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Guanidine

Guanidine is a chemical compound with the formula CH₅N₃, consisting of a carbon atom bonded to three nitrogen atoms.
It is a colorless, crystalline solid that is highly soluble in water and other polar solvents.
Guanidine and its derivatives have a wide range of applications in scientific research, including as reagents in biochemical assays, as intermediates in organic synthesis, and as probes for studying protein structure and function.
Researchers can leverage AI-driven protocol comparisons from PubCompare.ai to optimize their Guanidine-related experiments, locating the best protocols from literature, preprints, and patents to enhance reproducibility and accuaracy.
By harnessing the power of AI, scientists can identify the most effective Guanidine products and procedures, experieince the future of scientific research today.

Most cited protocols related to «Guanidine»

Improved Salt Bridge Interactions in CHARMM36

Another refinement in the C36m FF concerns improved description of salt bridge interactions involving guanidinium and carboxylate functional groups with a pair-specific non-bonded LJ parameter (NBFIX term in CHARMM) between the guanidinium nitrogen in arginine and the carboxylate oxygen in glutamate, aspartate as well as the C terminus. This salt bridge interaction was found to be too favorable in the CHARMM protein force fields as indicated by the overestimation of the equilibrium association constant of a guanidinium-acetate solution ,^{33 , 34} as well as the underestimation of its osmotic pressure (personal communication, Benoit Roux). The added NBFIX term increases the R_min from the 3.55 Å based on the Lorentz-Berthelot rule to a larger value of 3.637 Å (Shen and Roux, personal communication), which we subsequently showed to improve the agreement with the experimental osmotic pressure of guanidinium acetate solutions (Supplementary Figure 19). We noted that the NBFIX approach employed here differs from Piana et al’s work²⁷ where the CHARMM22 charges of the Arg, Asp and Glu side chains were reduced in magnitude, with both approaches leading to weaker and more realistic salt-bridge interactions. The NBFIX term makes sure only the specific interaction between Arg and Asp/Glu is modified, while the interaction of these residues with other amino acids, water, or ions are kept the same as in the C36 FF. Again, our aim is to improve the C36 FF with minimal changes in the model.

Huang J., Rauscher S., Nawrocki G., Ran T., Feig M., de Groot B.L., Grubmüller H, & MacKerell AD J.r. (2016). CHARMM36m: An Improved Force Field for Folded and Intrinsically Disordered Proteins. Nature methods, 14(1), 71-73.

Publication 2016

Acetate Amino Acids Arginine Aspartate aspartylglutamate Glutamate Guanidine Ions Nitrogen Osmotic Pressure Oxygen Proteins Sodium Chloride

Proteomic Identification of Fission Yeast Proteins

Two datasets corresponding to the spectral type (CID, Low, Standard, αLP) and (ETD, Low, Standard, αLP) contain 49,167 spectra each. These datasets were generated in the Komives laboratory (University of California, San Diego). The detailed experimental procedures to generate these datasets are as follows. Wild-type S. pombe cells were lysed in: 50mM Tris-HCl pH: 8.0; 150mM NaCl; 5mM EDTA; 10% Glycerol; 50mM NaF; 0.1mM Na3VO4; 0.2% NP40 and stored at −80°C. The debris was pelleted and then the supernatant was collected. The pellet was extracted according to [56 (link)]. Briefly, the pellet was resuspended in 200 ul of 0.1 M NaOH, 0.05 M ETDA, 2% SDS, and 2% beta-mercaptoethanol and incubated at 90°C for 10 minutes. Acetic acid was added to 0.1M and vortexed followed by an additional incubation at 90^°C for 10 minutes before clarification by centrifugation and Methanol/chloroform extraction. The pellet was resuspended in 100 mM Tris containing 0.1% sodium deoxycholate with TCEP at 5 mM. Free thiols were capped with n-ethylmaleimide. Excess reagent was removed by ultrafiltration with amicon-4 10 kDa centrifugal devices. The protein was then quantified and exchanged into 6M guanidine for digestion overnight by αLP. The digests were quenched by the addition of formic acid to 1%, followed by desalting by sep-pak (Waters, Milford, MA). Peptides were then fractionated with Electrostatic Repulsion-Hydrophilic Interaction Chromatography [57 (link)]. Fractions were assayed for protein concentration using a BCA assay and pooled into 18 fractions of equal protein concentration, evaporated to dryness and resuspended in 100 uL of 0.2% FA. Nano liquid chromatography tandem mass spectrometry (nLC-MS/MS) was performed with a LTQ XL mass spectrometer equipped with ETD. 10 ul of each fraction (≈ 1 ug) was injected onto a 12 cm × 75 um I.D.C18 column prepared in house and eluted in 0.2% FA with a gradient of 5% to 40% ACN over 60 min followed by wash and re-equilibration totaling 90 minutes of MS data per run. The flow was split about 1:500 to a flow rate of about 250 nL/min. A survey scan was followed by data dependent fragmentation of the 4 most abundant ions with both CID and ETD with supplemental activation. The maximum MS/MS ion accumulation time was set to 100 ms. Fragmented precursors were dynamically excluded for 45 seconds with one repeat allowed.

