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Azides

Azides are a class of chemical compounds containing the azido group (-N3).
They are widely used in various research fields, including organic synthesis, materials science, and biomedical applications.
Azides exhibit unique reactivity, such as the azide-alkyne cycloaddition reaction, making them valuable for the development of novel compounds and materials.
Researchers can leverage PubCompare.ai, an AI-driven platform, to enhance the reproducibility and accuracy of their Azides research.
The platform helps locate protocols from literature, pre-prits, and patents, and provides AI-driven comparisons to identify the best protocols and products for their experiments.
This streamlines the research process and improves results, leading to more efficient and effective Azides studies.

Most cited protocols related to «Azides»

1
In Vitro Synthesis of COX-2 Inhibitors
To investigate the COX-2 isozyme templated synthesis, each 5-azido-pyraozle (5, 14, 27, and 31, 1 µl of 3 mM DMSO solution) and alkyne (6a–6f, 15a–15e, 1 µl of 20 mM DMSO solution) were pairwise mixed with human recombinant COX-2 isozyme (95 µl COX-2) in 1 µl of 1 M Tris-HCl, pH 8.0. The each reaction mixture was vortexed for 1 min, and then incubated at room temperature (For temperature dependency of COX-2 enzyme activity, see Supplementary Fig. 16). Final reagent concentrations were as follows: COX-2 (7 µM), azide (30 µM) alkyne (200 µM). After 3, 6, 9, 12, 15, 18, 21, and 24 h each sample was analyzed in triplicate by injecting (10 µl) into the LC/MS instrument with SIM mode (Water’s Micromass ZQTM 4000 LC−MS instrument, operating in the ESI-positive mode, equipped with a Water’s 2795 separation module). Calibration curve for hit compounds 18 and 21 is given in Supplementary Fig. 17. Summaries of all LC/MS data are presented in Supplementary Tables 3–7. Separations were performed in triplicate using a Kromasil 100-5-C18 (100 μm pore size, 5 μm particle size) reverse phase column (2.1 mm diameter × 50 mm length), preceded by a Kromasil 100-5-C18 2.1 × guard column. Separations were effected using a gradient MeCN/H2O (0.05% trifluoroacetic acid (TFA))/MeOH in 40/30/30, v/v/v over 15 min at flow rate 0.25 ml min−1. Operating parameters were as follows: capillary voltage = 3.5 kV; cone voltage = 20 V; source temperature = 140 °C; sesolvation temperature = 250 °C; cone nitrogen gas flow = 100 l h−1; desolvation nitrogen gas flow = 550 l h−1. The identities of triazole products (retention time of 6.73 min for 18), (retention time of 4.56 min for 21), and the internal standard (retention time of 10.89 min) were confirmed by molecular weight and comparison of the retention times of the authentic products formed from copper catalyzed reactions. Control experiments in the presence of BSA (1 mg mL−1) instead of the COX-2 enzyme as well as in the absence of COX-2 enzyme and the known COX-2 selective inhibitor (1 µl of celecoxib, 100 µM final concentration) were run as described above. For multicomponent in situ click chemistry reactions, each azide (5, 14, 27, and 31, 1 µL of 3 mM DMSO solution) and eleven alkynes (6a–6f and 15a–15e, 1 µl of 20 mM DMSO solution) were thoroughly mixed together in the presence of COX-2 isozyme (95 µl COX-2) in 1 µl of 1 M Tris-HCl, pH 8.0 and incubated at room temperature. After 24 h each sample was analyzed in triplicate by injecting (10 µl) into the LC/MS instrument by following the procedure described above, except the ions are monitored for all possible masses. The cyclo addition products were identified by their molecular weights and by comparison of the retention times of authentic products prepared through Cu-catalyzed reactions. Control experiments using BSA (1 mg ml−1) in place of COX-2 isozyme and in the absence of COX-2 isozyme were run consecutively.
Bhardwaj A., Kaur J., Wuest M, & Wuest F. (2017). In situ click chemistry generation of cyclooxygenase-2 inhibitors. Nature Communications, 8, 1.
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Publication 2017
