Llama IgG Resin and Columns

Like all mammals, camelids produce conventional antibodies made of 2 heavy chains and 2 light chains bound together with disulfide bonds in a Y shape (IgG1). However, they also produce two unique subclasses of immunoglobulin G, IgG2 and IgG3, also known as heavy chain IgG (hcIgG). These antibodies are made of only two heavy chains 1, that lack the CH1 region but still bear an antigen binding domain at their N-terminus called VHH.

Llama antibodies are coming into greater use due to their unique characteristics including small size.  Their steric hindrance is reduced, allowing them to reach hardly accessible antigens that conventional antibodies cannot, such as active sites of enzymes (useful to inhibit enzyme activity) as well as smaller enzymes, such as lysozymes or ribonucleases.  Additionally, Llama antibodies have the capacity to penetrate tissues compared to conventional antibodies, allowing a more precise staining of tissue sections when performing immunohistochemistry.  The high refolding capacity of the VHH region allow them to be more thermodynamically stable and resistant to high temperatures (up to 90°C / 194°F) and extreme pH conditions, such as gastric acid (pH 14).

In addition to increased yields and purity levels, LigaTrap Technologies address many of the shortfalls related to standard affinity ligands including challenges.  Our peptide ligands provide for a robust lifecycle, mild elution conditions and no immunogenicity or leaching.