S1421S,  Hydrophilic Streptavidin Magnetic Beads - 5 ml

S1421S, Hydrophilic Streptavidin Magnetic Beads - 5 ml

S1423S,  Ni-NTA Magnetic Beads - 1 ml

S1423S, Ni-NTA Magnetic Beads - 1 ml

S1423L, Ni-NTA Magnetic Beads - 5 ml

6.309,38 RON

An affinity matrix for the small-scale isolation and purification of polyhistidine-tagged (His-tagged) fusion proteins in manual or automated formats.

SKU
NEB_S1423L

An affinity matrix for the small-scale isolation and purification of polyhistidine-tagged (His-tagged) fusion proteins in manual or automated formats. Immobilized Metal Affinity Chromatography (IMAC) purifications employing Ni-NTA (nickel-nitrilotriacetic acid) magnetic beads can be performed under native or denaturing conditions which permit efficient binding and purification of insoluble proteins, proteins that aggregate in inclusion bodies, or proteins that possess a tertiary structure that sequester the polyhistidine affinity tag. Immobilized His-tagged proteins can be used in subsequent experiments to pull-down proteins that may interact with the immobilized protein.

  • Prepared with agarose based, super-paramagnetic microparticles which provide high binding capacity and fast magnetic response permitting high throughput and scalable purification strategies of His tagged-fusion proteins.
  • NTA coordination exhibits low Nickel ion leaching.
  • Tolerates a wide range of conditions, including the presence of protein denaturants and detergents. Compatible with commercially available detergent based cell lysis reagents.
  • Elution of the target protein may be achieved by protonation, ligand exchange (with imidazole) or extraction of the metal ion by a stronger chelator (e.g. EDTA).
  • Extremely low non-specific binding properties permit immobilized fusion proteins to be used in subsequent experiments to capture or pull down interacting proteins from crude cell lysates

 

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Description

An affinity matrix for the small-scale isolation and purification of polyhistidine-tagged (His-tagged) fusion proteins in manual or automated formats. Immobilized Metal Affinity Chromatography (IMAC) purifications employing Ni-NTA (nickel-nitrilotriacetic acid) magnetic beads can be performed under native or denaturing conditions which permit efficient binding and purification of insoluble proteins, proteins that aggregate in inclusion bodies, or proteins that possess a tertiary structure that sequester the polyhistidine affinity tag. Immobilized His-tagged proteins can be used in subsequent experiments to pull-down proteins that may interact with the immobilized protein.

  • Prepared with agarose based, super-paramagnetic microparticles which provide high binding capacity and fast magnetic response permitting high throughput and scalable purification strategies of His tagged-fusion proteins.
  • NTA coordination exhibits low Nickel ion leaching.
  • Tolerates a wide range of conditions, including the presence of protein denaturants and detergents. Compatible with commercially available detergent based cell lysis reagents.
  • Elution of the target protein may be achieved by protonation, ligand exchange (with imidazole) or extraction of the metal ion by a stronger chelator (e.g. EDTA).
  • Extremely low non-specific binding properties permit immobilized fusion proteins to be used in subsequent experiments to capture or pull down interacting proteins from crude cell lysates