTT), and cysteine residues were alkylated with iodoacetamide as
previously described.17 (link) Protein lysates
were cleaned with methanol–chloroform precipitation.18 (link) The samples were redissolved in 6 M guanidiumthiocyanate,
50 mM Hepes pH 8.5, and diluted to 1.5 M guanidium thiocyanate, 50
mM Hepes (pH 8.5). Both lysates were digested overnight with Lys-C
(Wako) in a 1/50 enzyme/protein w/w ratio. Following digestion, the
sample was acidified with TFA to a pH < 2 and subjected to C18 solid-phase extraction (SPE, Sep-Pak, Waters).
The
TMT reagents were dissolved in 40 μL of acetonitrile, and 10
μL of the solution was added to 100 μg of peptides dissolved
in 100 μL of 50 mM HEPES (pH 8.5). After incubating for 1 h
at room temperature (22 °C), the reaction was quenched by adding
8 μL of 5% w/v hydroxylamine. Following labeling, the sample
was combined in desired ratios. Yeast aliquots were mixed at 10:4:1:1:4:10,
and HeLa was mixed at 1:1:1:0:0:0 (Figure 1A). Those two samples were then mixed at a 1/1 w/w ratio and subjected
to C18 solid-phase extraction.
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 Cells Chloroform Cysteine Digestion Disulfides Dithiothreitol Enzymes HeLa Cells HEPES Hydroxylamine Iodoacetamide link protein Methanol Peptides Proteins Proteome Saccharomyces cerevisiae Solid Phase Extraction Staphylococcal Protein A Thiocyanates
3
Tandem Mass Tag Protein Labeling
Cited 26 times
The reduced and alkylated proteins were bound to SP3 beads, washed three times with 80% ethanol and subjected to on-bead digestion overnight at 37 °C in 200 mM EPPS, pH 8.5 while shaking with Lys-C protease at a 1:100 protease-to-protein ratio. Trypsin was added to a 1:100 protease-to-protein ratio and the samples were incubated for 6 h at 37 °C while shaking. The beads were removed from the samples and anhydrous acetonitrile was added to a final concentration of around 30%. Roughly 75 μg of peptides were labeled with ~150 μg of TMT or TMTpro in the presence of ~28% acetonitrile at room temperature for 60 min. The labeled peptides were then quenched with hydroxylamine, pooled and desalted by Sep-Pak (Waters). Samples were dried, resuspended in 5% acetonitrile and 10 mM ammonium bicarbonate, pH 8 and subjected to bRPLC. Fractions were collected in a 96-well plate and combined for a total of 24 fractions (A and B set) before desalting and subsequent LC–MS/MS analysis of nonadjacent 12 fractions (A or B set).
Li J., Van Vranken J.G., Vaites L.P., Schweppe D.K., Huttlin E.L., Etienne C., Nandhikonda P., Viner R., Robitaille A.M., Thompson A.H., Kuhn K., Pike I., Bomgarden R.D., Rogers J.C., Gygi S.P, & Paulo J.A. (2020). TMTpro reagents: a set of isobaric labeling mass tags enables simultaneous proteome-wide measurements across 16 samples. Nature methods, 17(4), 399-404.
Publication 2020
acetonitrile ammonium bicarbonate Digestion Ethanol Hydroxylamine Peptide Hydrolases Peptides protease C Proteins Tandem Mass Spectrometry Trypsin
4
Quantitative Proteomics with Tandem Mass Tags
Cited 26 times
Protein content was measured using a BCA assay (Thermo Scientific); disulfide bonds were reduced with DTT and cysteine residues alkylated with iodoacetamide as previously described.10 (link) Protein lysates were cleaned up by methanol-chloroform precipitation and digested overnight with Lys-C (Wako) in a 1/100 enzyme/protein ratio in 4 M urea and 50 mM Tris-HCl, pH 8.8. The digest was acidified with formic acid (FA) to a pH of ~ 2–3 and subjected to C18 solid-phase extraction (SPE) (Sep-Pak, Waters).
