Cysteine-rich secretory proteins (CRISPs) represent a family of evolutionarily conserved proteins which may play a role in the innate immune system and are transcriptionally regulated by androgens in several tissues. CRISP proteins are highly expressed in the mammalian reproductive tract and in the venom secretory ducts of some reptiles. CRISP-10 (cysteine-rich secretory protein 10), also known as CocoaCrisp and Trypsin inhibitor Hl, is a 500 amino acid protein containing 2 LCCL domains, which are thought to function as autonomous folding domains used to construct modular proteins through exon shuffling. CRISP-10 differs from other CRISP proteins in that it does not contain the 10 conserved cysteine residues or ICR domains that are usually conserved throughout the CRISP family.