Sulfo nhs

Manufactured by Merck Group

Sourced in United States, Germany, France

Sulfo-NHS is a water-soluble, N-hydroxysulfosuccinimide ester that can be used to activate carboxyl groups for conjugation reactions. It is commonly used in protein labeling, cross-linking, and immobilization experiments.

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Lab products found in correlation

Gallic acid, by Merck Group (4 mentions) Pierce bca protein assay kit, by Thermo Fisher Scientific (4 mentions) Tween 20, by Merck Group (3 mentions) Bovine serum albumin (bsa), by Merck Group (3 mentions) Proteon xpr36 protein interaction assay v 3, by Bio-Rad (3 mentions) Poly l lysine (pll), by Merck Group (3 mentions) Sodium hydroxide (naoh), by Merck Group (2 mentions) Phosphate buffered saline (pbs), by Merck Group (2 mentions) Sodium chloride (nacl), by Merck Group (2 mentions) Peg amine molecules, by Laysan Bio (2 mentions) 0.1 m mes 2 n morpholino ethanesulfonic acid, by Merck Group (2 mentions) N 3 dimethylaminopropyl n 0 ethylcarbodiimide hydrochloride, by Merck Group (2 mentions) Lf20 40, by FMC Biopolymer (2 mentions) Sulfo nhs, by Thermo Fisher Scientific (2 mentions) Acetic acid, by Merck Group (2 mentions) 4 6 diamidino 2 phenylindole (dapi), by Thermo Fisher Scientific (2 mentions) Pbs buffer, by Thermo Fisher Scientific (2 mentions) Glycine solution, by Merck Group (1 mentions) Hydrochloric acid (hcl), by Merck Group (1 mentions) Glucono δ lactone gdl, by Merck Group (1 mentions)

Close spelling variants of this product

N-hydroxysulfosuccinimide sodium salt (sulfo-NHS) (26 citations) N-hydroxysulfosuccinimide (sulfo-NHS) (20 citations) Sulfo-NHS-LC-Biotin (6 citations) Sulfo-NHS-SS-biotin (5 citations) Sulfo-NHS-biotin (5 citations) Sulfo-N-hydroxy succinimide (sulfo-NHS) (3 citations) DBCO-sulfo-NHS (3 citations) DBCO-Sulfo-NHS ester (3 citations) Sulfo-N-hydroxysulfosuccinimide (sulfo-NHS; (3 citations) Sulfo-N-hydroxysuccinimide (S-NHS), (3 citations)

53 protocols using sulfo nhs

Antibody-Conjugated Quantum Dot Labeling

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Orange QDs were conjugated to anti-A (clone: 9113D10, lot: 71EF01EA; Fresenius Kabi) or anti-B (clone: 9621A8, lot: 08D01A21; Fresenius Kabi) by using N-ethyl-3-(3-dimethylaminopropyl)carbodiimide hydrochloride (EDC) (Fluka) and N-hydroxysulfosuccinimide sodium salt (Sulfo-NHS) (Sigma Aldrich Co.) as coupling reagents. We first adjusted the pH of 2 mL of CdTe QDs (3 μM) to 5.5 by using MSA at 4.9% (w/v). We then added 1 mL of EDC (at 0.4 mg·mL⁻¹) and, after 5 minutes, 1 mL of Sulfo-NHS at 1.1 mg·mL⁻¹ to the QDs sample.7 (link),21 Fifteen minutes later, we added 40 μL of anti-A antibody or anti-B antibody to the system (the same antibodies described in the section “Blood samples”).
Green QDs were also covalently bonded to the UEA I lectin, also known as anti-H, obtained from Sigma Aldrich Co. (reference L5505) by using EDC and Sulfo-NHS. To this end, we used 1 mL of green QDs (4.5 μM), 1 mL of EDC (at 4.0 mg·mL⁻¹), and 1 mL of Sulfo-NHS (at 10 mg·mL⁻¹). At the end of the process, we inserted 200 μL of UEA I (at 0.5 mg·mL⁻¹) into the system.
Prior to RBC labeling, systems were incubated with 50 μL of Tris base (at 1 mM) for 2 hours under slow agitation. This procedure was used to quench the free carboxyl groups of nonconjugated QDs to minimize unspecific targets.

Cabral Filho P.E., Pereira M.I., Fernandes H.P., de Thomaz A.A., Cesar C.L., Santos B.S., Barjas-Castro M.L, & Fontes A. (2015). Blood group antigen studies using CdTe quantum dots and flow cytometry. International Journal of Nanomedicine, 10, 4393-4404.