Isobaric labeling of the peptides was accomplished with 6-plex TMT reagents (Thermo Scientific). Reagents, 0.8 mg, were dissolved in 40 μl acetonitrile (ACN), and 10 μl of the solution was added to 100 μg of peptides dissolved in 100 μl of 50 mM HEPES, pH 8.5. We found that the generation of unidentified and unwanted side reaction products – singly charged ions with m/z of 303.26, 317.26, and 331.29 – was prevented by using a 200 mM HEPES pH 8.5 buffer instead of the triethylammonium bicarbonate (TEAB) buffer recommended by the manufacturer. After 1 h at room temperature, the reaction was quenched by adding 8 μl of 5% hydroxylamine. Yeast peptides were labeled with all six reagents (126–131), human peptides were labeled with reagents 126, 127, and 128. Labeled peptides from yeast and human were separately mixed in the ratios described in the main manuscript and subjected to C18 SPE on Sep-Pak cartridges. After individual LC-MS2 analysis of both samples (Supplementary Fig. 5), they were mixed to generate the final multi-proteome digest mixture. Two samples were prepared using the ratios presented in Fig. 1: one was used to study the influence of isolation specificity and precursor ion isolation width on the interference effect (see below and main manuscript), while all other experiments used the second sample. One sample was prepared using the ratios given in Supplementary Fig. 1.
Ting L., Rad R., Gygi S.P, & Haas W. (2011). MS3 eliminates ratio distortion in isobaric labeling-based multiplexed quantitative proteomics. Nature methods, 8(11), 937-940.
Publication 2011
acetonitrile Biological Assay Buffers Chloroform Cysteine Disulfides Enzymes formic acid HEPES Homo sapiens Hydroxylamine Iodoacetamide isolation link protein Methanol M protein, multiple myeloma Peptides Proteins Proteome Solid Phase Extraction triethylammonium bicarbonate Tromethamine Urea Yeast, Dried
5
Quantifying Lignin in Cell Walls
Cited 25 times
Protein-free cell wall sample (20 mg) was placed into a screw-cap centrifuge tube containing 0.5 ml of 25% acetyl bromide (v/v in glacial acetic acid) and incubated at 70°C for 30 min. After complete digestion, the sample was quickly cooled in an ice bath, and then mixed with 0.9 ml of 2 M NaOH, 0.1 ml of 5 M hydroxylamine-HCl, and a volume of glacial acetic acid sufficient for complete solubilization of the lignin extract (4 ml for soybean tissues or 6 ml for sugarcane bagasse). After centrifugation (1,400×g, 5 min), the absorbance of the supernatant was measured at 280 nm [21] (link). A standard curve was generated with alkali lignin (Aldrich 37, 096-7) and the absorptivity (ε) value obtained was 22.9 g−1 L cm−1. The results were expressed as mg lignin g−1 cell wall.
Moreira-Vilar F.C., Siqueira-Soares R.D., Finger-Teixeira A., de Oliveira D.M., Ferro A.P., da Rocha G.J., Ferrarese M.D., dos Santos W.D, & Ferrarese-Filho O. (2014). The Acetyl Bromide Method Is Faster, Simpler and Presents Best Recovery of Lignin in Different Herbaceous Tissues than Klason and Thioglycolic Acid Methods. PLoS ONE, 9(10), e110000.
Publication 2014
Acetic Acid acetyl bromide Alkalies bagasse Bath Cell Wall Centrifugation Digestion Gastrin-Secreting Cells Hydroxylamine Lignin Proteins Saccharum Soybeans Tissues

