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Creative Biolabs provides the zinc finger library construction service using our Hi-Affi™ phage display platform. This platform can achieve desired libraries with high affinity and diversity for screening and selecting of a broad range of target epitopes. Zinc finger, as a miniprotein composed of 26 amino acids, was firstly identified in a transcription study via Xenopus laevis (African clawed frog) and characterized by the coordination of one or more zinc ions in order to stabilize the fold. These proteins are now found with various binding properties which can also bind to DNA, RNA, protein or lipid substrates. Zinc finger is a member of the DNA-binding motifs family, contains multiple finger-like protrusions that can recognize a diverse set of DNA strings in a sequence-specific manner. The binding ability of zinc finger is considered to involve the sequences of finger domains and their linkers, as well as their number and structure order.
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