BMP-1 (EC 3.4.24.1), also known as Procollagen C-endopeptidase, Procollagen C-Peptidase, or Procollagen C-Proteinase, is an extracellular zinc endopeptidase of the Astacin family. PCOLE2 was described by Acott and Wirtz in a subtractive library in eye tissues, and little is known about its function. The human sequence of PCOLE-2 codes for a 415 amino acid protein, with 44% identity to PCOLE-1. PCOLE-2 does not appear to be eye-specific, and is produced by a wide range of cell types in culture. PCOLE-1 was described by Takahara and Greenspan, and by Kessler as an accessory protein that enhances the activity of BMP-1. PCOLE1 binds to Procollagen, and assists BMP-1, increasing the Type-I Procollagen C-Terminal processing activity 10-fold, although it does not directly activate the enzyme. The mature protein is seen as 50-55 kD on SDS PAGE gels under reducing conditions, and proteolytic removal of the carboxyterminal end generates 34 and 36 kD active fragments. PCOLE-1 is produced in tissues rich in Type-I collagen, such as skin, kidney and tendon. PCOLE-1 is secreted into culture media by a wide range of cell types. BMP-1 is produced in a number of different forms, with different carboxyterminal regions, PCOLE-1 and 2 may be isoform-or tissue specific enhancers, giving a degree of regulation to the activity of BMP-1 in different circumstances. Although it is assumed that PCOLE-2 interacts with BMP-1 in a manner similar to PCOLE-1, little is known about relative distribution, expression or regulation of PCOLE-2. RP1PCOLE-2 recognizes both full-sized and cleaved PCOLE-1, and can be used for Western blotting. 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. EDTA/EGTA treatment of tissues or lysates is required to see latent zymogen

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