Sulfo smcc crosslinker

Manufactured by Thermo Fisher Scientific

Sourced in United States

Sulfo-SMCC is a water-soluble, amine-reactive crosslinking reagent. It contains an N-hydroxysulfosuccinimide (sulfo-NHS) ester and a maleimide group, which allows it to conjugate primary amines and sulfhydryl groups.

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Lab products found in correlation

Bradford protein assay kit, by Thermo Fisher Scientific (2 mentions) Aptes, by Thermo Fisher Scientific (1 mentions) Aptes, by Merck Group (1 mentions) Carboxylated polystyrene beads, by Polysciences (1 mentions) Polystyrene beads, by Spherotech (1 mentions) Biotinylated bsa, by Merck Group (1 mentions) Streptavidin polystyrene beads, by Spherotech (1 mentions) Bovine serum albumin (bsa), by Merck Group (1 mentions) Biacore cm5 sensor chip, by GE Healthcare (1 mentions) Zeba spin desalting column, by Thermo Fisher Scientific (1 mentions) Ribolock rnase inhibitor, by Thermo Fisher Scientific (1 mentions)

Close spelling variants of this product

Sulfo-SMCC

8 protocols using sulfo smcc crosslinker

Synthesis and Validation of ADRQβ-004 Vaccine

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Peptide synthesis and vaccine preparation were performed as described previously [22 (link)]. In brief, the epitope CGITEEAGY (termed ADR-004), which belongs to the second extracellular loop (ECL2) of α1D-AR, was synthesized and validated by GL Ltd. (Shanghai, China) with a purity above 98%. VLP was expressed and purified and then identified using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and transmission electron microscopy. ADR-004 was covalently conjugated to VLP using a Sulfo-SMCC crosslinker (Thermo Fisher Scientific, Massachusetts, USA) to produce the vaccine called ADRQβ-004. The conjugation rate of the ADRQβ-004 vaccine was analyzed by SDS-PAGE. The concentration of the vaccine was determined using a Bradford protein assay kit (Thermo Fisher Scientific, Massachusetts, USA).

Li X., Ma W., Zhou Y., Li C., Shi D., Kuang W., Wu J., Liao Y., Qiu Z, & Zhou Z. (2023). Vaccine Targeting Alpha 1D-Adrenergic Receptor Improved Metabolic Syndrome in Mice. Cardiovascular Drugs and Therapy, 38(3), 539-554.

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DNA-Bead Tether Formation for Single-Molecule Stretching

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A flow channel (volume ∼10–20 μl) was constructed on a (3-aminopropyl)triethoxy silane (APTES) (Sigma-Aldrich) functionalized coverslip (32 × 22 mm). The channel was incubated with the sulfo-SMCC crosslinker (dissolved in 1× phosphate buffered saline (PBS) buffer, pH 7.4) for 30 min. After washing out the unbound sulfo-SMCC, the thiol-labeled DNA construct was introduced into the channel, and incubated for another 30 min. The thiol-end of the DNA construct was covalently attached to the amine group of APTES via this sulfo-SMCC crosslinker (Thermo Scientific). The channel was then blocked with bovine serum albumin (BSA) solution (10 mg/ml BSA, 1 mM 2-mercaptoethanol, 1× PBS saline pH 7.4 buffer) for at least 2 h before the experiment. For the experiment, 2.8 μm-diameter streptavidin coated paramagnetic beads (Dynal M-280, Life technologies) were incubated in the channel for ∼10 min to bind the biotinylated end of the DNA construct. For single-molecule stretching experiments, the working buffer (50 mM KCl, 10 mM Tris, pH 7.4) was flushed into the channel. All experiments were performed using these buffer conditions at 25°C.

Gulvady R., Gao Y., Kenney L.J, & Yan J. (2018). A single molecule analysis of H-NS uncouples DNA binding affinity from DNA specificity. Nucleic Acids Research, 46(19), 10216-10224.

