Rabbit Antibody to PC1 (paired basic amino acid cleaving enzyme-1, PC3, SPC3); homo-B domain

RP2-PC1 is a rabbit polyclonal antibody made to the subtilisin-like serine protease PC1.   The antibody is made to a synthetic peptide based on the carboxy end of the homo-B domain of human PC1. The antibody has been peptide-affinity purified, concentrated to 1.0 mg/ml, with the addition of 0.05% sodium azide as preservative and 50% glycerol as cryoprotectant.

PC1 was the first of the human prohormone convertasae enzymes to be discovered. A literature alias is PC3, and PC1 is often referred to as PC1/3. Like furin, PC2 and PACE4, PC1 is a serine proteinase that cleaves after pairs of basic amino acids, but with some differences in substrate specificity and distribution. The catalytic domain has homology to other PC enzymes, the prohormone convertase family initially discovered for their role in processing POMC, insulin and other pro-hormones, and later found to process a wider range of precursor proteins. Some have renamed the prohormone convertases as proprotein convertases, and another group has renamed the entire family with a uniform nomenclature of SPCs ( s ubtilisin-like p roprotein c onvertases), with PC1 getting the SPC3 moniker. PC1 structure contains a propeptide domain, a catalytic domain and an RGD containing cystein-rich domain (homo-B). The PCs have an RxxR consensus cleavage requirement, and the propeptide is separated from the mature protein by just such a sequence. After cleavage of the propeptide domain, PC1 becomes a two-chain form, and the propeptide piece is released after a second internal cleavage.   PC1 is further processed by cleavage at the carboxyterminal end, which enhances the PC1 enzymatic activity. PC1 resides mainly in the dense core secretory vesicles and the TGN, and is cycled to the surface, with some of the PC1 being secreted from the cells. PC1 has been reported to be elevated in tumor cell lines and to increase tumor progression. PC1 is expressed at low levels in most tissues, but found in highest concentration in the brain, the anterior pituitary, pancreatic islet cells, thyroid, parathyroid and gut. PC1 null mutant mice suffer dwarfism, and PC1 mutants have been linked to obesity and diabetes in humans. PC1 cleaves a wide variety of proteins, including growth factors, viral coat proteins, matrix metalloproteinases, mostly activating latent forms of the proteins. The message for PC1 encodes a 753 amino acid protein with a predicted mass of 84.15 kDa, and a pI of 5.58, but glycosylation and other post-translational modifications make the pre-pro PC1 run at 94 kDa, the mature PC1 at 87 and 83 kDa, and carboxy-processed PC1 at 66 kDa. Smaller cleavage products are also detected. A recommended starting concentration for Western blots is 1:1,000 when using colorimetric substrates such as BCIP/NBT, and 1:5,000 for chemiluminescent substrates.  

FOR RESEARCH USE ONLY. NOT FOR USE IN HUMANS.

The undiluted antibody solution is stable for 12 months at -20 ° C.

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