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Votre recherche pour: Protéines purification

Protein purification systems are intended to isolate one or multiple proteins from a complex mixture. Working with cells, tissues, or whole organisms, the machines purify with predefined start points and editable method templates. With a single click, the compact designed equipment offers real-time run control and visualization. Suitable for even cold-room operations, the products enable you to perform purification of affinity-tagged proteins, antibodies, untagged or native proteins, as well as sample clean-up.

Protein purification systems are intended to isolate one or multiple proteins from a complex mixture. Working with cells, tissues, or whole organisms, the machines purify with predefined start points and editable method templates. With a single click, the compact designed equipment offers real-time run control and visualization. Suitable for even cold-room operations, the products enable you to perform purification of affinity-tagged proteins, antibodies, untagged or native proteins, as well as sample clean-up.


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Fournisseur: Merck
Description: Ion Exchanger I is a strong acid cation exchangers widely used in separation of noble earths and amino acids, water treatment, analysis and food industry. The bond strength of equivalent ions increases with decreasing diameter of the hydrated ion.
Fournisseur: Avantor
Description: Les plaques d’extraction liquide (SLE) J.T.Baker® BAKERBOND® constituent une alternative idéale et plus rapide aux méthodes d’extractions traditionnelles liquide-liquide, et elles permettent une récupération excellente des analytes des matrices biologiques.

Fournisseur: Avantor
Description: J.T.Baker® BAKERBOND® protein precipitation plates enable fast protein removal from biological samples.

Fournisseur: Avantor
Description: The J.T.Baker<sup>®</sup> BAKERBOND<sup>®</sup> PROchievA™ protein A resin offers superior dynamic binding capacity with excellent alkaline stability linked to Avantor's proprietary ligand.
Fournisseur: Avantor
Description: Silica-based media used for the purification of proteins based on differential salt induced hydrophobicity. Mixed mode provides unique selectivity with its hydrophobic interaction and ion exchange function.
Fournisseur: G-Biosciences
Description: Glutathione resin is designed for the affinity purification of proteins with a glutathione S-transferase (GST) tag. The resin consists of reduced glutathione (GSH) covalently coupled to 4% cross-linked agarose, via a 10-carbon spacer arm. The resin has a binding capacity of ~8 mg GST/ml resin. Supplied as slurry in 20% ethanol.

Fournisseur: G-Biosciences
Description: Cobalt chelating resin, 0,2 ml columns, for the purification of 6X His proteins

Référence Produit: (IMMRIR1013)
Fournisseur: ImmunoReagents
Description: ImmunoReagents Mouse IgG Affinity Prep resins are prepared using highly purified species specific immunoglobulins. This resin is suitable for removal of proteins recognising Mouse IgG from liquid solutions, including traditional Immunoabsorptions and Immunoprecipitation protocols.
UOM: 1 * 2 mL


Fournisseur: G-Biosciences
Description: This avidin resin is designed for the single step small and large scale affinity purification of proteins and antibodies with a biotin tag. The resin can also be used for immunoprecipitations using biotin labelled antibodies.

Fournisseur: G-Biosciences
Description: Thiophilic adsorption or thiophilic chromatography is a routinely used technique for the low cost, simple purification of immunoglobulins. Thiophilic adsorption was first developed by Porath et al in 1984 and is a group specific, salt-dependent purification technique that has distinct affinity towards immunoglobulins and α2- macroglobulins. The thiophilic adsorption works on the principle that some proteins in high salt are able to bind to an immobilised ligand that contains a sulfone group in proximity to a thioether group. The bound proteins are then eluted in decreasing salt concentrations. The thiophilic resin binds immunoglobulins, including IgG, IgY and IgM, from serum, ascites or tissue culture supernatants and the purified immunoglobulins are then eluted in a near neutral aqueous buffer.

Fournisseur: AGILENT
Description: The affinity removal spin cartridge reagent kit is designed to remove the most interfering high-abundant protein (albumin) from human samples (such as plasma, serum, urine or cerebrospinal fluid).

Référence Produit: (IMMRIR1008)
Fournisseur: ImmunoReagents
Description: ImmunoReagents Chicken IgY Affinity Prep resins are prepared using highly purified species specific immunoglobulins. This resin is suitable for removal of proteins recognising Chicken IgY from liquid solutions, including traditional Immunoabsorptions and Immunoprecipitation protocols.
UOM: 1 * 2 mL


Fournisseur: G-Biosciences
Description: For the rapid purification of soluble, 6X His or GST tagged proteins.

Fournisseur: G-Biosciences
Description: Immobilised Protein A and G are designed for binding the constant domains of immunoglobulin (Ig) molecules. Immobilised Protein A is coupled to 6% highly cross-linked agarose beads by a proprietary coupling method that provides high coupling efficiency for immunoglobulins and minimal protein A leaching. The binding capacity of Protein A is 18 to 43 mg Human IgG per ml resin.
Fournisseur: G-Biosciences
Description: STRATEGY™ is designed to allow researchers to rapidly screen a number of purification techniques in a small scale format to identify the system to isolate their protein of interest. The self-contained kit allows researchers to save time and money as separate buffers, resins and columns are not needed.

Fournisseur: G-Biosciences
Description: Streptavidin Resin is designed for the single step small and large scale affinity purification of proteins and antibodies with a biotin tag. Biotin, a 244 Da vitamin (Vitamin H) molecule, exhibits an extraordinary binding affinity for avidin (Ka=10¹⁵ M⁻¹) and streptavidin (Ka=10¹⁵ M⁻¹). Biotin and (strept)avidin interaction is rapid and once the bond is established it can survive up to 3M guanidinehydrochloride and extremes of pH. Biotin-avidin bonds can only be reversed by denaturing the avidin protein molecule with 8M guanidine-hydrochloride at pH 1,5 or by autoclaving. The biotinylated molecules are efficiently probed with avidin or streptavidin conjugated to reporter molecules, such as peroxidases or phosphatases.

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