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> Chemicals & Drugs > Inorganic Chemical > Cyanogen Bromide

Cyanogen Bromide

Cyanogen bromide is a highly reactive chemical compound with the formula CNBr.
It is commonly used in biochemical and molecular biology research as a reagent for the cleavage of peptide bonds, enabling the analysis and identification of proteins.
Cyanogen bromide's ability to cleave proteins at specific amino acid residues makes it a valuable tool for protien sequencing and structural studies.
Its applications include the generation of peptide fragments for mass spectrometry, Edman degradation, and other analytical techniques.
Researchers must exercise caution when handling cyanogen bromide due to its toxicity and explosive nature.
Proper safety precautions are essential when utilizing this powferful chemical in the laboratory.

Most cited protocols related to «Cyanogen Bromide»

1
Purification and Characterization of Envelope Proteins
Env proteins were purified from the supernatants by affinity chromatography using either a 2G12 column or a Galanthus nivalis (GN)-lectin column [25] (link), [27] (link), [46] (link), [64] (link). Briefly, transfection supernatants were vacuum filtered through 0.2-µm filters and then passed (0.5–1 ml/min flow rate) over the column. The 2G12 column was made from CNBr-activated Sepharose 4B beads (GE Healthcare) coupled to the bNAb 2G12 (Polymun Sciences, Klosterneuburg, Austria). Purification using this column was performed as follows: the beads were washed with 2 column volumes of buffer (0.5 M NaCl, 20 mM Tris, pH 8.0) before eluting bound Env proteins using 1 column volume of 3 M MgCl2. The eluted proteins were immediately buffer exchanged into 75 mM NaCl, 10 mM Tris, pH 8.0, using Snakeskin dialysis tubing (10K WCMO) (Thermo Scientific). The buffer-exchanged proteins were further concentrated using Vivaspin columns with a 30-kDa cut off (GE Healthcare). For GN-lectin affinity purification, the wash buffer was Dulbecco's phosphate buffer saline (DPBS) supplemented with 0.5 M NaCl was used, and elution was carried out using DPBS supplemented with 1 M methyl mannopyranoside.
In both cases, the affinity-purified Env proteins were further purified to size homogeneity using size exclusion chromatography (SEC) on a Superdex 200 26/60 column (GE Healthcare). A Superose 6 column was sometimes used for analytical or preparative purposes. The trimer fractions and, occasionally also the SOSIP gp140 monomer fractions, were collected and pooled. Protein concentrations were determined using either a bicinchonic acid-based assay (BCA assay; Thermo Scientific, Rockford, IL) or UV280 absorbance using theoretical extinction coefficients [66] .
Sanders R.W., Derking R., Cupo A., Julien J.P., Yasmeen A., de Val N., Kim H.J., Blattner C., de la Peña A.T., Korzun J., Golabek M., de los Reyes K., Ketas T.J., van Gils M.J., King C.R., Wilson I.A., Ward A.B., Klasse P.J, & Moore J.P. (2013). A Next-Generation Cleaved, Soluble HIV-1 Env Trimer, BG505 SOSIP.664 gp140, Expresses Multiple Epitopes for Broadly Neutralizing but Not Non-Neutralizing Antibodies. PLoS Pathogens, 9(9), e1003618.
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Publication 2013
Acids Biological Assay Broadly Neutralizing Antibodies Buffers Chromatography, Affinity Cyanogen Bromide Dialysis Extinction, Psychological Gel Chromatography Gene Products, env GP 140 Magnesium Chloride Mannose Phosphates Proteins Saline Solution Sepharose 4B snowdrop lectin Sodium Chloride Transfection Tromethamine Vacuum
2
Affinity Purification of Protein Antibodies
The monoclonal anti-CD8 was obtained from Qbiogene. Anti-GM130 and anti-EEA1 were purchased from Becton Dickinson, and the anti-TfnR antibody was obtained from Zymed Laboratories. Polyclonal anti-actin was purchased from Sigma-Aldrich, and the polyclonal anti-CI-MPR (Reaves et al., 1996 (link)) was a gift from J. Paul Luzio (University of Cambridge, Cambridge, UK). Anti-cathepsin D antiserum was obtained from DakoCytomation, and anti-TGN46 was supplied by Serotec. Polyclonal anti-mVPS26, anti-Snx1, and anti-mVPS35 were produced in house using GST fusion proteins as antigens. The antisera were subsequently affinity purified using the respective antigens coupled to CNBr-Sepharose.
