Presenting: An immobilized GFP-binding protein derived from camelid single domain antibodies
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 size (13 KDa) and a very high stability (stable up to 70°C, functional in high salt concentrations or 0.5% SDS). One molecule of GFP-nAb™ binds one molecule of GFP with a dissociation constant (Kd) in the sub nanomolar range. This makes GFP-nAb™ resin the ideal candidate for a variety of biological assays, some of which are listed below:
- Immunoprecipitation / CO-IP
- Quantitative analysis
- Chromatin Immunoprecipitation (ChIP)
- Identifying Interacting Proteins
- RIP Assays (RNA Immunoprecipitation)
- CLIP Assays (in vivo Cross Linking and Immunoprecipitation)
GFP-nAb™ binds a large number of commonly used fluorescent proteins derived from the original Aequorea victoria GFP, including EGFP, Venus, Cerulean, EBFP2 and more. 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, allowing you to perform multiple immunoprecipitation reactions in a matter of minutes.
Request your Complementary Sample Vial of GFP-nAb Today
Insight Bio has 100 complementary sample size vials of GFP-nAb available to customers on a first come, first serve basis. Contact our PhD level technical team today by telephone +44(0)208 385 0303 or email email@example.com for further details
||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.