Kim S, & Pevzner P.A. (2014). Universal database search tool for proteomics. Nature communications, 5, 5277.

Publication 2014

2-Mercaptoethanol Acetic Acid Biological Assay Cells Centrifugation Chloroform Chromatography Deoxycholic Acid, Monosodium Salt Digestion Disgust Edetic Acid Electrostatics Ethylmaleimide formic acid Glycerin Guanidine Hydrophilic Interactions Liquid Chromatography M-200 Medical Devices Methanol Neoplasm Metastasis Peptides Proteins Radionuclide Imaging Sodium Chloride Sulfhydryl Compounds Tandem Mass Spectrometry tris(2-carboxyethyl)phosphine Tromethamine Ultrafiltration

Purification of Recombinant Prion Protein

DNA Sequences coding for hamster (residues 90–231 and 23–231; accession K02234), deer (residues 24–234; accession AF156185) and sheep (residues 25–234; accession AJ567988) rPrP^c residues were amplified and ligated into the pET41 vector (EMD Biosciences) and sequences were verified. After transforming the plasmids into E. coli Rosetta cells (EMD Biosciences), we expressed the rPrP^c using the Overnight Express Autoinduction system (EMD Biosciences). Cell pellets from 0.25 L cultures were then put through two liquid nitrogen freeze thaw cycles and further lysed with BugBuster master mix (EMD Biosciences) to isolate the inclusion bodies. Next, the inclusion bodies were washed twice with 0.1× BugBuster, pelleted by centrifugation, and frozen at −20°C for later use. Then they were denatured in 8 M guanidine-HCl at pH = 8.5 on a rotator for 50 min at room temperature. Following a 16,000×g spin for 5 min, the denatured protein was then bound to Ni-NTA Superflow resin (Qiagen) that had been equilibrated in denaturing buffer [100 mM sodium phosphate (pH 8.0), 10 mM tris, 6 M guanidine-HCl]. The resin was loaded into a column and, using an AKTA Explorer system (GE Healthcare), the denatured protein was refolded on the column using a linear gradient to refolding buffer [100 mM sodium phosphate (pH 8.0) and 10 mM tris] over 4.5 h at a flow rate of 0.75 mL/min. Next the protein was eluted with a linear gradient to elution buffer [100 mM sodium phosphate (pH 5.8), 10 mM tris, and 500 mM imidazole] at 2 mL/min over 45 min. The protein fractions were diluted 5–10-fold into dialysis buffer [10 mM phosphate (pH 5.8)], filtered with a 0.2 µm syringe filter, and dialyzed. The concentration of rPrP^c was determined by measuring absorbance at 280 nm and purity was ≥99%, as estimated by SDS-PAGE (see Results), immunoblotting (data not shown), and mass spectrometry (mass = 16,238 amu; data not shown) [31] (link)–[33] (link). rPrP^c preparations were aliquotted and stored at 0.2–0.4 mg/mL and −80°C.

