Sodium acetate

Manufactured by GE Healthcare

Sodium acetate is a chemical compound commonly used in laboratory settings. It serves as a buffer agent, maintaining a stable pH in various analytical and experimental procedures. The product is a white, crystalline solid that is soluble in water and other polar solvents. Sodium acetate is widely employed in fields such as biochemistry, analytical chemistry, and life sciences, where precise control of pH is critical for successful experimentation and analysis.

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Lab products found in correlation

Biacore 3000, by GE Healthcare (2 mentions) Hbs ep running buffer, by GE Healthcare (1 mentions) Cd3d cd3e heterodimer, by Sino Biological (1 mentions) Biacore 8k, by GE Healthcare (1 mentions) Surfactant p20, by GE Healthcare (1 mentions) Glycine hcl, by GE Healthcare (1 mentions) Hbs ep buffer, by GE Healthcare (1 mentions)

3 protocols using sodium acetate

Characterizing TF-TCB Binding Kinetics

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The affinities and kinetics of the TF-TCB binding to CD3D × CD3E and TF antigen were evaluated by surface plasmon resonance (Biacore 8K, GE Healthcare Life Sciences). TF-011, an anti-TF antibody sharing the same TF binding moieties with the TF-TCB, was used as control²¹ (link). CD3D × CD3E heterodimer (Sino Biological, Beijing, China) or the TF antigen (Peprotech, Rocky Hill, NJ, USA) was immobilized to CM5 chip surface using routine 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide/N-hydroxysuccinimide amine coupling protocols. The immobilization buffer was 10 mmol/L sodium acetate (pH 4.5, GE Healthcare Life Sciences). Surface densities after immobilization ranged from 50 to 100 RU. Two-fold serial dilutions of antibodies (TF-TCB or TF-011) ranging from 0.318 to 162.8 nmol/L in HBS-EP running buffer (GE Healthcare Life Sciences) were used to analyze binding. Running buffer alone was used as a zero reference. The antibodies were injected for 200 s followed by 180 s of dissociation time. Surface was regenerated by 0.1 mol/L glycine (pH 1.5) for 30 s. Data were analyzed using a 1:1 Langmuir binding model to calculate the kinetics and binding constants.

Pan Z., Chen J., Xiao X., Xie Y., Jiang H., Zhang B., Lu H., Yuan Y., Han L., Zhou Y., Zong H., Wang L., Sun R, & Zhu J. (2021). Characterization of a novel bispecific antibody targeting tissue factor-positive tumors with T cell engagement. Acta Pharmaceutica Sinica. B, 12(4), 1928-1942.

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Biacore-based Binding Kinetics Analysis

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Studies were performed on Biacore 3000 (GE Healthcare). GST–hTIM-3 protein, or GST alone as control, was immobilized on a CM5 sensor chip using amine coupling chemistry as per the manufacturer’s instructions. The coupling was performed by injecting 30 µg ml⁻¹ of protein into 10 mM sodium acetate, pH5.0 (GE Healthcare). HBS-EP buffer (0.01 M HEPES, 0.15 M NaCl, 3 mM EDTA, 0.005% surfactant P20; GE Healthcare) was used as running buffer and dilution buffer. Serial dilutions of analytes in HBS-EP were injected at 25 °C with a 25 µl min⁻¹ flow rate and data collected over time. The surface was regenerated between different dilutions with 10 mM glycine-HCl, pH2.5 (GE Healthcare). For blockade of single-chain binding to GST–hTIM-3, single-chain hCEACAM1– hTIM-3 protein was injected alone or together with antibody (anti-human CEACAM1 monoclonal antibody, 26H7) or TIM-3-specific peptide (residues 58–77, 58-CPV FECGNVVLRTDERDVNY-77) with IgG1 mouse antibody or scrambled peptide (TLCVCFVNPYDVRVNDEREG) used as controls, respectively. All data were zero adjusted, and the reference cell value was subtracted.

Huang Y.H., Zhu C., Kondo Y., Anderson A.C., Gandhi A., Russell A., Dougan S.K., Petersen B.S., Melum E., Pertel T., Clayton K.L., Raab M., Chen Q., Beauchemin N., Yazaki P.J., Pyzik M., Ostrowski M.A., Glickman J.N., Rudd C.E., Ploegh H.L., Franke A., Petsko G.A., Kuchroo V.K, & Blumberg R.S. (2014). CEACAM1 regulates TIM–3–mediated tolerance and exhaustion. Nature, 517(7534), 386-390.

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Kinetic Analysis of h9C12-TRIM21 Interaction

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A Biacore 3000 instrument (GE Healthcare) was used for all kinetics measurements. h9C12 variants were immobilized by amine coupling on CM5 sensor chips, according to the manufacturer’s instructions. The coupling was performed by injecting 1–2.5 µg/ml the IgG1 variants dissolved in 10 mM sodium acetate (pH 4.5) (GE Healthcare). HBS-P buffer (0.01 M HEPES, 0.15 NaCl, 0.005% surfactant P20 [pH 7.4]) was used as running and dilution buffer. Subsequently, concentration series of recombinant human TRIM21 PRYSPRY were injected. Kinetics analysis was performed using BIAevaluation software, and the binding data were fitted to a simple first-order (1:1) Langmuir biomolecular interaction model. Steady-state K_D values were obtained by immobilizing h9C12 variants at ~2500 RU and determined by an equilibrium (Req) binding model.

Foss S., Watkinson R.E., Grevys A., McAdam M.B., Bern M., Høydahl L.S., Dalhus B., Michaelsen T.E., Sandlie I., James L.C, & Andersen J.T. (2016). TRIM21 Immune Signaling Is More Sensitive to Antibody Affinity Than Its Neutralization Activity. Journal of immunology (Baltimore, Md. : 1950), 196(8), 3452-3459.

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