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Recombinant antibodies are produced using specific genes that code for the desired antibodies. These genes are cloned into an expression vector and expressed in vitro. The advantages of recombinant antibodies include: better specificity, animal origin-free formulation, and more lot-to-lot consistency.
Heterochromatin protein-1 (HP1) is a methyl-lysine binding protein localized at heterochromatin sites, where it mediates gene silencing. It has been shown that mammalian methyltransferases that selectively methylate histone H3 on lysine-9 generate a binding site for HP1 proteins, a family of heterochromatic adaptor molecules implicated in both gene silencing and supranucleosomal chromatin structure. High-affinity in vitro recognition of a methylated histone H3 peptide by HP1 requires a functional chromodomain. Thus, the HP1 chromodomain is a specific interaction motif for the methyl epitope on lysine-9 of histone H3. In vivo, heterochromatin association of HP1 proteins is lost in Suv39h double-null primary mouse fibroblasts but is restored after reintroduction of a catalytically active SUV39H1 HMTase.
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