Wilham J.M., Orrú C.D., Bessen R.A., Atarashi R., Sano K., Race B., Meade-White K.D., Taubner L.M., Timmes A, & Caughey B. (2010). Rapid End-Point Quantitation of Prion Seeding Activity with Sensitivity Comparable to Bioassays. PLoS Pathogens, 6(12), e1001217.

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Publication 2010

Buffers Cell Culture Techniques Centrifugation Cloning Vectors Deer Dialysis Domestic Sheep Escherichia coli Freezing Guanidine Hamsters imidazole Inclusion Bodies Mass Spectrometry Nitrogen Cycle Pellets, Drug Phosphates Plasmids Proteins Resins, Plant SDS-PAGE sodium phosphate Syringes Tromethamine

Optimized Phenol-Chloroform RNA Extraction

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Publication 2018

Acids Biological Assay Biological Processes Biopharmaceuticals Cells Chloroform Ethanol Gene Expression Gene Expression Profiling Guanidine guanidine thiocyanate isolation Phenol Protein Biosynthesis Reverse Transcriptase Polymerase Chain Reaction Reverse Transcription RNA Silicon Dioxide Sodium Chloride Tissues trizol

Molecular Modeling of Protein-Ligand Interactions

The MM/GBSA or MM/PBSA calculations were applied to six different protein systems, including α-thrombin (7 ligands), avidin (7 ligands), cytochrome C peroxidase (18 ligands), neuraminidase (8 ligands), P450cam (12 ligands) and penicillopepsin (7 ligands). The experimental binding data and the PDB entries for the six proteins are listed in Table S1 in the supporting materials. The chemical structures of the ligands are shown in Figure S1 in the supporting materials. The protonated states for all ligands are shown in Figure 1 in the Supporting Materials.
For ligands bound to α-thrombin, cytochrome C peroxidase, neuraminidase and penicillopepsin, MD simulations were performed based on the crystal structures of the complexes. The starting structures of the six avidin analogues (b2–b7) were generated based on the avidin-biotin complex (PDB entry: 1avd33 (link)). The biotin molecule in the crystal structure was manually mutated to the other ligands. It has been shown that the neutral form of the guanidinium group in b2 and b5 biotin analogues is dominant when it is bound to the protein.34 (link) Therefore, the neutral form of the guanidinium group was used in our simulations. The crystal structures of the nine P450cam ligands were used for MD simulations. Starting structures of the other three P450 ligands (e3, e5 and e6) were obtained by manually modifying the ligand (e1) in the crystal structure of 2cpp35 (link) with the conformation of the protein unaltered. The preparation of the models was accomplished in the SYBYL molecular simulation package.36
In the cytochrome C peroxidase complexes, the lone-pair electrons of the epsilon nitrogen in His175 form resonant bonds with the iron ion and the hydrogen atom is located at the delta nitrogen of His175. In the P450cam complexes, lone-pair electrons of the sulfur atom in Cys357 form resonant bonds with the iron ion and this cysteine residue is thus deprotonated. All the crystal water molecules were kept in the simulations.
The atomic partial charges of all ligands were derived by semiempirical AM1 geometry optimization and subsequent single-point Hartree-Fock (HF)/6-31G* calculations of the electrostatic potential, to which the charges were fitted using the RESP technique.37 The reason why we chose AM1 for optimization, not usually used HF/6-31G(d), is to reduce computational cost.38 (link) The optimization and the electrostatic potential calculations were conducted by Gaussian03.39 Partial charges and force field parameters of the inhibitors were generated automatically using the antechamber program in AMBER9.0.40 (link)
In molecular mechanics (MM) minimizations and MD simulations, the AMBER03 force field was used for proteins41 (link) and the general AMBER force field (gaff) was used for ligands.42 (link) The force field parameters developed by Giammona were used for the heme groups in the cytochrome C peroxidase and the P450cam systems.43 To neutralize the systems, counter ions of Cl− or Na+ were placed in grids that had the largest positive or negative Coulombic potential around the protein. The whole system was immersed in a rectangular box of TIP3P water molecules. The water box was extended 9 Å from solute atoms in all three dimensions.

