nanoCLAMP Technology

Next generation antibody based on an immunoglobulin-like scaffold

nanoCLAMPs (nano-CLostridial Antibody Mimetic Proteins) are based on an immunoglobulin-like, thermostable carbohydrate binding module from Clostridium hyaluronidase. Antibody mimetics based on nanoCLAMPs are small (4 nm X 2.5 nm, 15 kD) and have three variable loops comparable to immunoglobulin complementarity determining regions.

SDS PAGE purification by nanoCLAMP affinity chromatography

nanoCLAMPs are isolated from a phage display library containing over 10⁹ variants. nanoCLAMPs typically bind selectively with nanomolar K_d's and release antigen when treated with propylene glycol or glycerol. nanoCLAMP affinity columns have been used successfully to purify or deplete a variety of proteins, including avidin, beta-galactosidase, GFP, MBP, mCherry, NusA, SlyD, SUMO, and thioredoxin. See publication in Protein Expression and Purification.

nanoCLAMPs are readily modified for custom applications. The nanoCLAMP scaffold lacks a native cysteine and is amenable to the addition of a unique cysteine or the construction N- and C-terminal fusions. The addition of a unique cysteine enables conjugation with precise location and stoichiometry. nanoCLAMPs may be fused in a head-to-tail format for bi-specific or higher affinity binding.