Alkynes Anabolism Azides Capillaries Celecoxib compound 18 Copper Cyclooxygenase 2 Inhibitors enzyme activity Enzymes Homo sapiens Ions Isoenzymes Nitrogen PTGS2 protein, human Retention (Psychology) Retinal Cone Sulfoxide, Dimethyl Triazoles Trifluoroacetic Acid Tromethamine
2
Enhancing Molecular Property Prediction
Next, we discuss further extensions
and optimizations to improve performance. Although an MPNN should
ideally be able to extract any information about
a molecule that might be relevant to predicting a given property,
two limitations may prevent this in practice. First, many property
prediction data sets are very small, i.e., on the order of only hundreds
or thousands of molecules. With so little data, MPNNs are unable to
learn to identify and extract all features of a molecule that might
be relevant to property prediction, and they are susceptible to overfitting
to artifacts in the data. Second, most MPNNs use fewer message passing
steps than the diameter of the molecular graph, i.e., T < diam(G), meaning atoms that
are a distance of greater than T bonds apart will
never receive messages about each other. This results in a molecular
representation that is fundamentally local rather than global in nature,
meaning the MPNN may struggle to predict properties that depend heavily
on global features.
In order to counter these limitations, we
introduce a variant of the D-MPNN that incorporates 200 global molecular
features that can be computed rapidly in silico using
RDKit. The neural network architecture requires that the features
are appropriately scaled to prevent features with large ranges dominating
smaller ranged features, as well as preventing issues where features
in the training set are not drawn from the same sample distribution
as features in the testing set. To prevent these issues, a large sample
of molecules was used to fit cumulative density functions (CDFs) to
all features. CDFs were used as opposed to simpler scaling algorithms
mainly because CDFs have the useful property that each value has the
same meaning: the percentage of the population observed below the
raw feature value. Min-max scaling can be easily biased with outliers,
and Z-score scaling assumes a normal distribution which is most often
not the case for chemical features, especially if they are based on
counts.
The CDFs were fit to a sample of 100k compounds from
the Novartis
internal catalog using the distributions available in the scikit-learn
package,45 a sample of which can be seen
in Figure 2. One could
do a similar normalization using publicly available databases such
as ZINC46 (link) and PubChem.47 (link) scikit-learn was used primarily due to the simplicity of
fitting and the final application. However, more complicated techniques
could be used in the future to fit to empirical CDFs, such as finding
the best fit general logistic function, which has been shown to be
successful for other biological data sets.48 (link) No review was taken to remove odd distributions. For example, azides
are hazardous and rarely used outside of a few specific reactions,
as reflected in the fr_azide distribution in Figure 2. As such, since the sample data was primarily
used for chemical screening against biological targets, the distribution
used here may not accurately reflect the distribution of reagents
used for chemical synthesis. For the full list of calculated features,
please refer to the Supporting Information.
To incorporate these features, we modify the readout phase of the
D-MPNN to apply the feed-forward neural network f to the concatenation of the learned molecule feature vector h and the computed global features hf This
is a very general method of incorporating
external information and can be used with any MPNN and any computed
features or descriptors.
Yang K., Swanson K., Jin W., Coley C., Eiden P., Gao H., Guzman-Perez A., Hopper T., Kelley B., Mathea M., Palmer A., Settels V., Jaakkola T., Jensen K, & Barzilay R. (2019). Analyzing Learned Molecular Representations for Property Prediction. Journal of Chemical Information and Modeling, 59(8), 3370-3388.
Publication 2019
Azides Biopharmaceuticals Cloning Vectors
3
Mass Cytometry Immunophenotyping of Stimulated Cells