Hou T., Wang J., Li Y, & Wang W. (2010). Assessing the performance of the MM/PBSA and MM/GBSA methods: I. The accuracy of binding free energy calculations based on molecular dynamics simulations. Journal of chemical information and modeling, 51(1), 69-82.

Publication 2010

Amber Avidin Biotin Camphor 5-Monooxygenase Cysteine Cytochrome c Group Cytochrome c Peroxidase Cytochrome P450 Electrons Electrostatics Guanidine Heme Hydrogen inhibitors Ions Iron Ligands Mechanics Molecular Structure Neuraminidase Nitrogen Peroxidases poly(tetramethylene succinate-co-tetramethylene adipate) Proteins Respiratory Rate Sulfur Thrombin

Most recents protocols related to «Guanidine»

Molecular Modeling of ALK Inhibitor Compound 6

Not available on PMC !

Example 13

Molecular modeling study based upon the co-crystal structure of ALK with Alectinib (PDB: 3AOX) (Sakamoto, H. et al., Cancer Cell 2011, 19, 679) was performed to assess the structure-activity relationship of inhibition of ALK and/or ALK mutants by the compounds of the present application. The modeling showed that Compound 6 makes the same backbone hinge contact as Alectinib, however, Compound 6 forms two additional hydrogen bond interactions between the guanidine moiety of R1120 and the carbonyl group of the dimethyl acetamide group (FIG. 1A). Furthermore, in the G1202R mutant, Compound 6 forms an additional hydrogen bond interaction between the guanidine moiety of R1202 and the nitrogen of the pyrazole ring (FIG. 1B). The modeling study predicted that the methylene spacer between the pyrazole ring and the dimethylacetamide moiety is preferable for the carbonyl amide of Compound 6 to interact with the guanidine moiety of R1120.

US11858897B2. Substituted 6,11-dihydro-5H-benzo[b]carbazoles as inhibitors of ALK and SRPK (2024-01-02). DANA-FARBER CANCER INSTITUTE, INC. [US]. Inventors: John Hatcher [US], Nathanael S. Gray [US], Hwangeun Choi [KR], Pasi Janne [US], Tinghu Zhang [US].

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Patent 2024

alectinib Amides carbene Cells dimethylacetamide Guanidine Hydrogen-6 Hydrogen Bonds Malignant Neoplasms Nitrogen Psychological Inhibition pyrazole Vertebral Column

Synthesis of Pyridine-Substituted Guanidine Compound

Not available on PMC !

Example 13

35 mg of 1-cyano-2-phenyl-3-(pyridin-4-yl)isourea (28) and 50 mg of 1-benzoyl-4-(5′-amino-1′-pentyl)piperazine (6) was dissolved in 5 ml of acetonitrile, and 20.8 μl of triethyl amine was added and stirred overnight at 30° C. (30 hrs). The reaction solution was concentrated under reduced pressure, and directly separated by column chromatography (ethyl acetate/methanol=10:1-5:1 vol/vol, gradient elution), to obtain about 60 mg of a sticky target compound 2-cyano-1-(5-((1-(benzoyl)piperazine-4-yl)pentyl)-3-(4-pyridinyl)guanidine (BSS-PC003). ¹HNMR (400 MHz, CDCl3): δ=8.47-8.29 (m, 2H), 7.41-7.36 (d, 3H), 7.31-7.27 (m, 2H), 7.17-7.03 (m, 2H), 6.02-5.92 (m, 1H, N—H), 3.09-3.03 (m, 4H), 2.89-2.71 (m, 2H), 2.57-2.48 (m, 2H), 2.48-2.43 (m, 2H), 2.41-2.32 (m, 4H), 1.57-1.41 (m, 4H); [M+H]: 420.3.

[Figure (not displayed)]

US11873284B2. Pyridinylcyanoguanidine derivative and use thereof (2024-01-16). None [CN], Rushi Biotech (Hangzhou) Co., Ltd [CN]. Inventors: Zheming Wang [CN], Hao Tan [CN].

