Log In Sign up
The largest database of trusted experimental protocols

Zeba spin desalting plates

Manufactured by Thermo Fisher Scientific
Visit Supplier
Sourced in United States

The Zeba Spin Desalting Plates are a size-exclusion chromatography-based product designed for the rapid and efficient desalting and buffer exchange of protein samples. The plates contain a hydrophilic resin that allows for the separation of proteins from small molecules, salts, and other contaminants.

Automatically generated - may contain errors

Lab products found in correlation

Nanodrop, by Thermo Fisher Scientific (2 mentions) Sulfo smcc, by Thermo Fisher Scientific (1 mentions) Slide a lyzer mini dialysis device, by Thermo Fisher Scientific (1 mentions) Dithiothreitol (dtt), by Merck Group (1 mentions) Mabselect sure resin, by Cytiva (1 mentions) Hitrap mabselect sure column, by Cytiva (1 mentions) Amicon ultra 4 50 kda centrifugal filter units, by Merck Group (1 mentions) Trypsin from bovine pancreas, by Merck Group (1 mentions) Pierce albumin depletion kit, by Thermo Fisher Scientific (1 mentions) Trypsin, by Merck Group (1 mentions) Deep well plate, by Eppendorf (1 mentions) Biologic biofrac fraction collector, by Bio-Rad (1 mentions)

Close spelling variants of this product

Zeba 7K spin desalting plates Zeba Spin plates Zeba plates

5 protocols using zeba spin desalting plates

1

Conjugation of Oligonucleotides to Antibodies

Check if the same lab product or an alternative is used in the 5 most similar protocols
The conjugation of oligonucleotides to antibodies (Supplementary table 2) was performed as follows: Twenty μg of each antibody was activated by adding 1 μl of 4 mM Sulfo-SMCC (Thermo Scientific) in dimethyl sulfoxide (DMSO; Sigma–Aldrich), and incubating at room temperature (RT) for 2 h. After 1 h of antibody activation, 3 μl of each 5’ thiol-modified oligonucleotide at a concentration of 100 μM was reduced by adding 12 μl of 100 mM DTT (Sigma–Aldrich) in 1x PBS with 5 mM EDTA, and incubating at 37 °C for 1 h. The activated antibodies and reduced oligonucleotides were separately purified using Zeba Spin Desalting Plates, 7 K MWCO (Thermo Scientific) according to the manufacturer’s recommended procedure. Each purified antibody was then mixed with one type of oligonucleotide (Supplementary Table 1), and directly followed by dialysis in a Slide-A-Lyzer MINI Dialysis Device, 7 K MWCO, 0.1 ml (Thermo Scientific) against 5 l PBS with constant stirring by a magnetic bar at 4 °C overnight. The conjugates were stored at 1 μM antibody concentration in PBS with 0.1% BSA at 4 °C.
Wu D., Yan J., Shen X., Sun Y., Thulin M., Cai Y., Wik L., Shen Q., Oelrich J., Qian X., Dubois K.L., Ronquist K.G., Nilsson M., Landegren U, & Kamali-Moghaddam M. (2019). Profiling surface proteins on individual exosomes using a proximity barcoding assay. Nature Communications, 10, 3854.
+ Open protocol
+ Expand
2

Polymer Purification via Zeba Spin Desalting

Check if the same lab product or an alternative is used in the 5 most similar protocols
For purification of polymers, Zeba™ spin desalting plates (Thermo Fisher Scientific) were manually loaded with Sephadex G-25 superfine resin which has a molecular weight cutoff (MWCO) of 5 kDa. The resin was stored in DMSO for 6 hours to swell prior to use. The protocol which includes wash steps, sample loading volumes, and centrifugation rate was consistent with a previous study from our group.54 Purified polymers were diluted 3x in DMSO and then an additional 3x in ultrapure water. Diluted polymers were then dialyzed using Spectra/Por regenerated cellulose pre-wetted dialysis tubing (Repligen) with a MWCO of 1 kDa. Dialysis was completed after 12 hours, at which point polymers were lyophilized in 15 mL centrifuge tubes.
Upadhya R., Punia A., Kanagala M.J., Liu L., Lamm M., Rhodes T.A, & Gormley A.J. (2021). Automated PET-RAFT Polymerization Towards Pharmaceutical Amorphous Solid Dispersion Development. ACS applied polymer materials, 3(3), 1525-1536.
+ Open protocol
+ Expand
3