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Crosslinker-Mediated Biomolecular Conjugation

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Sulfo-SMCC crosslinker (Thermo Scientific—22622), 1,010 bp DNA functionalized with appropriate end groups (primers specified in the following methods), 1.25 μm streptavidin polystyrene beads (Spherotech—SVP-10-5), 0.75 μm polystyrene beads (Spherotech—PP-08-10), 1.0 μm carboxylated polystyrene beads (Polysciences—08266), biotinylated BSA (5 mg ml⁻¹, received as a gift from Ted Feldman at Harvard University), BSA (Sigma—A3059), 50 mM acetate buffer (pH 4.9), PBS (1 × , pH 7.4), Whatman Grade 1 Filter Paper (Sigma—WHA1001110), Trichoderma reesei cellulase mixture (Sigma—C2730) and deionized (DI) water were used.

Brady S.K., Sreelatha S., Feng Y., Chundawat S.P, & Lang M.J. (2015). Cellobiohydrolase 1 from Trichoderma reesei degrades cellulose in single cellobiose steps. Nature Communications, 6, 10149.

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EGFL7 Protein Interaction Profiling

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All procedures were done according to the SPRimager®II array instrument (GWC Technologies) guidelines. Briefly, amine-reactive SPR chip (GWC Technologies) was subjected to the Sulfo-SMCC crosslinker (Thermo Scientific) for functionalization with a maleimide group. Each peptide containing a Cys molecule was immobilized onto the gold-coated spots on the SPR chip. Different concentrations (1 nM, 20 nM, and 50 nM) of purified EGFL7 were introduced as a continuous flow over the chip for 10 min. Real-time images and percent change in reflectivity (%ΔR) were recorded and analyzed.
For nanoparticles characterization, purified recombinant EGFL7 (Sino Biological Inc.) was diluted to a final concentration of 0.25 µM in 10 mM sodium acetate at pH 5, and coupled to a Biacore Sensor chip CM5 (GE Healthcare). Different concentrations of CPMV-PEG-E7p72 or CPMV-PEG nanoparticles (90, 45, 22.5, 11.3, 5.6, 2.8 and 1.4 µg mL⁻¹) were injected into the Biacore 3000 instrument, and allowed to flow over the chip (flow rate: 30 µL min⁻¹; injection time: 2 min). Dissociation curves were obtained by flowing binding buffer over the chip for 15 minutes. Chip regeneration was performed by exposing chip to a high salt solution (5 M NaCl) for 30 seconds in between samples. Response units were plotted over time to generate an association and dissociation curve.

Cho C.F., Yu L., Nsiama T.K., Kadam A.N., Raturi A., Shukla S., Amadei G.A., Steinmetz N.F., Luyt L.G, & Lewis J.D. (2017). Viral nanoparticles decorated with novel EGFL7 ligands enable intravital imaging of tumor neovasculature. Nanoscale, 9(33), 12096-12109.

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Antibody-Peptide Conjugation Protocol

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Rat anti-mouse TNF-α antibody (clone XT3.11, Bio X Cell) or mouse anti-mouse TGF-β antibody (clone 1D11.16.8, Bio X Cell) was incubated with 30-fold molar excess of sulfo-SMCC cross-linker (Thermo Fisher Scientific) for 30 min at room temperature. Unreacted cross-linker was removed using a Zeba spin desalting column (Thermo Fisher Scientific), and then 30-fold molar excess of CBP (LRELHLNNNC) or CBP sequence scrambled peptide [scramble 1 (LNNLRLHENC), scramble 2 (LEHNNRLLNC), or scramble 3 (RNNLHENLLC)] was added and reacted for 1 hour at room temperature for conjugation to the thiol moiety on the C residue. The peptide had been synthesized with >95% purity by GenScript.

Katsumata K., Ishihara J., Mansurov A., Ishihara A., Raczy M.M., Yuba E, & Hubbell J.A. (2019). Targeting inflammatory sites through collagen affinity enhances the therapeutic efficacy of anti-inflammatory antibodies. Science Advances, 5(11), eaay1971.