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Patent 2024

acetonitrile Amines Chromatography ethyl acetate Guanidine Methanol Piperazine Pressure

Synthesis and Characterization of Oligochitosan Guanidine

Not available on PMC !

EXAMPLE 1

OCG was synthesized and the average molecular weight of OCG was confirmed by both gel permeation chromatography (GPC) and proton nuclear magnetic resonance (H NMR) spectroscopy (FIG. 1), indicating that the number of CG repeating unit is ˜7. The pKa of OCG was determined as ˜5 (FIG. 2), indicating that the OCG backbone is neutral in the physiological condition while the two chain end groups (i.e., secondary amine and guanidine, FIG. 3) are positively charged. Nonhemolytic OCG showed no indication of decreased cell viability of a murine macrophage (i.e., J774) and a human liver carcinoma cell line (i.e., Hep G2) up to 200 μg/mL (FIG. 4).

US11857521B1. Anti-mycobacterial drugs (2024-01-02). None [US], None [US]. Inventors: Joong Ho Moon [US], Michelle Miranda [US].

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Patent 2024

Amines Cell Lines Cell Survival Cytotoxin Gel Chromatography Guanidine Hepatocellular Carcinomas Homo sapiens Macrophage Magnetic Resonance Imaging Mus physiology Protons Spectroscopy, Nuclear Magnetic Resonance Vertebral Column

Synthesis of 2-Cyano-1-(5-((1-Benzoyl)pyrrolidine-3-yl)pentyl)-3-(4-Pyridinyl)Guanidine

Not available on PMC !

Example 15

36 mg of 1-cyano-2-phenyl-3-(pyridin-4-yl)isourea (28) and 51 mg of 1-benzoyl-3-(5′-amino-1′-pentyl)pyrrolidine (15) were dissolved in 5 ml of acetonitrile and then 20.8 μl of triethyl amine was added and stirred overnight at 30° C. (30 hrs). The reaction solution was concentrated under reduced pressure, and directly separated by column chromatography (dichloromethane/methanol vol/vol=10:1-5:1, gradient elution), to obtain about 63 mg of a sticky target compound 2-cyano-1-(5-((1-benzoyl)pyrrolidine-3-yl)pentyl)-3-(4-pyridinyl)guanidine (BSS-PC028). 1HNMR (400 MHz, CDCl3): δ=8.42-8.21 (m, 2H), 7.37-7.30 (m, 3H), 7.29-7.26 (m, 2H), 7.16-7.04 (m, 2H), 6.04-5.83 (m, 1H, N—H), 4.11-3.95 (m, 2H), 3.89-3.74 (m, 2H), 3.65-3.11 (m, 3H), 2.29-1.92 (m, 2H), 1.70-1.53 (m, 2H), 1.47-1.32 (m, 4H), 1.32-1.19 (m, 2H); LC-MS: 405[M+H].

[Figure (not displayed)]

US11873284B2. Pyridinylcyanoguanidine derivative and use thereof (2024-01-16). None [CN], Rushi Biotech (Hangzhou) Co., Ltd [CN]. Inventors: Zheming Wang [CN], Hao Tan [CN].

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Patent 2024

acetonitrile Amines Chromatography Guanidine Methanol Methylene Chloride Pressure pyrrolidine

Synthesis of 2-Cyano-1-(5-((1-Furoyl)piperazine-4-yl)pentyl)-3-(4-Pyridinyl)Guanidine

Not available on PMC !

Example 14

37 mg of 1-cyano-2-phenyl-3-(pyridin-4-yl)isourea (28) and 53 mg of 1-furoyl-4(5′-amino-1′-pentyl)piperazine (5) were dissolved in 5 ml of acetonitrile and then 20.8 μl of triethyl amine was added and stirred overnight at 30° C. (30 hrs). The reaction solution was concentrated under reduced pressure, and directly separated by column chromatography (ethyl acetate/methanol=10:1-5:1 vol/vol, gradient elution), to obtain about 72 mg of a sticky target compound 2-cyano-1-(5-((1-furoyl)piperazine-4-yl)pentyl)-3-(4-pyridinyl)guanidine (BSS-PC007). ¹HNMR (400 MHz, CDCl3): δ=8.55-8.47 (m, 2H), 7.50-7.47 (d, 1H), 7.35-7.28 (m, 2H), 7.09-7.03 (d, 1H), 6.47-6.44 (m, 1H), 6.07-5.90 (m, 1H, N—H), 3.12-3.05 (m, 4H), 2.92-2.77 (m, 2H), 2.59-2.50 (m, 2H), 2.49-2.45 (m, 2H), 2.44-2.35 (m, 4H), 1.55-1.39 (m, 4H); [M+H]: 410.5.