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Crosslinking Approach for Porous Materials

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The buffer was changed to 0.02 M 2-(N-morpholino)ethanesulfonic acid sodium salt (MES) (Sigma Aldrich) and 0.15 M NaCl before crosslinking. Crosslinking agents were N-(3dimethylaminopropyl)-N'-ethylcarbodiimide hydrochloride (EDC) and Nhydroxysulfosuccinimide sodium salt (sulfo-NHS) (Sigma Aldrich) in 0.02 M MES and 0.15 M NaCl for 16 hours. EDC was either set to 100 mM or 200 mM, and the concentration of sulfo-NHS was kept constant at 50 mM. Glucono-δ-lactone (GDL) (Sigma Aldrich) was used to dissolve the template core at pH 6.5 in a ratio GDL:CaCO3 2:1. For removal of impurities after crosslinking, dialysis with a membrane of 8-10 kDa in pore size was used (Spectrum Laboratories Inc., USA).

Craig M ., Altskär A ., Nordstierna L , & Holmberg K . (2016). Bacteria-triggered degradation of nanofilm shells for release of antimicrobial agents. Journal of materials chemistry. B, 4(4).

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Avidin-Functionalized Gold Nanoparticles

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Citrate-capped gold nanoparticles with a diameter of ca. 40 nm were synthesized with the Turkevich method as previously described. (25) The nanoparticles were then modified with 0.1 mM thiolated polyethylene glycol (PEG) molecules ending in carboxylate moieties [poly(ethylene glycol) 2-mercaptoethyl ether acetic acid, Mn 2100, Sigma] overnight. The resulting pegylated nanoparticles were concentrated and washed with water five times via centrifugation at 8000 rpm for 6 min. The nanoparticles were finally suspended in 0.5 M 2-(Nmorpholino)ethanesulfonic acid (Sigma) adjusted at pH 5.5. Carboxylate moieties around the nanoparticles were then transformed into sulfo-NHS esters by adding 1 mg of N-(3dimethylaminopropyl)-Nâ€²-ethylcarbodiimide hydrochloride (Sigma) and 2 mg of N-hydroxysulfosuccinimide sodium salt (sulfo-NHS, Sigma) for 20 min. Then, the nanoparticles were pelleted by centrifugation, and the supernatant was substituted for a solution containing 1 mgÂ•mL â€"1 avidin in 0.1 M phosphate buffer pH 7.4. After 1 h, unreacted sulfo-NHS esters were capped with 0.1 M glycine and 10 mgÂ•mL â€"1 bovine serum albumin (BSA) for 30 min. The nanoparticles were then washed five times with phosphate buffer saline (PBS) containing 0.1% Tween-20 (PBST). The resulting avidincovered nanoparticles were kept at 4 Â°C until used.

Alba-Patiño A., Adrover-Jaume C, & Rica R. (2020). Nanoparticle Reservoirs for Paper-Only Immunosensors. ACS sensors, 5(1).

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Measuring HA Ectofusion Immunogen Binding

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The binding affinity of the HA ectofusion immunogens to conformation-specific antibodies was measured using SPR (ProteOn XPR36 Protein Interaction Array V.3.1, Bio-Rad). First, the GLM sensor chip was activated using EDC and sulfo-NHS (Sigma, St. Louis, MO, USA), followed by Protein G (10 μg/mL) (Sigma) immobilization in various channels for 300 s (30 μL/min) in the presence of 10 mM sodium acetate buffer (pH 4.0) and then using 1 M ethanolamine excess sulfo-NHS esters quenched. Nearly 1000 response units (RU) of monoclonal antibodies MAb2077, C05, and CR9114 were immobilized at a flow rate of 5 μg/mL for 100 s. Five different concentrations (100 nM, 50 nM, 25 nM, 12.5 nM, and 6.25 nM) of HA ectofusion immunogens were passed at a flow rate of 30 μL/min for 100 s over the chip surface, followed by a dissociation step of 200 s. After each kinetic assay, the chip was regenerated in 0.1 M Glycine-HCl (pH 2.7), and kinetic parameters were obtained by fitting the data to a simple 1:1 Langmuir interaction model using Proteon Manager.

Mittal N., Sengupta N., Malladi S.K., Reddy P., Bhat M., Rajmani R.S., Sedeyn K., Saelens X., Dutta S, & Varadarajan R. (2021). Protective Efficacy of Recombinant Influenza Hemagglutinin Ectodomain Fusions. Viruses, 13(9), 1710.

