Pd 10 prepoured gel filtration columns

Manufactured by GE Healthcare

The PD-10 prepoured gel-filtration columns are laboratory equipment designed for size-exclusion chromatography. These columns are pre-packed with a gel matrix that separates molecules based on their size as they pass through the column. The core function of the PD-10 columns is to facilitate the rapid and efficient purification and desalting of proteins, peptides, and other macromolecules from complex mixtures.

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Lab products found in correlation

Nuclease p1 from penicillium citrinum, by Merck Group (2 mentions) Vent polymerase, by New England Biolabs (2 mentions) Talon metal affinity resin, by Takara Bio (1 mentions) Cobalt talon resin, by Takara Bio (1 mentions) Antarctic phosphatase, by New England Biolabs (1 mentions)

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PD-10 column (853 citations) PD-10 (119 citations) PD-10 gel filtration column (26 citations) Gel filtration columns (7 citations)

2 protocols using pd 10 prepoured gel filtration columns

Enzymatic Synthesis and Purification of Isotopically Labeled RNA

Cited 1 time

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Vent polymerase and Antarctic phosphatase
were purchased from New England Biolabs (Ipswich, MA). Nuclease P1
from Penicillium citrinum was purchased
from Sigma-Aldrich (St. Louis, MO). All oligonucleotide primers were
obtained from Integrated DNA Technologies (Coralville, IA) and used
as received. Talon metal affinity resin was purchased from Clontech
(Mountain View, CA). PD-10 prepoured gel-filtration columns were purchased
from GE Biosciences (Piscataway, NJ). S-Adenosylmethionine
and S-adenosyl-[methyl-¹³C]methionine were synthesized enzymatically and purified as described
previously.^{27 (link)} [2-²H]Adenosine
triphosphate (97% enrichment) was purchased from Cambridge Isotopes
(Andover, MA). The 155-mer and [2-²H]A-155-mer RNA substrates
(encompassing positions 2454–2608 of E. coli 23S rRNA) were prepared using runoff transcription as previously
described.^{25 (link)}Ec flavodoxin
(Fld) and flavodoxin reductase (Flx) were purified as previously described.^{28 (link)}

Silakov A., Grove T.L., Radle M.I., Bauerle M.R., Green M.T., Rosenzweig A.C., Boal A.K, & Booker S.J. (2014). Characterization of a Cross-Linked Protein–Nucleic Acid Substrate Radical in the Reaction Catalyzed by RlmN. Journal of the American Chemical Society, 136(23), 8221-8228.

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Enzymatic Synthesis and Purification of Methyl Donor Compounds

Cited 1 time

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Vent polymerase and Antarctic phosphatase were purchased from New England Biolabs (Ipswich, MA). Nuclease P1 from Penicillium citrinum was purchased from Sigma-Aldrich (St. Louis, MO). All oligonucleotide primers were obtained from Integrated DNA Technologies (Coralville, IA) and used as received. Talon cobalt-resin was purchased from Clontech (Mountain View, CA). PD-10 pre-poured gel-filtration columns were purchased from GE Biosciences (Piscataway, NJ). S-Adenosylmethionine (SAM) and S-adenosyl[methyl-d₃]methionine (d₃-methyl-SAM) were synthesized enzymatically and purified as described previously.^{15 (link) 2}H₈-adenosine 5’-triphosphate (90% D) was purchased from Cambridge Isotopes (Andover, MA). RNA substrates (155mer, deu155mer, 16mer, deu16mer) were prepared using run-off transcription as previously described.^{9 (link)}E. coli flavodoxin and flavodoxin reductase were generated as previously described.^{16 (link)}

Bauerle M.R., Grove T.L, & Booker S.J. (2018). Investigation of Solvent Hydron Exchange in the Reaction Catalyzed by the Antibiotic Resistance Protein, Cfr. Biochemistry, 57(30), 4431-4439.

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