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Publication 2012
Amines Antibodies Azides Brefeldin A Buffers Cells Combined Antibody Therapeutics Cross Reactions Edetic Acid Electron Microscopy Endotoxins Enzyme-Linked Immunosorbent Assay Erythrocytes Fetal Bovine Serum Ficoll Homo sapiens Immunoglobulins Indium-115 indium trichloride Ionomycin Iridium Isotopes LAMP2 protein, human Ligands Magnetic Fields Metals Molar Monensin Muromonab-CD3 Mus paraform Protoplasm Pulse Rate Receptors, Antigen, B-Cell Sodium Azide stains-all Sulfhydryl Compounds TAPI-2 Tetrameres tetraxetan Vision
4
Flow Cytometry Analysis of THP-1 Cells
THP-1 cells were plated in 24-well tissue culture treated plates (Costar) as described above. Cells were removed from the well using TrypLE (Invitrogen) incubation for 10 min at 37°C. Cells were collected on ice and all subsequent steps were performed at 4°C. Cells were pelleted and resuspended in FACS buffer (0.1% azide, 2% fetal calf serum in PBS) containing 11 μg/mL IgG (Jackson). Cells were then stained with PerCP/Cy5.5 anti-mouse/human CD11b antibody (Biolegend, #101227) and eFluor 450 anti-human CD14 antibody (eBioscience, CD14 eFlour 450) before fixation in 2% (w/v) paraformaldehyde (PFA) and analyzed using flow cytometry. Analysis was done using FlowJo software (TreeStar, Inc. vX.0.7 and v9.5.2).
Starr T., Bauler T.J., Malik-Kale P, & Steele-Mortimer O. (2018). The phorbol 12-myristate-13-acetate differentiation protocol is critical to the interaction of THP-1 macrophages with Salmonella Typhimurium. PLoS ONE, 13(3), e0193601.
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Publication 2018
Antibodies, Anti-Idiotypic Azides Buffers Cells CY5.5 cyanine dye Fetal Bovine Serum Flow Cytometry Homo sapiens ITGAM protein, human Mus paraform THP-1 Cells Tissues
5
Purification of BG505 SOSIP.664 HIV-1 Env Trimer
The crystallized HIV-1-Env construct from strain BG505 was generated following published reports10 (link),15 (link),16 (link), using BG505 genbank accession numbers ABA61516 and DQ20845846 (link); including the “SOS” mutations (A501C, T605C), the isoleucine to proline mutation at residue 559 (I559P), and the glycan site at residue 332 (T332N); mutating the cleavage site to 6R (REKR to RRRRRR); and truncating the C terminus to residue 664 (all HIV-1 Env numbering according to the HX nomenclature). This construct is referred to as BG505 SOSIP.664 throughout this entire manuscript.
The BG505 SOSIP.664 construct was co-transfected with furin in HEK 293 GnTI−/− cells using 600 μg of BG505 SOSIP.664 and 150 μg of furin plasmid DNAs as described previously16 (link). Transfection supernatants were harvested after 7 days, and passed over either a 2G12 antibody- or VRC01 antibody-affinity column. After washing with phosphate-buffered saline (PBS), bound proteins were eluted with 3M MgCl2, 10 mM Tris pH 8.0. The eluate was concentrated to less than 5 ml with Centricon-70 and applied to a Superdex 200 column, equilibrated in 5 mM HEPES, pH 7.5, 150 mM NaCl, 0.02% azide. The peak corresponding to trimeric HIV-1 Env was identified, pooled, concentrated and used immediately or flash-frozen in liquid nitrogen and stored at −80° C.
Pancera M., Zhou T., Druz A., Georgiev I.S., Soto C., Gorman J., Huang J., Acharya P., Chuang G.Y., Ofek G., Stewart-Jones G.B., Stuckey J., Bailer R.T., Joyce M.G., Louder M.K., Tumba N., Yang Y., Zhang B., Cohen M.S., Haynes B.F., Mascola J.R., Morris L., Munro J.B., Blanchard S.C., Mothes W., Connors M, & Kwong P.D. (2014). Structure and immune recognition of trimeric prefusion HIV-1 Env. Nature, 514(7523), 455-461.
Publication 2014
Antibodies Antibody Affinity Azides Cytokinesis DNA Freezing FURIN protein, human HEK293 Cells HEPES HIV-1 Isoleucine Magnesium Chloride MLL protein, human Mutation Nitrogen Phosphates Plasmids Polysaccharides Proline Proteins Saline Solution Sodium Chloride Strains Transfection Tromethamine