[Figure (not displayed)]

US11873284B2. Pyridinylcyanoguanidine derivative and use thereof (2024-01-16). None [CN], Rushi Biotech (Hangzhou) Co., Ltd [CN]. Inventors: Zheming Wang [CN], Hao Tan [CN].

Full text: Click here

Patent 2024

acetonitrile Amines Chromatography ethyl acetate Guanidine Methanol Piperazine Pressure

Top products related to «Guanidine»

Ni nta bead by Qiagen

Sourced in Germany, United States, Netherlands, France

Ni-NTA beads are a type of agarose-based affinity resin used for the purification of recombinant proteins that contain a polyhistidine (His) tag. The Ni-NTA (Nickel-Nitrilotriacetic Acid) moiety on the beads binds to the His-tagged proteins, allowing them to be separated from other cellular components during the purification process.

Guanidine hcl by Merck Group

Sourced in United States, Germany

Guanidine-HCl is a chemical compound used in various laboratory applications. It is a salt of guanidine and hydrochloric acid, and is commonly used as a denaturing agent in protein purification procedures.

Trizol by Thermo Fisher Scientific

Sourced in United States, Germany, China, Japan, United Kingdom, Canada, France, Italy, Australia, Spain, Switzerland, Belgium, Denmark, Netherlands, India, Ireland, Lithuania, Singapore, Sweden, Norway, Austria, Brazil, Argentina, Hungary, Sao Tome and Principe, New Zealand, Hong Kong, Cameroon, Philippines

TRIzol is a monophasic solution of phenol and guanidine isothiocyanate that is used for the isolation of total RNA from various biological samples. It is a reagent designed to facilitate the disruption of cells and the subsequent isolation of RNA.

Trizol reagent by Thermo Fisher Scientific

Sourced in United States, China, Japan, Germany, United Kingdom, Canada, France, Italy, Australia, Spain, Switzerland, Netherlands, Belgium, Lithuania, Denmark, Singapore, New Zealand, India, Brazil, Argentina, Sweden, Norway, Austria, Poland, Finland, Israel, Hong Kong, Cameroon, Sao Tome and Principe, Macao, Taiwan, Province of China, Thailand

TRIzol reagent is a monophasic solution of phenol, guanidine isothiocyanate, and other proprietary components designed for the isolation of total RNA, DNA, and proteins from a variety of biological samples. The reagent maintains the integrity of the RNA while disrupting cells and dissolving cell components.

Rneasy mini kit by Qiagen

Sourced in Germany, United States, United Kingdom, Netherlands, Spain, Japan, Canada, France, China, Australia, Italy, Switzerland, Sweden, Belgium, Denmark, India, Jamaica, Singapore, Poland, Lithuania, Brazil, New Zealand, Austria, Hong Kong, Portugal, Romania, Cameroon, Norway

The RNeasy Mini Kit is a laboratory equipment designed for the purification of total RNA from a variety of sample types, including animal cells, tissues, and other biological materials. The kit utilizes a silica-based membrane technology to selectively bind and isolate RNA molecules, allowing for efficient extraction and recovery of high-quality RNA.

Protease inhibitor cocktail by Merck Group

Sourced in United States, Germany, China, United Kingdom, Italy, Japan, Sao Tome and Principe, France, Canada, Macao, Switzerland, Spain, Australia, Israel, Hungary, Ireland, Denmark, Brazil, Poland, India, Mexico, Senegal, Netherlands, Singapore

The Protease Inhibitor Cocktail is a laboratory product designed to inhibit the activity of proteases, which are enzymes that can degrade proteins. It is a combination of various chemical compounds that work to prevent the breakdown of proteins in biological samples, allowing for more accurate analysis and preservation of protein integrity.

