Seldi tof

Manufactured by Bio-Rad

Sourced in United States

The SELDI-TOF (Surface-Enhanced Laser Desorption/Ionization Time-of-Flight) is a mass spectrometry-based analytical instrument developed by Bio-Rad. It is designed to detect and analyze proteins in complex biological samples. The SELDI-TOF utilizes a protein chip array to selectively capture proteins, which are then ionized and detected by a time-of-flight mass spectrometer. This technique allows for the identification and relative quantification of proteins in the sample.

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Lab products found in correlation

Phastsystem, by GE Healthcare (1 mentions) Protein chip datamanager 3, by Bio-Rad (1 mentions)

2 protocols using seldi tof

Characterization of scFvD2B Antibody Fragment

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The scFvD2B used in this study was produced in GMP-compliant conditions in a eukaryotic system (ExcellGene) starting from a clone in which the Myc tag and His tag were removed. The antibody fragment was purified using a HiTrap Protein L chromatography column (GE Healthcare Life Sciences) according to the manufacturer's instructions and characterized for integrity and biochemical and biological activity as described elsewhere [13 (link), 16 (link)].
The theoretical and experimental molecular weight (MW) and isoelectric point (pI) of scFvD2B produced in a prokaryotic system and an eukaryotic system were determined. The theoretical values were obtained using the ExPASy tool (http://web.expasy.org/compute_pi/); experimental MW and pI were calculated by SELDI-TOF (Bio-Rad laboratories) analysis and isoelectrofocusing gel (pH 3-9) using the PhastSystem (GE Healthcare Life Sciences), respectively.

Frigerio B., Franssen G., Luison E., Satta A., Seregni E., Colombatti M., Fracasso G., Valdagni R., Mezzanzanica D., Boerman O., Canevari S, & Figini M. (2016). Full preclinical validation of the 123I-labeled anti-PSMA antibody fragment ScFvD2B for prostate cancer imaging. Oncotarget, 8(7), 10919-10930.

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SELDI-TOF Mass Spectrometry Protocol

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The ProteinChips were analyzed using a linear TOF mass spectrometer SELDI‐TOF (BioRad Laboratories, USA), with the following protocols. Protocol A: laser power 3000 nJ, matrix attenuation 2700, focus mass 12,500, sample rate 600 and 50% spot surface fired for ion profiling between the mass/charge (m/z) range of 0–25,000. Protocol B: laser power 5000 nJ, matrix attenuation 2500, focus mass 30,000, sample rate 600 and 50% spot surface fired for ion profiling between the mass/charge (m/z) range of 25,000–50,000. We have used the ProteinChip Data Manager 3.5 software (BioRad Laboratories), and the spectra were externally calibrated with ProteinChip all‐in‐one peptide standard (BioRad Laboratories). We have processed the spectra through baseline subtraction and smoothing. The mass has been aligned and normalized using the total ion current within the m/z range of 3–30 kDa for the low mass proteins and 25–50 kDa for the high mass proteins.

Nardone D., Ciaramella A., Cerreta M., Pulcrano S., Bellenchi G.C., Leone L., Manco G, & Febbraio F. (2021). Selymatra: A web application for protein‐profiling analysis of mass spectra. Biotechnology and Applied Biochemistry, 69(5), 1821-1829.

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