Most recents protocols related to «Azides»

1
Targeted Peptide-Nanoparticle Coupling
Not available on PMC !

Example 20

Coupling of the ligand to the nanoparticle may be achieved uniquely by following an inclusion compound protocol with β-cyclodextrin (β-CD) on the particle spontaneously interacting with adamantane on the peptide or small molecule ligand to form an inclusion complex. Briefly, cyclodextrin-PEG-DSPE derivative will be synthesized via mono-6-deoxy-6-amino-β-cyclodextrin. One of the seven primary hydroxyl groups of β-cyclodextrin will be tosylated using p-toluenesulfonyl chloride. Substitution of the tosyl group by azide and subsequent reduction with triphenylphosphine will yield mono-6-deoxy-6-amino-β-cyclodextrin. Carboxyl-activated PEG-DSPE will be conjugated to mono-6-deoxy-6-amino-β-cyclodextrin to produce cyclodextrin-PEG-DSPE. Adamantane-amine will be directly conjugated through a short spacer in the solid phase peptide synthesis to the carboxyl end of the peptide to produce adamantane-peptide/ligand. The simple room temperature mixing of adamantane-amine and β-cyclodextrin bearing nanoparticle will produce peptide coupled targeted nanoparticle.

US11872313B2. Prodrug compositions, prodrug nanoparticles, and methods of use thereof (2024-01-16). Washington University [US]. Inventors: Gregory M. Lanza [US], Dipanjan Pan [US].
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Patent 2024
4-toluenesulfonyl chloride Adamantane Amines Azides Cyclodextrins Hydroxyl Radical Ligands oxytocin, 1-desamino-(O-Et-Tyr)(2)- Peptides polyethylene glycol-distearoylphosphatidylethanolamine triphenylphosphine
2
Synthesis of Alkenyl β-Lactam Antibiotic-Cannabinoid Conjugates
Not available on PMC !

Example 32

Monobactam alkenyl aminal, alkenyl carbamate, alkenyl thiocarbamate, and alkenyl isourea linked β-lactam antibiotic cannabinoid conjugate components are synthesized as shown in the Scheme below. The starting material [410524-32-2] is reduced to the alcohol intermediate. This alcohol is then converted to the iodide using known (Tetrahedron, 73(29), 4150-4159; 2017) conditions. The iodide intermediate is converted to the primary amine using the two step azide addition/reduction protocol described above for synthesis of propenylamine cephem β-lactam antibiotic cannabinoid conjugate components. This amine is then reacted and connected to a cannabinoid by any of the aforementioned links, using the previously described chemistry and conditions associated with the non-alkenyl variant.

[Figure (not displayed)]

US11877988B2. Conjugate molecules (2024-01-23). Diverse Biotech, Inc. [US]. Inventors: Paul Hershberger [US], Philip Arlen [US].
Full text: Click here
Patent 2024
Amines Anabolism Azides Cannabinoids Carbamates Ethanol Iodides Monobactams Thiocarbamates
3
Azide-Alkyne Click Conjugation of Polymer and DNA Oligo
Not available on PMC !

Example 47

Azide Polymer Synthesis for Click Conjugation to Alkyne Terminated DNA Oligo

A solution of azidohexanoic acid NHS ester (2.5 mg) in anhydrous DMF (100 μL) was added to a solution of the amine-functional polymer (9.9 mg) in anhydrous DMF (100 μL) under argon. Diisopropylethylamine (2 μL) was then added. The reaction was agitated at room temperature for 15 hours. Water was then added (0.8 mL) and the azide-modified polymer was purified over a NAP-10 column. The eluent was freeze dried overnight. Yield 9.4 mg, 95%.

Oligo Synthesis with Pendant Alkyne (Hexyne) for Click Conjugation to Azide Polymer

The 3′ propanol oligo A8885 (sequence YATTTTACCCTCTGAAGGCTCCP, where Y=hexynyl group and P=propanol group) was synthesized using 3′ spacer SynBase™ CPG 1000 column on an Applied Biosystems 394 automated DNA/RNA synthesizer. A standard 1.0 mole phosphoramidite cycle of acid-catalyzed detritylation, coupling, capping and iodine oxidation was used. The coupling time for the standards monomers was 40 s, and the coupling time for the 5′ alkyne monomer was 10 min.

The oligo was cleaved from the solid support and deprotected by exposure to concentrated aqueous ammonia for 60 min at room temperature, followed by heating in a sealed tube for 5 h at 55° C. The oligo was then purified by RP-HPLC under standard conditions. Yield 34 OD.