Most recents protocols related to «Hydroxylamine»

1
Synthesis of 6-(3-Isoquinolyl)Spiro[Chromane-2,4'-Piperidine] Derivative
Not available on PMC !

Example 146

[Figure (not displayed)]

This compound was synthesized using CDI, O-(tetrahydro-2H-pyran-2-yl)hydroxylamine, and 6-(3-isoquinolyl)spiro[chromane-2,4′-piperidine] TFA salt. Analysis: LCMS m/z=474 (M+1); 1H NMR (400 MHz, CDCl3) δ: 9.30 (s, 1H), 8.00-7.95 (m, 2H), 7.92 (d, J=2.3 Hz, 1H), 7.88-7.82 (m, 2H), 7.68 (td, J=7.6, 1.1 Hz, 1H), 7.58-7.52 (m, 1H), 7.30 (s, 1H), 6.97 (d, J=8.5 Hz, 1H), 5.01-4.84 (m, 1H), 4.02-3.91 (m, 1H), 3.90-3.78 (m, 2H), 3.71-3.57 (m, 1H), 3.41-3.26 (m, 2H), 2.91 (t, J=6.8 Hz, 2H), 1.95-1.76 (m, 7H), 1.71-1.53 (m, 5H).

US11878982B2. Spiropiperidine derivatives (2024-01-23). 89BIO LTD [IL]. Inventors: Robert L Hudkins [US], David B. Whitman [US], Craig A. Zificsak [US], Allison L. Zulli [US], Melody McWherter [US].
Patent 2024
1H NMR Hydroxylamine Laser Capture Microdissection piperidine Pyrans Salts
2
Synthesis and Characterization of Pyrazolo-Pyridine Derivative
Not available on PMC !

Example 171

[Figure (not displayed)]

This compound was synthesized using 5-(7-methylpyrazolo[1,5-a]pyridin-6-yl)spiro[3H-benzofuran-2,4′-piperidine] 2HCl and O-(tetrahydro-2H-pyran-2-yl)hydroxylamine. Analysis: LCMS m/z=463 (M+1); 1H NMR (400 MHz, DMSO-d6) δ 9.73 (s, 1H), 8.05 (d, J=2.3 Hz, 1H), 7.64 (d, J=8.8 Hz, 1H), 7.28 (d, J=1.5 Hz, 1H), 7.21-7.11 (m, 2H), 6.87 (d, J=8.3 Hz, 1H), 6.68 (d, J=2.3 Hz, 1H), 4.76 (t, J=3.0 Hz, 1H), 4.02-3.93 (m, 1H), 3.56-3.43 (m, 3H), 3.43-3.34 (m, 2H), 3.10 (s, 2H), 2.65 (s, 3H), 1.89-1.44 (m, 10H).

US11878982B2. Spiropiperidine derivatives (2024-01-23). 89BIO LTD [IL]. Inventors: Robert L Hudkins [US], David B. Whitman [US], Craig A. Zificsak [US], Allison L. Zulli [US], Melody McWherter [US].
Patent 2024
1H NMR Benzofurans Hydroxylamine Laser Capture Microdissection piperidine Pyrans Sulfoxide, Dimethyl
3
Synthesis of Spirocyclic Chromane-Piperidine Compounds
Not available on PMC !

Example 141

[Figure (not displayed)]

This compound was synthesized using O-(tetrahydro-2H-pyran-2-yl)hydroxylamine and 6-(5-methylimidazo[1,2-a]pyridin-6-yl)-N-tetrahydropyran-2-yloxy-spiro[chromane-2,4′-piperidine]-1′-carboxamide. 6-(5-Methylimidazo[1,2-a]pyridin-6-yl)-N-tetrahydropyran-2-yloxy-spiro[chromane-2,4′-piperidine]-1′-carboxamide Analysis: LCMS m/z=477 (M+1); 1H NMR (400 MHz, CDCl3) δ: 7.94 (d, J=10.0 Hz, 1H), 7.71 (s, 1H), 7.59-7.51 (m, 2H), 7.19 (d, J=9.3 Hz, 1H), 7.10-7.02 (m, 2H), 6.91 (d, J=8.3 Hz, 1H), 5.01-4.88 (m, 1H), 4.08-3.93 (m, 1H), 3.87 (br d, J=11.8 Hz, 2H), 3.68-3.58 (m, 1H), 3.33 (br t, J=12.9 Hz, 2H), 2.89-2.71 (m, 4H), 2.56 (s, 3H), 1.96-1.75 (m, 6H), 1.74-1.49 (m, 6H). 6-(5-Methylimidazo[1,2-a]pyridin-6-yl)spiro[chromane-2,4′-piperidine]-1′-carbohydroxamic acid Analysis: LCMS m/z=393 (M+1); 1H NMR (400 MHz, DMSO-d6) δ: 9.06 (s, 1H), 7.97 (s, 1H), 7.88 (s, 1H), 7.67 (d, J=1.3 Hz, 1H), 7.51 (d, J=9.0 Hz, 1H), 7.25-7.09 (m, 3H), 6.89 (d, J=8.3 Hz, 1H), 3.65 (br d, J=13.6 Hz, 2H), 3.15 (br t, J=10.7 Hz, 2H), 2.80 (br t, J=6.8 Hz, 2H), 2.55 (s, 3H), 1.83 (br t, J=6.8 Hz, 2H), 1.70 (br d, J=13.3 Hz, 2H), 1.61-1.48 (m, 2H).