, & Seaman M.N. (2004). Cargo-selective endosomal sorting for retrieval to the Golgi requires retromer. The Journal of Cell Biology, 165(1), 111-122.
Publication 2004
Actins anti-d antibody Antibodies, Anti-Idiotypic Antigens BDP1 protein, human Cathepsins Cyanogen Bromide IGF2R protein, human Immune Sera Proteins Sepharose
3
In Vitro Translation Assays for Ribosome-Associated mRNA
All transcripts utilized PCR products as templates for in vitro transcription (Sharma et al., 2010 (link)) except β-VHP-SL, which was transcribed from linearized plasmid. β-VHP-pA transcript was generated by treating β-VHP transcript with poly(A) polymerase to add an ∼200 nt poly(A) tail. 33P-labeled transcripts were generated with 33P-UTP (Perkin-Elmer) in transcription reactions. In vitro translation reactions using rabbit reticulocyte lysate (RRL), phenyl-depleted RRL, and DEAE fractionated RRL (Fr-RRL) were done as before (Sharma et al., 2010 (link); Hessa et al., 2011 (link)). ΔHbs1 RRL was generated by incubating 800 μl RRL with 200 μl of Pelota resin (immobilized via CnBr). Unconjugated and quenched CnBr resin served as a control. Unless indicated otherwise, translation reactions were for 60 min at 32°C. Where indicated, WT or DN Hbs1 was added at 10 min together with 100 μM aurin tricarboxylic acid to inhibit initiation. For direct analyses, translation reactions were denatured in 1% SDS and heated to 100°C. For downstream applications, translation reactions were cooled on ice and manipulated at 0°C–4°C for RNC isolation, sucrose gradients, and native immunoprecipitations (IPs).
Shao S., von der Malsburg K, & Hegde R.S. (2013). Listerin-Dependent Nascent Protein Ubiquitination Relies on Ribosome Subunit Dissociation. Molecular Cell, 50(5), 637-648.
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Publication 2013
2-diethylaminoethanol Aurintricarboxylic Acid Cardiac Arrest Cyanogen Bromide Immunoprecipitation isolation Plasmids Poly(A) Tail Polynucleotide Adenylyltransferase Rabbits Resins, Plant Reticulocytes Sucrose Transcription, Genetic
4
Recombinant Protein Expression in E. coli
Constructs containing a His6 tag, followed by a solubility tag (NTwt, NT*, PGB1, MBP or Trx), a cleavage site (3C protease, tobacco etch virus (TEV) protease, thrombin or CNBr) and a target protein/peptide (rSP-C33Leu, rKL4, rCCK-58, rfhSP-D, rAβ1-40, rAβ1-42, rhCAP-18, rβ17 or rSP-Css) were cloned into pT7 vectors (see Supplementary Fig. 2 for sequences) and subsequently transformed into chemically competent E. coli BL21 (DE3) cells or Origami 2 (DE3) cells (only for NT*-rhCAP-18). Plasmid-containing cells were inoculated to 10 ml LB medium with 70 mg l−1 kanamycin and grown at 37 °C and 180 r.p.m. overnight. Overall, 5 ml over-night culture was inoculated to 500 ml LB medium (1/100) with kanamycin and cells were further grown at 30 °C to OD600∼1. The cells were induced by addition of IPTG to a final concentration of 0.5 mM and expression was performed at 20 °C overnight. The day after, cells were collected by centrifugation, resuspended in 20 mM Tris, pH 8 to 30 ml and stored at −20 °C for at least 24 h. Comparable amounts of cells were taken before induction and after expression and analysed by SDS-PAGE using 15% acrylamide gels stained with Coomassie Brilliant Blue.
Kronqvist N., Sarr M., Lindqvist A., Nordling K., Otikovs M., Venturi L., Pioselli B., Purhonen P., Landreh M., Biverstål H., Toleikis Z., Sjöberg L., Robinson C.V., Pelizzi N., Jörnvall H., Hebert H., Jaudzems K., Curstedt T., Rising A, & Johansson J. (2017). Efficient protein production inspired by how spiders make silk. Nature Communications, 8, 15504.