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PCSK9 Peptide Vaccine Development

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The PCSK9‐003 epitope peptide (F‐A‐Q‐S‐I‐P‐W‐N) derived from human PCSK9 was synthesized by GL Ltd. (Shanghai, China). The purity was above 98% and was determined using high‐performance liquid chromatography and mass spectrometry. The peptide was conjugated to the Qβ virus‐like particles using Sulfo‐SMCC crosslinker (Thermo Fisher Scientific, Waltham, MA, USA) to produce the PCSK9Qβ‐003 vaccine. The conjugation rate of PCSK9Qβ‐003 vaccine was analyzed on an SDS‐PAGE gel. The vaccine concentration was determined using Bradford protein assay kit (Thermo Fisher Scientific, Waltham, MA, USA).

Wu D., Zhou Y., Pan Y., Li C., Wang Y., Chen F., Chen X., Yang S., Zhou Z., Liao Y, & Qiu Z. (2019). Vaccine Against PCSK9 Improved Renal Fibrosis by Regulating Fatty Acid β‐Oxidation. Journal of the American Heart Association: Cardiovascular and Cerebrovascular Disease, 9(1), e014358.

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Magnetic Tweezers Assay for G4 Structures

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A flow chamber was established on a (3-aminopropyl) triethoxy silane (APTES; Sigma-Aldrich) functionalized coverslip 32 × 24 mm in size. The thiol-end of DNA was covalently attached to the amine group of APTES through a sulfo-SMCC crosslinker (ThermoFisher Scientific). The chamber was then blocked with BSB solution (1 × phosphate buffered saline buffer containing 2% BSA, 0.02% Tween-20, and 0.1 g/l NaN₃) before introducing 2.7 μm diameter streptavidin-coated paramagnetic beads. Unfolding and refolding assays were carried out at 22°C in a buffer of 10 mM Tris–HCl (pH 8.0), 100 mM KC1, 4 mM MgCl₂ and 1 U/μl, Ribolock RNase inhibitor (EO0382, ThermoFisher Scientific, USA). The extension change of the construct was detected from the diffraction pattern of the bead recorded using a CCD camera that acquired ∼200 frames per second. Force was controlled by changing the distance between the permanent magnets and the functionalized flow chamber. The magnetic tweezers have a spatial resolution for beads stuck on the surface of ∼2 nm, and the force calibration has a relative error of <10%. All experiments were carried out at 22°C, and the temperature was controlled by a thermostat. The unfolding and refolding of the G4 structures were reflected by the abrupt change of the height of the magnetic ball.

Fang P., Xie C., Pan T., Cheng T., Chen W., Xia S., Ding T., Fang J., Zhou Y., Fang L., Wei D, & Xiao S. (2023). Unfolding of an RNA G-quadruplex motif in the negative strand genome of porcine reproductive and respiratory syndrome virus by host and viral helicases to promote viral replication. Nucleic Acids Research, 51(19), 10752-10767.

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Anti-S scFV-Linker-hIgG1Fcmut Antibody Modification

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The anti-S scFV-Linker-hIgG1Fcmut
antibodies (MoMAb) used to capture subviral particles and HBV virions
were previously described and characterized.^{25 (link)} Large-scale production was contracted to InVivo Biotech Services
GmbH. The produced antibodies were modified with a 26 bp DNA sequence
complementary to the handle sequence inside the nanoshells (Table 1).
The modification was accomplished by connecting the
thiol-modified
DNA strand to the antibody via a sulfo-SMCC cross-linker from Thermo
Scientific, using a ratio of antibody/DNA strand of 1:7 (Figures S2 and S3 of
the Supporting Information). The resulting mixture was purified using
the ion-exchange chromatography system proFire by Dynamic Biosensors.

Willner E.M., Kolbe F., Momburg F., Protzer U, & Dietz H. (2024). Hepatitis B Virus Neutralization with DNA Origami Nanoshells. ACS Applied Materials & Interfaces, 16(20), 25836-25842.

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