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Synthesis and Characterization of Aminated Graphene

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The aqueous dispersion of the initial GO employed for the synthesis of the aminated graphene was purchased from Graphene Technologies (Moscow, Russia, www.graphtechrus.com (accessed on 24 April 2023)). Formamide (CH₃NO), 2-(N-morpholino)ethanesulfonic acid (MES free acid), 1-ethyl-3-carbodiimide hydrochloride (EDC), N-hydroxysuccinimide (NHS), Sulfo-NHS, phosphate buffered saline (PBS), Tween 20, sodium hydroxide (NaOH), sodium chloride (NaCl), glycine solution and hydrochloric acid (HCl) were acquired from Merck KGaA (Darmstadt, Germany).
Monoclonal antibodies towards human IgM immunoglobulins were purchased from ImteK, Ltd. (Moscow, Russia). IgM immunoglobulins from human serum (~95% HPLC, buffered aqueous solution) and bovine serum albumin (BSA) were purchased from Merck KGaA (Darmstadt, Germany).
All the organic solvents used in this work were acquired from Vecton Ltd. (Saint-Petersburg, Russia).
All the chemicals were of analytical purity grade, commercially available and used as received without additional purification.

Rabchinskii M.K., Besedina N.A., Brzhezinskaya M., Stolyarova D.Y., Ryzhkov S.A., Saveliev S.D., Antonov G.A., Baidakova M.V., Pavlov S.I., Kirilenko D.A., Shvidchenko A.V., Cherviakova P.D, & Brunkov P.N. (2023). Graphene Amination towards Its Grafting by Antibodies for Biosensing Applications. Nanomaterials, 13(11), 1730.

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SARS-CoV-2 Spike Protein RBD Assay

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S2k sensor chips with gold surfaces modified with carboxylated polysaccharide were purchased from SensiQ Technologies, Inc., Oklahoma City, OK, USA. EDC, Sulfo-NHS, and other reagents for the immobilisation of proteins were supplied by Merck, Darmstadt, Germany. Anti-SARS-CoV-2 Spike Glycoprotein RBD antibody (ab277628) and recombinant human coronavirus SARS-CoV-2 Spike Glycoprotein RBD (ab273065) were purchased from Abcam, Cambridge, UK. Anti-SARS-CoV-2 QuantiVac ELISA test kits for the reference sample evaluation were purchased from Euroimmun, Wrocław, Poland. Reagents used to prepare buffers were purchased from Merck, Darmstadt, Germany and POCh, Gliwice, Poland. Plasma samples from both positive and negative COVID-19 patients were stored, prepared, and used for experiments in the microbiological laboratory of the National Institute of Tuberculosis and Lung Diseases in Warsaw, Poland.

Trzaskowski M., Mazurkiewicz-Pisarek A., Trzciński J.W., Drozd M., Podgórski R., Zabost A, & Augustynowicz-Kopeć E. (2023). Portable Surface Plasmon Resonance Detector for COVID-19 Infection. Sensors (Basel, Switzerland), 23(8), 3946.

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Synthesis and Functionalization of Silica Nanoparticles

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2-(N-morpholino)ethanesulfonic acid (MES, Sigma-Adrich, Darmstadt, Germany), 3-aminopropyltriethoxysilane (APTES, Sigma-Adrich), 3-mercaptopropyl triethoxysilane (MPTES, >95%, Sigma-Adrich), ammonium fluoride (NH₄F, >98% Fluka, Darmstadt, Germany), Atto 633-carboxy dye (Atto-Tec, Siegen, Germany), 4′,6-diamidino-2-phenylindole (DAPI, Thermo Fisher, Schwerte, Germany), block copolymer surfactant (Pluronic F127 (EO₁₀₆PO₇₀EO₁₀₆), Sigma-Aldrich), cetyltrimethyl-ammonium chloride (CTAC, 25% in H₂O, Sigma-Adrich), N-(3-dimethylaminopropyl)-N′-ethylcarbodiimide hydrochloride (EDC, >97%, Sigma-Adrich), N-hydroxysulfosuccinimide (sulfo-NHS, 98%, Sigma-Adrich), octadecyltrimethylammonium bromide (C₁₈Br, Sigma-Adrich), propidium iodide, tetraethylorthosilicate (TEOS, >98%, Sigma-Aldrich), triethanolamine (TEA, 98%, Fluka), triisopropylbenzene (TiPB, 96%, Sigma-Adrich). Oligomer 454 [42 (link)] and Mal-PEG-GE11 [41 (link)] were synthesized as described before. siRNA and miRNA duplexes were purchased from Axolabs GmbH (Kulmbach, Germany): control RNA (sense: 5-AuGuAuuGGccuGuAuuAGdTsdT-3′, antisense: 5′-CuAAuAcAGGCcAAuAcAUdTsdT-3), miR200c (sense: 5′-UCCAUCAUUACCCGGCAGUAUUA-3, antisense: 5′-UAAUACUGCCGGGUAAUGAUGGA-3).

Haddick L., Zhang W., Reinhard S., Möller K., Engelke H., Wagner E, & Bein T. (2020). Particle-Size-Dependent Delivery of Antitumoral miRNA Using Targeted Mesoporous Silica Nanoparticles. Pharmaceutics, 12(6), 505.

