RECK was first described as a “reversion inducing cysteine rich protein with Kazal motifs” in transformed NIN 3T3 cells. The RECK protein was implicated as a protein that caused the transformed fibroblasts to revert to a more normal, flattened morphology. When RECK was elevated, the levels of gelatinase-B (MMP-9) were decreased in the cell culture media, another indication of a more normal, less tumor-like cell. Human RECK message encodes a protein of 971 amino acids with predicted mass of 106.5 kDa and a pI of 6.37. RECK is glycosylated, and the apparent weight on SDS-PAGE gels is closer to 110 kDa. Human, dog and mouse RECK are well conserved, and have the same number of residues. Pan RECK sequences encode for two shorter sequences, and it is not clear if the same protein is expressed in that species. RECK message is found in many tissues, including lung, kidney, uterus, kidney, ovary, small intestine, skeletal muscle, prostate and testis. The RECK levels are reduced in many tumor cell lines, such as HT-1080 cells. The RECK sequence codes for a signal sequence, followed by five cysteine-knot motifs, a spacer region, an EGF-like region, another spacer region, a Kazal-like serine proteinase inhibitor domain, another EGF-like region, three more Kazal-like sequences, and a GPI anchor at the carboxyterminal end. RECK interferes with MMP-2, MMP-9 and MMP-14 processing, and apparently leads to lower levels of gelatinolytic activity. Soluble RECK is also active, and the “shed” form of RECK may be processed by proteolytic cleravage. It is not clear which serine proteinases are effected by RECK, but MTSP-1 is one potential target. RECK protein can be detected in cell lysates and in conditioned media from cells. A recommended starting concentration for Western blots is 1:1000 when using colorimetric substrates such as BCIP/NBT, and 1:5000 for chemiluminescent substrates. Higher concentrations of antibody may be needed for samples from more distantly related species.

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