Ni-NTA MagBeads für die His-tagged Proteinreinigung
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Produktinformationen "Ni-NTA MagBeads für die His-tagged Proteinreinigung"
Protein purification based on magnetic beads has become popular because they are useful to extract proteins from diluted solutions, such as cell culture supernatants purify proteins expressed at low levels perform pull-down experiments We use magnetic beads with a ferrimagnetic core and an agarose coating coupled to a ligand of choice, our beads meet our own high quality standards. They enable fast and easy purification steps, which can be automated. The amount of magnetic beads used for a purification setup can be easily scaled up and down to match protein expression rates and culture volumes. Genaxxon MagBeads are ferrimagnetic agarose beads coupled to a chelating ligand (IDA or NTA) coordinating nickel or cobalt ions. All offered ligand-metal systems efficiently bind histidine-tagged proteins. With a binding capacity of up to 40mg protein per mL (Ni-IDA) and 70mg per mL (Ni-NTA) of settled MagBeads, Genaxxon Ni-IDA MagBeads are comparable to equivalent beads from alternative providers.
Specifications:
Protein binding capacity: up to 70mg/mL settled beads
Metal capacity: >12µeqv Ni2+/mL
Possible metal ions: Co2+, Zn2*, Fe3+, Al3+ and Cu2+
Microbial preservative: 20% ethanol
Delivered as a 25% suspension (1mL suspension will result in 250µL gel bed volume). Suspension contains 20% ethanol as a microbial preservative.
Applikation / Application:
Affinity chromatography, Purification of recombinant Proteins carrying a polyhistidine tagQuelle / Source:
syntheticKlassifizierungen / Classification
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Quelle: NCBI PubMed
Retinol and ascorbate drive erasure of epigenetic memory and enhance reprogramming to naïve pluripotency by complementary mechanisms
Timothy Alexander Hore, Ferdinand von Meyenn, Mirunalini Ravichandran, Martin Bachman, Gabriella Ficz, David Oxley, Fátima Santos, Shankar Balasubramanian, Tomasz P. Jurkowski, Wolf Reik
Proc Natl Acad Sci U S A. 2016 Oct 25; 113(43): 12202–12207.
doi: 10.1073/pnas.1608679113
PMCID: PMC5086989
The UHRF1 Protein Stimulates the Activity and Specificity of the Maintenance DNA Methyltransferase DNMT1 by an Allosteric Mechanism
Pavel Bashtrykov, Gytis Jankevicius, Renata Z. Jurkowska, Sergey Ragozin, Albert Jeltsch
J Biol Chem. 2014 Feb 14; 289(7): 4106–4115.
doi: 10.1074/jbc.M113.528893
PMCID: PMC3924276
