Useful polyclonal antibodies against synthetic peptides corresponding to immunoglobulin light chain constant region for immunohistochemical detection of immunoglobulin light chain amyloidosis

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Abstract
For the immunohistochemical detection of immunoglobulin (Ig) light chain amyloidosis on formalin‐fixed, paraffin‐embedded tissue sections, we prepared polyclonal antibodies against synthetic peptides corresponding to positions 118–134 of Ig λ light chain and positions 116–133 of Ig κ light chain. Nineteen cases of systemic Ig λ light chain amyloidosis (Aλ amyloidosis), 10 cases of systemic Ig κ light chain amyloidosis (Aκ amyloidosis), one case of immunohistochemically unclassified systemic amyloidosis and five cases of localized Aλ amyloidosis were tested with these antibodies. Anti‐λ (118–134) antiserum and the affinity‐purified antibody both reacted with 18 of the 19 cases of systemic Aλ amyloidosis and all cases of localized Aλ amyloidosis, although the immunoexpression was somewhat variable in intensity in different areas within the same specimen in both systemic and localized amyloidosis. The signal intensities in plasma cells and serum reacted for anti‐λ (118–134) antiserum were weaker than signals obtained with commercially available anti‐Ig λ light chain antibodies. Anti‐κ (116–133) antiserum and the affinity‐purified antibody reacted with nine of the 10 cases of systemic Aκ amyloidosis. We conclude that these antibodies against synthetic peptides corresponding to the Ig light chain constant region are useful for the classification of amyloidosis on formalin‐fixed, paraffin‐embedded tissue sections.