Caspase-14 (human), (recombinant)

Caspase-14 is considered a member of the caspase-1 subfamily and is the only subfamily member with a short (or absent) N-terminal prodomain. In mouse, caspase-14 is highly expressed in embryos, and in adult skin. Within the skin, caspase-14 is present only in the suprabasal layers of the epidermis. A deficiency in caspase-14 expression and processing is associated with psoriasis lesions, raising the possibility that low caspase-14 levels may be among the factors that cause the disease. Elevated caspase-14 expression has been reported in ductal carcinoma in situ and invasive breast cancers. Unlike other procaspases, which are processed by cleavage after aspartate residues, procaspase-14 processing occurs between Ile¹⁵² and Lys¹⁵³. In the presence of the kosmotropic salt, sodium citrate, both recombinant caspase-14, cut in vitro after Asp¹⁴⁶ by granzyme B9, and the endogenous form extracted from human epidermal stratum corneum, are activated to cleave tetrapeptide substrates incorporating the sequence WEHD.