Optimizing GFP Protein Purification: STARTER Anti-GFP Nanobody Agarose Beads for Enhanced Efficiency

Green Fluorescent Protein (GFP), originally isolated from the jellyfish Aequorea victoria, is a structurally unique protein exhibiting intrinsic autofluorescence properties. This 238-amino acid protein demonstrates the remarkable capability to absorb light energy at specific wavelengths (typically blue or ultraviolet light) and subsequently emit green fluorescence through an internal chromophore formation process.

Crystal Structure of GFP

Featured Product:

STARTER Anti-GFP Nanobody Agarose Beads (Catalog : S0B1843)

Background:

Anti-GFP nanobody agarose beads is an affinity chromatography medium designed for easy, one-step purification of recombinant GFP fusion proteins in E. coli, insect cells and mammalian cells. The recombinant GFP fusion proteins can be purified directly from pre-treated cell lysate using Anti-GFP nanobody agarose beads. It is the excellent choice for high performance purifications.

Product Advantages:

Structural Stability - Resistant to fragmentation with no contamination from conventional antibody light or heavy chains

Chemical Robustness - Tolerant to high temperatures and stringent incubation/elution conditions

High Affinity - Exceptional binding capacity with minimal target protein dissociation, significantly reducing processing time

Product Specifications

Validation Data:

Anti-GFP Nanobody Agarose Beads is used to immunoprecipitated GFP-fusion proteins from Escherichia coli lysate supernatant. During elution with Acidic elution buffer, the enriched GFP-fusion proteins are released from Anti-GFP Nanobody Agarose Beads.

SDS-PAGE analysis was performed.

Lane 1: Input

Lane 2: Flow-through

Lane 3: GFP-fusion protein eluted by acidic buffer

Lane 4: Agarose Beads after elution

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