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Publication 2017
Acrylamide brilliant blue G Cells Centrifugation Cloning Vectors Cyanogen Bromide Cytokinesis Escherichia coli Gels his6 tag Isopropyl Thiogalactoside Kanamycin Peptide Hydrolases Peptides Plasmids prostaglandin B1 Proteins SDS-PAGE TEV protease Thrombin Tromethamine
5
Optimizing GABA(A)R-β3 Subunit Expression
A synthetic cDNA construct encoding the full length human GABAAR β3 subunit, based on GenBank accession number M82919, was codon-optimised for expression in mammalian cells. Approximately one-hundred construct variants were subsequently generated by PCR, to evaluate the consequences of N-linked glycosylation sites removal, mutation of Cysteine residues, N-terminal and C-terminal truncations, truncations in the intracellular loop connecting the transmembrane helices 3 and 4 (M3-M4) and introduction of chimeric domains (such as T4 lysozyme) into predicted flexible loops. These constructs were cloned into the pHLsec vector51 (link), making use of the secretion signal sequence provided by the plasmid. To facilitate small scale screening of protein expression, solubilisation, purification and stabilization conditions, constructs were tagged N-terminally with monoVenus52 (link),53 (link) and C-terminally with a nine amino acid sequence derived from bovine rhodopsin (TETSQVAPA) that is recognised by the Rho-1D4 monoclonal antibody (University of British Columbia)54 (link),55 (link). Small-scale expression trials were performed by transient transfection in adherent HEK293T cell cultures, as previously described51 (link). Expression levels of recombinant GABAAR-β3 variants were evaluated by western blotting using Rho-1D4 as a primary antibody and the efficiency of their cell surface trafficking was monitored by wide-field fluorescence microscopy.
Suitable constructs underwent high-throughput solubilisation screening by FSEC56 (link), using a broad panel of detergents. For this and all subsequent steps, small-scale expression was performed in HEK293S-GnTI− cells, to reduce N-linked glycosylation heterogeneity57 (link),58 (link). Cells were transiently transfected using lipofectamine (Invitrogen) in an adherent format and 48-72 h later were re-suspended and solubilized in a 10 mM HEPES pH 7.2, 300 mM NaCl buffer supplemented with a 1:100 (v/v) dilution of mammalian protease inhibitor solution (Sigma-Aldrich) and 1 % detergent, for 2 h at 4 °C. Insoluble material was removed by centrifugation (10,000g, 15 min) and the supernatant incubated for 2 h at 4 °C with purified Rho-1D4 antibody coupled to CNBr-activated sepharose beads (GE Healthcare). Resin-bound samples were washed with 10 mM HEPES pH 7.2, 300 mM NaCl buffer containing detergent at 3 × CMC and receptor constructs were eluted overnight in the same buffer supplemented with 500 μM TETSQVAPA peptide (Genscript). For size-exclusion chromatography (SEC), samples were loaded onto a Superdex 200 3.2/300 column (GE Healthcare) equilibrated in 10 mM HEPES pH 7.2, 300 mM NaCl, 0.02 % n-Dodecyl-β-D-maltopyranoside (DDM, Anatrace), attached to a high-performance liquid chromatography system with automated micro-volume loader and in-line fluorescence detection (Shimadzu).
Miller P.S, & Aricescu A.R. (2014). Crystal structure of a human GABAA receptor. Nature, 512(7514), 270-275.