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Engineered Alginate Hydrogel Synthesis

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Sodium alginate with an average molecular weight of 280kDa (high-MW) was obtained for these studies (LF20/40, FMC Biopolymer). Molecular weight of alginate was modulated as has been described previously^{18 (link)}. Briefly, Mid- or low-MW alginate was prepared by irradiating high-MW alginate with a 3 or 8 Mrad cobalt source, respectively. mid-MW alginate had an average molecular weight of 70 kDA and low-MW alginate had an average molecular weight of 35 kDa. Polyethylene glycol (PEG) coupled alginate was prepared following a previous protocol^{18 (link)}. Briefly, one chain of low-MW alginate was covalently coupled to an average of two PEG-amine molecules (5 kDa, Laysan Bio) using carbodiimide chemistry. Specifically, at a pH of 6.5, 500 mg of alginate was dissolved in 50 ml of 0.1 M MES (2-(N -morpholino) ethanesulfonic acid, Sigma-Aldrich) buffer. Then 13.7 mg of Sulfo-NHS, 24.2 mg of EDC (N -(3-dimethylaminopropyl)-N⁰ -ethylcarbodiimide hydrochloride, Sigma-Aldrich), and 295 mg of PEG-amine was mixed with the solution, and the reaction was allowed to proceed for 20 h. The resulting solution was dialyzed for three days in deionized water (molecular weight cutoff of 10 kDa). Finally, the product was purified with activated charcoal, sterile filtered, frozen and lyophilized.

Lee H.P., Gu L., Mooney D.J., Levenston M.E, & Chaudhuri O. (2017). Mechanical confinement regulates cartilage matrix formation by chondrocytes. Nature materials, 16(12), 1243-1251.

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Electrochemical Biosensing with AuNHA

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Carbon screen-printed electrodes (CSPE), DRP-110, used for EC sensing purposes, were bought from DropSens (Llanera, Asturias, Spain). EC measurements were conducted by an AUTOLAB PGSTAT204 (Metrohm AG, Herisau, Switzerland) compact and modular potentiostat/galvanostat. Gold nanohole arrays (AuNHA) were fabricated in-house as described elsewhere [28 (link)]. Optical measurements were performed with an inverted microscope (Nikon Eclipse-Ti, Tokio, Japan) and a CCD spectrometer (Andor Shamrock 303i, Andor Technology Ldt., Belfast, UK).
All chemicals used throughout the study; phosphate-buffered saline (PBS, 1×), K₄Fe(CN)₆, K₃Fe(CN)₆, KCl, dopamine hydrochloride, buspirone hydrochloride, etoposide, and acetaminophen (APAP), carboxylic acid-functionalized 50 nm gold nanoparticles coated with polyethylene glycol (PEG 3000), crosslinking reagents EDC, sulfo-NHS, bis(sulfosuccinimidyl)suberate (BS3), ethanolamine, bovine serum albumin (BSA), and Tween 20 were purchased from Sigma-Aldrich (Buchs, Switzerland). PEGylated alkanethiol compounds HS-C₆EG₄OH and HS-C₁₁EG₄OCH₂COOH were acquired from Prochimia Surfaces (Sopot, Poland). Dopamine (D3) receptor synthetic peptide (ab128688) was purchased from Abcam (Cambridge, UK).

Kilic T., Soler M., Fahimi-Kashani N., Altug H, & Carrara S. (2018). Mining the Potential of Label-Free Biosensors for In Vitro Antipsychotic Drug Screening. Biosensors, 8(1), 6.

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Covalent Modification of PLGA Nanoparticles

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The covalent modification of PLGA nanoparticles with affibody was carried out using EDC (Sigma, Darmstadt, Germany) and sulfo-NHS (Sigma, Darmstadt, Germany) as crosslinking agents via the formation of amide bonds between the carboxyl groups of affibody and amino groups of PLGA. An amount of 100 µg of affibody (purified as described by us previously [17 (link)]) in 100 μL of 0.1 M 2-(N-morpholino) ethanesulfonic acid buffer, pH 5.0 was activated with 50 µg EDC and 25 µg sulfo-NHS for 45 min at 15 °C. Next, the activated affibody Z_HER2:342 was quickly added to 1 mg of PLGA nanoparticles in 300 μL of borate buffer (0.4 M H₃BO₃, 70 mM Na₂B₄O₇, pH 8.0) and sonicated for several seconds. The reaction was carried overnight at room temperature, followed by particle washing from non-bound proteins by triple centrifugation at 4000× g for 10 min.

Shipunova V.O., Sogomonyan A.S., Zelepukin I.V., Nikitin M.P, & Deyev S.M. (2021). PLGA Nanoparticles Decorated with Anti-HER2 Affibody for Targeted Delivery and Photoinduced Cell Death. Molecules, 26(13), 3955.

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