Allele Biotechnology社 GFPと特異的に結合するVHH抗体　GFP-nAb

GFP融合タンパク質を特異的かつ簡単に単離可能　(GFP-nAb)

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Optimized by the research team at Allele Biotechnology, GFP-nAb™ is a highly specific GFP (Green Fluorescent Protein) binding protein derived from camelids. It is characterized by a small barrel shaped structure (13 KDa, 2.5nm X 4.5 nm) and a very high stability (stable up to 70°C, functional within 2M NaCl or 0.5% SDS). Experiments have shown that one molecule of GFP-nAb™ binds one molecule of GFP with a dissociation constant (Kd) in the sub nanomolar range. This makes GFP-nAb™ the ideal candidate for a variety of biological assays, some of which are listed below:

• Immunoprecipitation / CO-IP
• Quantitative analysis
• Chromatin Immunoprecipitation (ChIP)
• Superresolution Imaging

GFP-nAb™ binds a large number of commonly used fluorescent proteins derived from the original Aequorea victoria GFP, including EGFP, Venus, Cerulean, and EBFP2 (full list coming soon). Conveniently, it displays no binding affinity to non-jellyfish-derived fluorescent proteins, including the "mFruits" such as mCherry, or Allele's mNeonGreen, mTFP1, mWasabi, and mMaple fluorescent proteins. The GFP-nAb™ Spin Kit offers a simple, consistent protocol to cleanly pull down GFP fusions. Each GFP-nAb™ Spin Kit comes with all required buffers and spin columns to eliminate inconsistent elutions and allow you to perform multiple immunoprecipiation reactions in a matter of minutes.

Complete Pulldown using the GFP-nAb™ Spin Kit.

EGFP-expressing Sf9 (insect) cell lysate contained a total of 16µg of EGFP in total volume of 500µl, determined spectrophotometrically. Following the GFP-nAb™ Spin Kit binding and wash protocols, the protein was eluted in 2 x 50 µl elution buffer (0.2M glycine pH 2.5), pooled, and neutralized with 10µl of 1M Tris base. Equal volumes of lysate input (I), flow-through (FT) after binding to GFP-nAb™ agarose resin, and elution (E) fractions were analyzed by SDS-PAGE followed by Coomassie staining. In this experiment, EGFP was quantitatively removed from the lysate.

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