Parallel Production of Recombinant mAbs

Cited 1 time
Check if the same lab product or an alternative is used in the 5 most similar protocols
For parallel production of recombinant mAbs, we used approaches designated as ‘micro-scale’ or ‘midi-scale’ (26 (link)). For ‘micro-scale’ mAbs expression, we performed transfection (~1 mL per antibody) of CHO cell cultures using a protocol for deep 96-well blocks (Thermo Fisher Scientific), as we previously described (26 (link)). For high-throughput micro-scale mAb purification, clarified culture supernatants were incubated with MabSelect SuRe resin (Cytiva), washed with PBS, eluted, buffer-exchanged into PBS using Zeba Spin Desalting Plates (Thermo Fisher Scientific) and stored at 4°C until use. For ‘midi-scale’ mAbs expression, we performed transfection (~35 mL per antibody) of CHO cell cultures as described by the vendor. MAbs were purified form culture supernatants using HiTrap MabSelect SuRe columns (Cytiva). Purified mAbs were buffer-exchanged into PBS, concentrated using Amicon Ultra-4 50 KDa Centrifugal Filter Units (Millipore Sigma) and stored at 4°C until use. To quantify purified mAbs, absorption at 280 nm (A280) was measured using a NanoDrop (Thermo Fisher Scientific).
Gilchuk P., Guthals A., Bonissone S.R., Shaw J.B., Ilinykh P.A., Huang K., Bombardi R.G., Liang J., Grinyo A., Davidson E., Chen E.C., Gunn B.M., Alter G., Saphire E.O., Doranz B.J., Bukreyev A., Zeitlin L., Castellana N, & Crowe JE J.r. (2021). Proteo-Genomic Analysis Identifies Two Major Sites of Vulnerability on Ebolavirus Glycoprotein for Neutralizing Antibodies in Convalescent Human Plasma. Frontiers in Immunology, 12, 706757.
+ Open protocol
+ Expand
4

Serum Proteomic Sample Preparation

Check if the same lab product or an alternative is used in the 5 most similar protocols
Serum samples were desalted using Zeba™ Spin desalting plates (Thermo Scientific, MA, USA) prior to 50 μL aliquots being depleted of excess albumin using the Pierce™ albumin depletion kit (ThermoFisher Scientific, MA, USA). The remaining protein concentration was determined using the Bradford MX Protein Assay (Expedeon, Germany), after which the samples were dried then resuspended with 35 μL 6 M urea, then as previously described by Kontro et al., reduced, then alkylated prior to trypsin digestion.
24 (link) The samples were diluted 1:10 with 50 mM Tris solution to reduce the urea concentration; then trypsin (from bovine pancreas [Sigma Aldrich, MO, USA]) was added at a mass ratio of 1:50 and incubated at 37°C overnight. These samples were then dried and frozen at −72°C until further use.
Dickinson A., Joenväärä S., Tohmola T., Renkonen J., Mattila P., Carpén T., Mäkitie A, & Silén S. (2023). Altered microheterogeneity at several N‐glycosylation sites in OPSCC in constant protein expression conditions. FASEB BioAdvances, 6(1), 26-39.
+ Open protocol
+ Expand
5

Venom Protein Fractionation and Cytotoxicity Screening

Check if the same lab product or an alternative is used in the 5 most similar protocols
Venom components were separated using anion-exchange chromatography followed by size exclusion chromatography. For anion-exchange chromatography, a similar process was applied as described previously 15 (link). Briefly, venom proteins from ~1000 venom reservoirs were loaded on Bio SAX column (5 μm, 4.6 × 50 mm, Agilent, USA) using a Biologic Duo-Flow high-performance chromatography system (Bio-rad, Germany). Proteins were eluted at a flow rate of 0.5 ml/min with a gradient of buffer B (25 mM Tris-HCl, 1 M NaCl, pH = 7.5) against buffer A (25 mM Tris-HCl, pH = 7.5). Protein level was monitored by absorbance at 280 nm. Fractions of 200 μl were collected in a deep well plate (Eppendorf, Germany) using the BioLogic BioFrac fraction collector (Bio-rad, Germany), then desalted using Zeba spin desalting plates (Thermo Scientific, USA). Fractions 56 and 57, which showed the highest cytotoxicity on Hi-5 cells, were pooled for further size exclusion chromatography using Agilent Bio SEC columns (3 μm, 300 A, 4.6 × 300 mm) at a flow rate of 0.2 ml/min using PBS as the running buffer. Protein level was monitored by absorbance at 214 nm. The fraction with cytotoxicity was pooled and subjected to SDS-PAGE.
Wang J., Yan Z., Xiao S., Wang B., Fang Q., Schlenke T, & Ye G. (2020). Characterization of a cell death-inducing endonuclease-like venom protein from the parasitoid wasp Pteromalus puparum (Hymenoptera: Pteromalidae). Pest management science, 77(1), 224-233.
+ Open protocol
+ Expand

About PubCompare

Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.

We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.

However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.

Ready to get started?

Sign up for free.
Registration takes 20 seconds.
Available from any computer
No download required

Sign up now

Revolutionizing how scientists
search and build protocols!