Publication 2014
Amino Acid Sequence Bos taurus Buffers Cell Culture Techniques Cells Centrifugation Chimera Codon Cyanogen Bromide Cysteine Detergents DNA, Complementary Fluorescence Gel Chromatography Helix (Snails) HEPES High-Performance Liquid Chromatographies Homo sapiens Immunoglobulins Lipofectamine Mammals Microscopy, Fluorescence Monoclonal Antibodies Muramidase Mutation Peptides Plasmids Protease Inhibitors Protein Glycosylation Proteins Protein Subunits Protoplasm Resins, Plant Rhodopsin secretion Sepharose Signal Peptides Sodium Chloride Technique, Dilution Transfection Transients

Most recents protocols related to «Cyanogen Bromide»

1
Characterization of Recombinant SLC44A2 Protein
Recombinant human SLC44A2 was produced in Sf9 insect cells transfected with full‐length SLC44A2 cDNA as described (Kommareddi et al, 2009 (link)). SLC44A2–NT (CTL2‐NT) rabbit antiserum against synthetic SLC44A2 peptides was coupled to CNBr beads as previously described and used to immunoprecipitate SLC44A2 from cell lysates as described (Nair et al, 2004 (link)). Whole cell lysates from lung tissues of Slc44a2 wild‐type and knockout FVB mice (Kommareddi et al, 2015 (link)) were prepared in lysis buffer with 1% NP‐40 and stored frozen until use. UM‐SCC‐47, a human squamous cell carcinoma cell line, naturally expresses wild‐type SLC44A2 and served as a source of wild‐type SLC44A2 protein. Cell lysates of Sf9 insect cells expressing full‐length rHuSLC44A2 and UM‐SCC 47 expressing wild‐type SLC44A2 protein were similarly prepared. The cell lysates (150 μg protein) were immunoprecipitated with anti CTL2‐NT beads at a concentration of 2 μg/ml, collected and washed by centrifugation and subjected to sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS–PAGE) as described previously (Kommareddi et al, 2009 (link)). The primary antibodies, rabbit anti‐CTL2‐NT (1/500 or 2 μg/ml), human alloantibodies RIF, and VER were used at 1:10. Antibody binding on Western blots was detected with enhanced chemiluminescence using the appropriate affinity purified secondary antibody. Rabbit antihuman IgG‐IgM‐specific antiserum was diluted 1:2,000. Goat anti‐rabbit IgG heavy and light chain specific was used at 1:5,000.
Koehl B., Vrignaud C., Mikdar M., Nair T.S., Yang L., Landry S., Laiguillon G., Giroux‐Lathuile C., Anselme‐Martin S., El Kenz H., Hermine O., Mohandas N., Cartron J.P., Colin Y., Detante O., Marlu R., Le Van Kim C., Carey T.E., Azouzi S, & Peyrard T. (2023). Lack of the human choline transporter‐like protein SLC44A2 causes hearing impairment and a rare red blood phenotype. EMBO Molecular Medicine, 15(3), e16320.
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Publication 2023
anti-IgG Antibodies Buffers Cells Centrifugation Chemiluminescence Cyanogen Bromide DNA, Complementary Freezing Goat Homo sapiens Immune Sera Immunoglobulins Insecta Isoantibodies Lung Mice, Knockout Nonidet P-40 Peptides Proteins Rabbits SDS-PAGE Sf9 Cells Squamous Cell Carcinoma Staphylococcal Protein A Tissues TNFSF14 protein, human Western Blot
2
Affinity Purification of Target Proteins
Cell lysate (500 μg) or recombinant proteins (200 ng) were incubated with erianin-CNBr activated sepharose 4B overnight at 4 °C, and the protein-beads complex was washed four times by the use of rotational incubator to remove non-specific binding. Western blotting was developed to check the pull-down bands.
Wang P., Jia X., Lu B., Huang H., Liu J., Liu X., Wu Q., Hu Y., Li P., Wei H., Liu T., Zhao D., Zhang L., Tian X., Jiang Y., Qiao Y., Nie W., Ma X., Bai R., Peng C., Dong Z, & Liu K. (2023). Erianin suppresses constitutive activation of MAPK signaling pathway by inhibition of CRAF and MEK1/2. Signal Transduction and Targeted Therapy, 8, 96.