US11878982B2. Spiropiperidine derivatives (2024-01-23). 89BIO LTD [IL]. Inventors: Robert L Hudkins [US], David B. Whitman [US], Craig A. Zificsak [US], Allison L. Zulli [US], Melody McWherter [US].
Patent 2024
1H NMR Acids Hydroxylamine Lincomycin piperidine Pyrans Sulfoxide, Dimethyl
4
Synthesis of 6-(8-Chloro-7-quinolyl)-N-tetrahydropyran-2-yloxy-spiro[4H-1,3-benzodioxine-2,4′-piperidine]-1′-carboxamide
Not available on PMC !

Example 136

[Figure (not displayed)]

This compound was synthesized using 6-(8-chloro-7-quinolyl)spiro[4H-1,3-benzodioxine-2,4′-piperidine] and O-(tetrahydro-2h-pyran-2-yl)hydroxylamine. 6-(8-Chloro-7-quinolyl)-N-tetrahydropyran-2-yloxy-spiro[4H-1,3-benzodioxine-2,4′-piperidine]-1′-carboxamide (0.125 g, 0.24 mmole) in DCM (5 mL) and TFA (2 mL) was stirred 2 h and concentrated. The product was purified by Gilson chromatography (5-45% ACN in water with 0.1% TFA). The pure fractions were concentrated, freebased and dried at 50° C. under vacuum. Analysis: LCMS m/z=426 (M+1); 1H NMR (400 MHz, DMSO-d6) δ: 9.15 (s, 1H), 9.06 (dd, J=4.1, 1.6 Hz, 1H), 8.49 (dd, J=8.3, 1.5 Hz, 1H), 8.09-7.99 (m, J=8.8 Hz, 2H), 7.67 (dd, J=8.3, 4.3 Hz, 1H), 7.62 (d, J=8.5 Hz, 1H), 7.40 (dd, J=8.4, 2.1 Hz, 1H), 7.31 (d, J=2.0 Hz, 1H), 7.00 (d, J=8.5 Hz, 1H), 4.95 (s, 2H), 3.51-3.35 (m, 4H), 1.93-1.80 (m, 4H).

US11878982B2. Spiropiperidine derivatives (2024-01-23). 89BIO LTD [IL]. Inventors: Robert L Hudkins [US], David B. Whitman [US], Craig A. Zificsak [US], Allison L. Zulli [US], Melody McWherter [US].
Patent 2024
1H NMR Acids Chromatography Hydroxylamine Lincomycin piperidine Pyrans Sulfoxide, Dimethyl Vacuum
5
Synthesis of Quinoline-Benzofuran Compound
Not available on PMC !

Example 168

[Figure (not displayed)]

This compound was synthesized using 5-(8-methoxy-7-quinolyl)spiro[3H-benzofuran-2,4′-piperidine] 2HCl and O-(tetrahydro-2H-pyran-2-yl)hydroxylamine. Analysis: LCMS m/z=490 (M+1); 1H NMR (400 MHz, DMSO-d6) δ: 9.73 (s, 1H), 8.94 (dd, J=4.3, 1.8 Hz, 1H), 8.38 (dd, J=8.3, 1.8 Hz, 1H), 7.75 (d, J=8.5 Hz, 1H), 7.57 (d, J=8.3 Hz, 1H), 7.54 (dd, J=8.3, 4.3 Hz, 1H), 7.47 (d, J=1.5 Hz, 1H), 7.38 (dd, J=8.3, 1.8 Hz, 1H), 6.88 (d, J=8.3 Hz, 1H), 4.76 (t, J=3.1 Hz, 1H), 4.02-3.95 (m, 1H), 3.91 (s, 3H), 3.53-3.44 (m, 3H), 3.43-3.34 (m, 2H), 3.12 (s, 2H), 1.89-1.43 (m, 10H).

US11878982B2. Spiropiperidine derivatives (2024-01-23). 89BIO LTD [IL]. Inventors: Robert L Hudkins [US], David B. Whitman [US], Craig A. Zificsak [US], Allison L. Zulli [US], Melody McWherter [US].
Patent 2024
1H NMR Benzofurans Hydroxylamine Laser Capture Microdissection piperidine Pyrans Sulfoxide, Dimethyl

Top products related to «Hydroxylamine»

