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.
nanoCLAMPs are isolated from a phage display library containing over 109 variants. nanoCLAMPs typically bind selectively with nanomolar Kd'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.