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Publication 2023
Cells Cyanogen Bromide Erianin Lanugo Proteins Recombinant Proteins Sepharose 4B
3
Recombinant Protein Production and Antibody Generation
The ectodomains from Mus musculus DCC, neogenin, and UNC5B were amplified by PCR and ligated into a modified PCEP-4 expression vector (gift from Ernst Poeschl) containing a His-8 tag and a BM40 signal peptide. 293-EBNA cells (Invitrogen) were transformed (FuGENE HD; Promega GmbH) with the expression vector and selected after 2 days with puromycin (SigmaAldrich). Conditioned media were applied onto nickel-chelated Sepharose columns (Thermo Fisher Scientific) and after extensive wash with the binding buffer (200 mm NaCl, 20 mm tris-HCl, pH 8) and eluted stepwise by applying binding buffer containing increasing concentrations of imidazole (10–150 mm). The purified recombinant proteins were used to immunise rabbits. The antisera obtained were purified by affinity chromatography on columns with antigens coupled to CNBr-activated Sepharose (Thermo Fisher Scientific). The specific antibodies were eluted with 150 mm NaCl, 0.1 m triethylamine, pH 11.5 and neutralised with 1 m tris-HCl, pH 6.8. To verify the specificity of the different antibodies, western blot analysis with the supernatants from cells expressing the DCC, neogenin, and UNC5B ectodomains were performed.
Meier M., Gupta M., Akgül S., McDougall M., Imhof T., Nikodemus D., Reuten R., Moya-Torres A., To V., Ferens F., Heide F., Padilla-Meier G.P., Kukura P., Huang W., Gerisch B., Mörgelin M., Poole K., Antebi A., Koch M, & Stetefeld J. (2023). The dynamic nature of netrin-1 and the structural basis for glycosaminoglycan fragment-induced filament formation. Nature Communications, 14, 1226.
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Publication 2023
Antibodies Antibody Specificity Antigens Buffers Cells Chromatography, Affinity Cloning Vectors Culture Media, Conditioned Cyanogen Bromide FuGene imidazole Immune Sera Mice, House neogenin Nickel Oryctolagus cuniculus Promega Puromycin Recombinant Proteins Sepharose Signal Peptides Sodium Chloride triethylamine Tromethamine Western Blot
4
Purification and Neutralization of PV
Supernatants with PV were added to columns containing Sepharose 4B beads with CNBr-coupled PGT145, PGT151, or no antibody (as mock control). PV mixed with beads were incubated at 37°C with 5% CO2 for 3h on a nutator. After 3h, beads were allowed to settle down at room temperature. PV was collected by gravity flow from the respective column, filtered through 0.45μm membranes, concentrated by Vivaspin columns with a 100-kDa cut off (Cytiva), and immediately tested in the neutralization assay.
Colin P., Ringe R.P., Yasmeen A., Ozorowski G., Ketas T.J., Lee W.H., Ward A.B., Moore J.P, & Klasse P.J. (2023). Conformational antigenic heterogeneity as a cause of the persistent fraction in HIV-1 neutralization. Research Square.
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Publication Preprint 2023
Biological Assay Cyanogen Bromide Gravity Immunoglobulins Sepharose 4B Tissue, Membrane
5
Polyclonal Antibody Generation and Localization of GSBP
Polyclonal primary antibodies of GSBP1 and GSBP2 were generated in both rabbit and mouse hosts. In detail, hydrophilic regions were selected to generate the antibodies of GSBP1 and GSBP2. An N-terminal fragment (265 to 454) containing 190 residues and a C-terminal fragment (17,623 to 17,823) containing 201 residues were used as antigens for GSBP1 and GSBP2, respectively. The fragment of GSBP1 showed about 28% identity to GSBP2, and the fragment of GSBP2 showed about 38% identity to GSBP1.
To generate the corresponding recombinant proteins of these two antigens, codon-optimized sequences were cloned into the pET32 expression vector and transformed into the E. coli BL21 DE3 strain. Recombinant proteins were purified by Ni-NTA (nitrilotriacetic acid) agarose. The protein molecular weight, purity, and concentration were identified by SDS–polyacrylamide gel electrophoresis. For rabbit antibody, 2 mg of purified protein was mixed with Freund’s complete adjuvant (FCA) or Freund’s incomplete adjuvant (FIA), followed by injection into Japanese White rabbit five times. For mouse antibody, 2 mg of purified protein was mixed with FCA or FIA, followed by injection into Balb/C mice four times. Antiserum titer was tested by enzyme-linked immunosorbent assay. An affinity column was used for antibody purification and was made by coupling 1 mg of antigen to CNBr-activated Sepharose 4B (GE). The antibody was purified by incubating 10 ml of antiserum in the column for 12 hours and then eluted with the glycine buffer (0.15 M, pH 2.5). Commercial primary antibodies for β-tubulin (rat, Thermo Fisher Scientific Invitrogen, catalog no. MA180017) and centrin (mouse, Millipore-Sigma, catalog no. 04-1624) were used for IF.
