Abstract
Monoclonal antibodies (mabs) have been raised against human transthyretin (hTTR). The protein was isolated by an affinity chromatography procedure using Sepharose-hRBP and BALB/c mice were immunized. Following fusion with SP 2/0 myeloma cells, 26 single cell clones producing antibodies against hTTR were isolated. These mabs have been characterized and efforts have been made to establish the epitopes that they recognize. So far at least two different epitopes have been identified both residing in a mid-region fragment corresponding to the amino acid sequence 35-103 of the hTTR subunit. All mabs have been found suitable for immunohistochemical localization of hTTR even in formaldehyde fixed and paraffin embedded tissues.
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