1
Hydroxylamine by Merck Group
Sourced in United States, Germany, United Kingdom
Hydroxylamine is a chemical compound with the formula NH2OH. It is a colorless, crystalline solid that is commonly used as a laboratory reagent. Hydroxylamine is a reducing agent and can be used in various chemical reactions and analyses.
2
Tmt reagent by Thermo Fisher Scientific
Sourced in United States
The TMT reagent is a set of isobaric labeling reagents used for quantitative proteomics analysis. The reagents are designed to covalently tag peptides, allowing for the simultaneous identification and relative quantification of proteins across multiple samples.
3
Sep pak by Waters Corporation
Sourced in United States, Ireland
Sep-Pak is a solid-phase extraction (SPE) device produced by Waters Corporation. It is designed to extract, purify, and concentrate analytes from liquid samples prior to analysis. The Sep-Pak device contains a sorbent material, which selectively retains the target analytes, allowing for the removal of unwanted matrix components. This process helps to improve the sensitivity and accuracy of subsequent analytical techniques.
4
Tmt 10 plex reagent by Thermo Fisher Scientific
Sourced in United States, United Kingdom
The TMT 10-plex reagents are a set of isobaric labeling reagents designed for quantitative proteomic analysis. The reagents enable the simultaneous identification and quantification of proteins across 10 different samples in a single mass spectrometry experiment.
5
Trypsin by Promega
Sourced in United States, Germany, United Kingdom, China, Japan, France, Switzerland, Sweden, Italy, Netherlands, Spain, Canada, Brazil, Australia, Macao
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.
6
Iodoacetamide by Merck Group
Sourced in United States, Germany, United Kingdom, Sao Tome and Principe, Italy, France, Macao, China, Canada, Australia, Switzerland, Spain
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.
7
Hydroxylamine by Thermo Fisher Scientific
Sourced in United States
Hydroxylamine is a chemical compound used in various laboratory applications. It functions as a reducing agent and can be used in the synthesis of other chemicals. Hydroxylamine is commonly employed in analytical chemistry, organic synthesis, and biochemistry.
8
T sod assay kit by Nanjing Jiancheng
Sourced in China
The T-SOD assay kit is a laboratory equipment product designed to measure the activity of Superoxide Dismutase (SOD) enzyme in biological samples. The kit provides the necessary reagents and protocols to quantify SOD levels using a colorimetric or spectrophotometric method.
9
Tmt10plex by Thermo Fisher Scientific
Sourced in United States
The TMT10plex is a multiplexed isobaric mass tagging reagent system developed by Thermo Fisher Scientific. It allows for the simultaneous quantification of up to 10 different protein samples in a single mass spectrometry experiment. The core function of the TMT10plex is to enable comparative proteomic analysis across multiple biological conditions.
10
Sodium hydroxide (naoh) by Merck Group
Sourced in Germany, United States, India, United Kingdom, Italy, China, Spain, France, Australia, Canada, Poland, Switzerland, Singapore, Belgium, Sao Tome and Principe, Ireland, Sweden, Brazil, Israel, Mexico, Macao, Chile, Japan, Hungary, Malaysia, Denmark, Portugal, Indonesia, Netherlands, Czechia, Finland, Austria, Romania, Pakistan, Cameroon, Egypt, Greece, Bulgaria, Norway, Colombia, New Zealand, Lithuania
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.

More about "Hydroxylamine"

Hydroxylamine is a versatile chemical compound with the formula NH2OH.
This colorless, crystalline solid is widely used in organic synthesis, biochemistry, and as a reducing agent.
It plays a crucial role in various biological processes, including the metabolism of certain amino acids and the production of nitric oxide.
Researchers can leverage the power of PubCompare.ai to optimize their hydroxylamine-related studies.
This AI-driven platform enables users to locate and compare protocols from literature, preprints, and patents, ensuring reproducibility and accuracy.
By utilizing this comprehensive, SEO-optimized resource, researchers can enhance their investigations on hydroxylamine and related topics.
Hydroxylamine is closely associated with other important compounds and techniques, such as TMT reagent, Sep-Pak, TMT 10-plex reagents, Trypsin, Iodoacetamide, T-SOD assay kit, TMT10plex, and Sodium hydroxide.
These tools and reagents are often employed in conjunction with hydroxylamine-based research, providing researchers with a robust set of resources to explore the diverse applications and nuances of this remarkable chemical.
Whether you're studying the metabolic pathways involving hydroxylamine, investigating its role in nitric oxide production, or exploring its synthetic applications, PubCompare.ai can be a valuable asset in your research endeavors.
Unlock the full potential of your hydroxylamine-focused studies and take advantage of the insights and resources available through this innovative AI platform.