Solution Phase Click Conjugation: Probe Synthesis

A solution of degassed copper sulphate pentahydrate (0.063 mg) in aqueous sodium chloride (0.2 M, 2.5 μL) was added to a degassed solution of tris-benzo triazole ligand (0.5 mg) and sodium ascorbate (0.5 mg) in aqueous sodium chloride (0.2 M, 12.5 μL). Subsequently, a degassed solution of oligo A8885 (50 nmole) in aqueous sodium chloride (0.2 M, 30 μL) and a degassed solution of azide polymer (4.5 mg) in anhydrous DMF (50 μL) were added, respectively. The reaction was degassed once more with argon for 30 s prior to sealing the tube and incubating at 55° C. for 2 h. Water (0.9 mL) was then added and the modified oligo was purified over a NAP-10 column. The eluent was freeze-dried overnight. The conjugate was isolated as a distinct band using PAGE purification and characterized by mass spectrometry. Yield estimated at 10-20%.

Fluorescence Studies

The oligo-polymer conjugate was used as a probe in fluorescence studies. The probe was hybridized with the target A8090 (sequence GGAGCCTTCAGAGGGTAAAAT-Dabcyl), which was labeled with dabcyl at the 3′ end to act as a fluorescence quencher. The target and probe were hybridized, and fluorescence monitored in a Peltier-controlled variable temperature fluorimeter. The fluorescence was scanned every 5° C. over a temperature range of 30° C. to 80° C. at a rate of 2° C./min. FIG. 25 shows increasing fluorescence intensity or emission with increasing temperature, indicating that as the probe-target pair melt, the polymer and quencher separate and fluorescence is recovered.

Polymer conjugation to nucleic acids can also be performed using methods adapted from the protocols described in Examples 14, 45 and 46.

US11874278B2. Reagents for directed biomarker signal amplification (2024-01-16). SIRIGEN II LIMITED [GB]. Inventors: Brent S. Gaylord [US], Glenn P. Bartholomew [US], Russell A. Baldocchi [US], Janice W. Hong [US], William H. Huisman [US], Yongchao Liang [US], Trung Nguyen [US], Lan T. Tran [US], Jean M. Wheeler [US], Adrian Charles Vernon Palmer [GB], Frank Peter Uckert [US].
Full text: Click here
Patent 2024
4-(4-dimethylaminophenylazo)benzoic acid Acids Alkynes Amines Ammonia Anabolism Argon Azides DNA Replication Esters Fluorescence Freezing High-Performance Liquid Chromatographies Iodine Ligands Mass Spectrometry Moles Nucleic Acids Oligonucleotides phosphoramidite Polymers Propanols Sodium Ascorbate Sodium Chloride Spacer DNA Sulfate, Copper Triazoles Tromethamine
4
Optimizing Targeted Molecular Probe Avidity
Not available on PMC !

Example 14

Eight NH2—PEGn-RGD peptides containing spacers of various PEG lengths (n=2, 4, 6, 8, 10, 12, 14, 16) will be prepared by adding the corresponding Boc-PEGn-NHS to RGD in a PBS buffer (pH=8.2), followed by Boc deprotection. Photo-ODIBO-NHS, prepared using previously reported procedures, will then be mixed with the prepared NH2—PEGn-RGD in a PBS buffer (pH=8.2) to produce photo-OIDBO-PEGn-RGD. N3-PEG4-cetuximab will be prepared using previously reported procedures. N3—PEG4-cetuximab and the eight photo-ODIBO-PEGn-RGD peptides (n=2, 4, 6, 8, 10, 12, 14, 16) will be used for in vitro screening (at 4° C. to minimize the internalization of targeting probes). As shown in FIG. 11: 1): eight mixed-ligands stock solutions will be prepared by mixing N3-PEG4-cetuximab with one of the eight photo-OIDBO-PEGn-RGD peptides; 2) U87MG cells will be cultured in a 96-well plate; 3) one of the above eight mixed-ligands stock solution will be added into each well (eight wells in total) pre-seeded with U87MG; 2) after the ligands bind to the targeted receptors, the excess (unbound) targeting ligands will be washed off using a PBS buffer (repeated 5 times to ensure complete removal); 3) a UV lamp (365 nm) will be applied to deprotect the azide-inactive photo-ODIBO and generate azide-active “ODIBO”, subsequently triggering ligation between the N3-PEG4-cetuximab and ODIBO-PEGn-RGD; 4) after being incubated for an additional 2 h, 64Cu-labeled N3—NOTA will be added to click with the “excess” ODIBO-PEGn-RGD (that binds to cells, but does not click to N3-PEG4-cetuximab); and 5) the excess N3-(64Cu)NOTA will be removed, and the N3-(64Cu)NOTA clicked to “excess” ODIBO-PEGn-RGD will be measured on MicroBeta2 Plate Counter. One group without UV irradiation will be used as a negative control to get counts from the non-specific binding of N3-(64Cu)NOTA. After subtracting the non-specific binding, the specific binding of N3-(64Cu)NOTA obtained from the eight ODIBO-PEGn-RGD (n=2, 4, 6, 8, 10, 12, 14, 16) will be compared. The well with the lowest specific binding will contain the highest amount of clicking product (between cetuximab-PEG4-N3 and ODIBO-PEGn-RGD), thus the corresponding spacer will be the most potent.