Ni nta agarose by Qiagen

Sourced in Germany, United States, United Kingdom, Netherlands, China, Switzerland, Italy, Canada, Spain, India

Ni-NTA agarose is a solid-phase affinity chromatography resin designed for the purification of recombinant proteins containing a histidine-tag. It consists of nickel-nitrilotriacetic acid (Ni-NTA) coupled to agarose beads, which selectively bind to the histidine-tagged proteins.

Ni nta agarose bead by Qiagen

Sourced in Germany, United States, United Kingdom, Netherlands, Italy

Ni-NTA agarose beads are a chromatography resin used for the purification of His-tagged proteins. The beads consist of a nickel-nitrilotriacetic acid (Ni-NTA) complex immobilized on an agarose matrix. These beads can selectively bind and capture proteins with a polyhistidine (His-tag) affinity tag, allowing for their efficient separation and purification from complex mixtures.

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.

What are some common applications of Guanidine?

How can I optimize my Guanidine-related experiments?

PubCompare.ai can help you optimize your Guanidine-related experiments. The platform allows you to screen protocol literature more efficiently and leverage AI to pinpoint critical insights. By comparing protocols from literature, preprints, and patents, PubCompare.ai can help you identify the most effective Guanidine products and procedures to enhance reproducibility and accuracy in your research.

What are the different variations or types of Guanidine?

Guanidine is a chemical compound with the formula CH₅N₃, consisting of a carbon atom bonded to three nitrogen atoms. While the basic Guanidine structure remains the same, there are various derivatives and analogues that have been synthesized and studied, each with their own unique properties and applications. These include substituted Guanidines, Guanidinium salts, and Guanidine-containing heterocyclic compounds, among others.

How can I address common usage challenges with Guanidine?

One common challenge with Guanidine is its high solubility in water and other polar solvents, which can make it difficult to handle and measure accurately. Additionally, Guanidine and its derivatives can be sensitive to pH and temperature, requiring careful control of experimental conditions. PubCompare.ai can help you identify the most reliable and effective protocols for working with Guanidine, addressing these usage challenges and improving the reproducibility of your results.

How can PubCompare.ai assist in the optimal use and comparison of Guanidine?

PubCompare.ai allows you to screen protocol literature more efficiently and leverage AI to pinpoint critical insights. The platform's AI-driven analysis can highlight key differences in protocol effectiveness, enabling you to choose the best option for your Guanidine-related research. By harnessing the power of AI, PubCompare.ai can help you identify the most effective Guanidine products and procedures, experieince the future of scientific research today.

More about "Guanidine"

Guanidine is a versatile chemical compound with the formula CH₅N₃, consisting of a carbon atom bonded to three nitrogen atoms.
It is a colorless, crystalline solid that is highly soluble in water and other polar solvents.
Guanidine and its derivatives, including Guanidine-HCl, have a wide range of applications in scientific research, serving as reagents in biochemical assays, intermediates in organic synthesis, and probes for studying protein structure and function.
Researchers can leverage AI-driven protocol comparisons from PubCompare.ai to optimize their Guanidine-related experiments, locating the best protocols from literature, preprints, and patents to enhance reproducibility and accuracy.
By harnessing the power of AI, scientists can identify the most effective Guanidine products and procedures, such as Ni-NTA beads, TRIzol reagent, RNeasy Mini Kit, and Protease inhibitor cocktail, to name a few.
Ni-NTA agarose and Ni-NTA agarose beads are commonly used in conjunction with Guanidine for protein purification and analysis.
Trypsin, another related term, is often employed for protein digestion and sample preparation in Guanidine-based experiments.
PubCompare.ai empowers researchers to experieince the future of scientific research today, where AI-driven protocol comparisons can streamline Guanidine-related experiments and unlock new insights, leading to more accurate and reproducible results.