| Application notes
(see key) | Recommended dilutions
WB: 1/1000 when using colorimetric substrates such as BCIP/NBT, 1/5000 for chemiluminescent substrates. Predicted molecular weight: 102 kDa. Ab40133 detects Pre-pro PC6 at 117 kDa (this is higher than the predicted molecular weight due to glycosylation and other post-translational modifications) and the mature PC6 at 65 kDa. Smaller cleavage products are also detected. Dilution optimised using Chromogenic detection. Not yet tested in other applications. Optimal dilutions/concentrations should be determined by the end user. |
| Relevance | The protein encoded by this gene belongs to the subtilisin-like proprotein convertase family. The members of this family are proprotein convertases that process latent precursor proteins into their biologically active products. This encoded protein mediates posttranslational endoproteolytic processing for several integrin alpha subunits. It is thought to process prorenin, pro-membrane type 1 matrix metalloproteinase and HIV1 glycoprotein gp160. Two alternatively spliced transcripts are described for this gene but only one has its full length nature known.
PC5 was the first described in the rat and mouse as a neuroendocrine and endocrine protein of the gut, adrenal gland, ovary, lung, pituitary gland and thyroid. A literature alias is PC6, and PC5 is often referred to as PC5/6. Two splice variants are reported; the original 913 amino acid sequence (PC5A) and an 1877 amino acid membrane-associated form (PC5B). The longer form is thought to be bound in the Golgi, and the shorter form secreted through dense core secretory granules. PC5 has been shown to cleave the neural adhesion protein L1, Preo-neurotension, VEGF-C, Integrin alpha V, some viral surface proteins, and is thought to process prorenin. Like furin, PC2 and PACE4, PC5 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 (subtilisin-like proprotein convertases), with PC5 getting the SPC5 moniker. PC5 structure contains a propeptide domain, a catalytic domain and an RGD containing cystein-rich domain (homo-B). The longer sequence contains an extended cysteinc-rich domain. 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, PC5 becomes a two-chain form, and the propeptide piece is released after a second internal cleavage. PC5A resides mainly in the dense core secretory vesicles and the TGN, and is cycled to the surface, with some of the PC5 being secreted from the cells. PC5 has been reported to be elevated in tumor cell lines and to increase tumor progression. The message for PC5A encodes a 913 amino acid protein with a predicted mass of 101.65 kDa, and a pI of 7.62, but glycosylation and other post-translational modifications make the pre-pro PC5 run at 117 kDa, the mature PC5 at 65 kDa. Smaller cleavage products are also detected. The PC5B protein has an apparent mass of 210 kDa on reduced SDS PAGE gels, and is processed to a secreted 170 kDa form.
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