The ODIBO-PEGn-RGD containing the most potent PEG spacer will click with Tz-NOTA-N3 and then be radiolabeled with 64Cu, and the resulting Tz-(64Cu)NOTA-PEGn-RGD will be used for the in vitro avidity studies on U87MG cells. Tz-(64Cu)NOTA-RGD (without a PEG spacer) will be used as a negative control because the distance between RGD and cetuximab in the resulting heterodimer is too short to achieve avidity effect (proved in preliminary study, FIG. 5B). Briefly, Tz-(64Cu)NOTA-PEGn-RGD/TCO-PEG4-cetuximab ligation product (cetuximab-PEG4-(64Cu)NOTA-PEGn-RGD) will be used for cell uptake/efflux, binding affinity and Bmax measurements on U87MG cells. After high avidity effect is confirmed on the above ligation product, in vivo evaluation will be performed then. Mice bearing U87MG xenografts will be pre-injected with 100 μg of TCOPEG4-cetuximab, and 24 h later, ˜250-350 pCi of Tz-(64Cu)NOTA-PEGn-RGD (or Tz-(64Cu)NOTA-RGD in the negative control group) will be injected. Then 1 h dynamic PET scans will be performed at multiple time points (p.i., 4, 18, and/or 28 h). As cetuximab is cleared through the liver, kinetics on tumor and liver at mid and late time points can be evaluated. At mid/late time points (4, 18, 28 h) when most of the un-ligated Tz-(64Cu)NOTAPEGn-RGD has been washed off, observation of relatively slower tumor washing out and faster liver clearing (compared to that from Tz-(64Cu)NOTA-RGD) can indicate the much stronger binding with tumor cells, and thus an avidity effect of in vivo ligation product (cetuximab-PEG2-(64Cu)NOTA-PEGn-RGD) is being achieved.

Various references are cited in this document, which are hereby incorporated by reference in their entireties herein.

US11857648B2. Dimerization strategies and compounds for molecular imaging and/or radioimmunotherapy (2024-01-02). UNIVERSITY OF PITTSBURGH—OF THE COMMONWEALTH SYSTEM OF HIGHER EDUCATION [US]. Inventors: Dexing Zeng [US], Lingyi Sun [US], Yongkang Gai [US].
Full text: Click here
Patent 2024
1,4,7-triazacyclononane-N,N',N''-triacetic acid Azides Buffers Cells Cetuximab Heterografts Kinetics Ligands Ligation Liver Mus Neoplasms Peptides Positron-Emission Tomography Ultraviolet Rays
5
Hydrogenation of Azide Compound with Pd/C
Not available on PMC !

Example 25

[Figure (not displayed)]

Dry Pd/C (10 wt %, 300 mg) and azide compound 16 (3.33 g, 6.61 mmol) were added to pentafluorophenyl ester 23 in EtOAc. The reaction mixture was stirred under hydrogen atmosphere for 27 h, and then filtered through a plug of Celite, with washing of the filter pad with EtOAc. The combined organic portions were concentrated and purified by column chromatography with a gradient of 0-5% methanol in EtOAc to deliver compound 30 (3.90 g, 86% yield). MS ESI m/z calcd for C32H59N4O5SSi [M+H]+ 639.39, found 639.39.