Cells were transferred from cultures into a plate and washed twice with ddH2O. The cells were permeabilized in 200 μl of 0.5× PHEM (60 mM Pipes, 25 mM HEPES, 10 mM EGTA, 2 mM MgCl2) buffer at 4°C, incubated for 1 hour, and fixed with 200 μl of 1× PHEM–2% paraformaldehyde (PFA) for 15 min. Fixed cells were then treated with 300 μl of 2% PFA–1× PHEM for 1 hour and washed three times with 300 μl of 1× PBS for 10 min each.
IF experiments were done through combinations of primary antibodies from different hosts with corresponding secondary antibodies. To determine the localization of GSBP and spasmin, two primary antibodies were used, i.e., the GSBP polyclonal antibody (rabbit) and centrin antibody (mouse, Millipore-Sigma, catalog no. 04-1624). Cells were incubated in 200 μl of primary antibody solution, which was diluted (1:100) in 1× PBST (1× PBS containing 0.3% Triton X-100)–3% bovine serum albumin at 4°C for 12 hours, and washed three times with 300 μl of 1× PBS for 10 min each. Alexa Fluor 594–conjugated goat anti-rabbit immunoglobulin G (IgG) (Proteintech Group, catalog no. SA00006-4) and Alexa Fluor 488–conjugated goat anti-mouse IgG (Abcam, catalog no. ab150113) were used as the secondary antibodies. Cells were incubated in 200 μl of working solution in 1× PBST (1× PBS containing 0.05% Triton X-100) for 2 hours at room temperature (25°C) in a dark wet box and washed three times with 300 μl of 1× PBS for 10 min each. After washing, cells were stained with anti-fading agent containing DAPI (0.05 mg/ml).
To determine the localization of GSBP1 and GSBP2, primary antibodies of GSBP1 (mouse) and GSBP2 (rabbit) and secondary antibodies of Alexa Fluor 488–conjugated goat anti-mouse IgG and Alexa Fluor 594–conjugated goat anti-rabbit IgG, respectively, were used. The experimental conditions were the same as those for GSBP and spasmin described above.
To determine the localization of tubulin, spasmin, and GSBP, primary antibodies for β-tubulin (rat), centrin (mouse), and GSBP (rabbit) were used. The secondary antibodies used were DyLight 488–conjugated goat anti-rat IgG (Abcam, catalog no. ab98420), Alexa Fluor 680–conjugated goat anti-mouse IgG (Thermo Fisher Scientific Invitrogen, catalog no. A21057), and Alexa Fluor 594–conjugated goat anti-rabbit IgG, respectively. The experimental conditions were the same as for GSBP and spasmin described above. Fluorescence staining was observed at ×100 magnification, and images were recorded with a Leica TCS SP8 STED laser scanning confocal microscope (Leica Microsystems, Mannheim, Germany) and Leica LAS AF lite software (https://webshare.leica-microsystems.com/latest/core/widefield/).
Zhang J., Qin W., Hu C., Gu S., Chai X., Yang M., Zhou F., Wang X., Chen K., Yan G., Wang G., Jiang C., Warren A., Xiong J, & Miao W. (2023). Giant proteins in a giant cell: Molecular basis of ultrafast Ca2+-dependent cell contraction. Science Advances, 9(8), eadd6550.