US11873281B2. Conjugates of cell binding molecules with cytotoxic agents (2024-01-16). HANGZHOU DAC BIOTECH CO., LTD. [CN], None [US], None [CN], None [CN]. Inventors: R. Yongxin Zhao [US], Yue Zhang [CN], Yourang Ma [CN].
Full text: Click here
Patent 2024
Anabolism Atmosphere Azides Celite Chromatography compound 30 Esters Hydrogen Methanol

Top products related to «Azides»

1
5 ethynyl 2 deoxyuridine (edu) by Thermo Fisher Scientific
Sourced in United States, United Kingdom, Germany, Japan
EdU is a synthetic nucleoside analog of thymidine that can be incorporated into the DNA of dividing cells during the S phase of the cell cycle. It can be used to detect and quantify cell proliferation in various cell culture and tissue samples.
2
Click it edu imaging kit by Thermo Fisher Scientific
Sourced in United States, Germany, United Kingdom, France
The Click-iT EdU Imaging Kit is a tool designed for the detection and visualization of DNA synthesis in proliferating cells. It utilizes a chemical labeling technique to incorporate the nucleoside analog EdU (5-ethynyl-2'-deoxyuridine) into newly synthesized DNA, which can then be detected using a fluorescent azide dye. This kit provides the necessary reagents and protocols for this process.
3
Click it cell reaction buffer kit by Thermo Fisher Scientific
Sourced in United States, Germany
The Click-iT Cell Reaction Buffer Kit is a laboratory tool designed to facilitate the detection and analysis of cellular processes. It provides the necessary components to perform click chemistry reactions within cells, enabling the labeling and visualization of specific biomolecules or cellular events.
4
Click it nascent rna capture kit by Thermo Fisher Scientific
Sourced in United States
The Click-iT Nascent RNA Capture Kit is a tool designed for the labeling and identification of newly synthesized RNA in cells. The kit utilizes a modified nucleoside analog, which is incorporated into the RNA during transcription, enabling the subsequent capture and isolation of the labeled RNA for further analysis.
5
Alexa fluor 488 azide by Thermo Fisher Scientific
Sourced in United States
Alexa Fluor 488 azide is a fluorescent dye used in various biological applications. It is a bright, photostable dye that emits green fluorescence when excited at the appropriate wavelength. The azide group on the dye allows for covalent attachment to biomolecules through click chemistry reactions.
6
Facscalibur by BD
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The FACSCalibur is a flow cytometry system designed for multi-parameter analysis of cells and other particles. It features a blue (488 nm) and a red (635 nm) laser for excitation of fluorescent dyes. The instrument is capable of detecting forward scatter, side scatter, and up to four fluorescent parameters simultaneously.
7
Alexa fluor 647 azide by Thermo Fisher Scientific
Sourced in United States
Alexa Fluor 647 azide is a fluorescent dye used in various laboratory applications. It is a bright, photostable dye with a red-orange fluorescence emission. The azide functional group allows for conjugation to biomolecules through click chemistry reactions.
8
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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Triton x 100 by Merck Group
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Triton X-100 is a non-ionic surfactant commonly used in various laboratory applications. It functions as a detergent and solubilizing agent, facilitating the solubilization and extraction of proteins and other biomolecules from biological samples.
10
Hoechst 33342 by Thermo Fisher Scientific
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Hoechst 33342 is a fluorescent dye that binds to DNA. It is commonly used in various applications, such as cell staining and flow cytometry, to identify and analyze cell populations.

More about "Azides"

Azido compounds, azido group, organic azides, nitrogen-based compounds, click chemistry, Huisgen cycloaddition, bioconjugation, biomolecular labeling, fluorescent probes, bioorthogonal reactions, EdU (5-ethynyl-2'-deoxyuridine), Click-iT EdU Imaging Kit, Click-iT Cell Reaction Buffer Kit, Click-iT Nascent RNA Capture Kit, Alexa Fluor 488 azide, FACSCalibur flow cytometer, Alexa Fluor 647 azide, Bovine serum albumin (BSA), Triton X-100, Hoechst 33342 nuclear stain.
Azides are a versatile class of chemical compounds containing the azido group (-N3), widely used in organic synthesis, materials science, and biomedical applications.
They exhibit unique reactivity, such as the azide-alkyne cycloaddition (also known as 'click chemistry'), making them valuable for developing novel compounds and materials.
Researchers can leverage AI-driven platforms like PubCompaer.ai to enhance the reproducibility and accuracy of their azides research by locating protocols from literature, pre-prints, and patents, and comparing them to identify the best approaches for their experiments.
This streamlines the research process and improves results, leading to more efficient and effective azides studies.