Publication 2023
Alexa594 alexa fluor 488 Anti-Antibodies Antibodies Antigens Buffers Cells Cloning Vectors Codon Cyanogen Bromide DAPI Egtazic Acid Enzyme-Linked Immunosorbent Assay Escherichia coli Fluorescence Freund's Adjuvant Glycine Goat HEPES Immune Sera Immunoglobulin G Immunoglobulins Japanese Magnesium Chloride Mice, House Mice, Inbred BALB C Microscopy, Confocal Nitrilotriacetic Acid paraform piperazine-N,N'-bis(2-ethanesulfonic acid) Proteins Rabbits Recombinant Proteins SDS-PAGE Sepharose Sepharose 4B Serum Albumin, Bovine spasmin Strains Trimethoprim-Sulfamethoxazole Combination Triton X-100 Tubulin

Top products related to «Cyanogen Bromide»

1
Sepharose 4b by GE Healthcare
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Sepharose 4B is a cross-linked agarose-based gel matrix used as a chromatography medium for the purification and separation of biomolecules. It provides a high degree of chemical and physical stability, as well as a porous structure that facilitates efficient adsorption and elution of target molecules.
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Cnbr activated sepharose by GE Healthcare
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CNBr-activated Sepharose is a lab equipment product that serves as a solid support matrix for protein purification and immobilization. It is a beaded agarose medium activated with cyanogen bromide, enabling covalent coupling of ligands for affinity chromatography applications.
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Cnbr activated sepharose 4b by GE Healthcare
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CNBr-activated Sepharose 4B is a chromatography resin used in affinity purification of proteins and other biomolecules. It consists of agarose beads that have been activated with cyanogen bromide, allowing for covalent coupling of ligands such as antibodies or enzymes. The resin can be used to capture and purify target molecules from complex mixtures.
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Sepharose 4b by Merck Group
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Sepharose 4B is a cross-linked agarose-based chromatography medium used for the separation and purification of biomolecules. It offers a highly porous structure, providing a large surface area for adsorption and separation processes. Sepharose 4B can be used in a variety of chromatographic techniques, including size exclusion, ion exchange, and affinity chromatography.
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Sepharose 4b beads by GE Healthcare
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Dimethyl sulfoxide (dmso) by Merck Group
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Cyanogen bromide activated sepharose 4b by Merck Group
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Cyanogen bromide-activated-Sepharose 4B is a matrix product used for the immobilization and purification of various biomolecules, such as proteins, enzymes, and antibodies. It is a covalent coupling agent that attaches ligands to the Sepharose 4B resin, enabling the capture and isolation of target molecules from complex samples.
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Sepharose by GE Healthcare
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Sepharose is a cross-linked agarose-based gel matrix used in chromatography applications for the purification and separation of biomolecules. It provides a porous structure that allows for efficient liquid-solid interactions and high binding capacities. Sepharose can be functionalized with various ligands to enable the capture and separation of specific target molecules from complex mixtures.
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Cnbr activated sepharose 4b beads by GE Healthcare
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Cyanogen bromide is a chemical compound commonly used in various laboratory applications. It serves as a reagent for the cleavage of peptide bonds in proteins during protein analysis and purification procedures.

More about "Cyanogen Bromide"

Cyanogen bromide (CNBr) is a highly reactive chemical compound with the formula CNBr, commonly utilized in biochemical and molecular biology research.
It serves as a powerful reagent for the cleavage of peptide bonds, enabling the analysis and identification of proteins.
This capability makes cyanogen bromide a valuable tool for protein sequencing and structural studies, as it can generate peptide fragments for mass spectrometry, Edman degradation, and other analytical techniques.
Researchers often employ cyanogen bromide in conjunction with Sepharose 4B, a popular chromatography resin.
CNBr-activated Sepharose 4B is a common affinity chromatography medium used for protein purification and immobilization.
The cyanogen bromide activation allows for the covalent coupling of ligands, such as antibodies or enzymes, to the Sepharose 4B beads, enabling efficient capture and separation of target proteins.
When handling cyanogen bromide, it is crucial to exercise caution due to its toxicity and explosive nature.
Proper safety precautions, such as the use of personal protective equipment and well-ventilated workspaces, are essential.
Dimethyl sulfoxide (DMSO) is sometimes used as a solvent for cyanogen bromide to improve its solubility and handling properties.
Researchers can leverage the power of AI-driven platforms like PubCompare.ai to optimize their cyanogen bromide research protocols.
These tools can help locate the best procedures from literature, preprints, and patents, while providing advanced AI comparisons to ensure reproducibility and accuracy.
By utilizing these resources, researchers can take their cyanogen bromide studies to new heights and unlock valuable insights into protein structure and function.