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Application notes
(see key)
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Recommended dilutions
ELISA: Use at an assay dependent dilution. WB: Use at an assay dependent dilution. This peptide can be used with studies using ab28571. Dilution optimised using Chromogenic detection. Not yet tested in other applications. Optimal dilutions/concentrations should be determined by the end user.
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Relevance
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PC2 was initially found as an insulin processing enzyme, and was the third of the human prohormone convertasae enzymes to be discovered. Like furin, PC1 and PACE4, PC2 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 PC2 getting the SPC2 moniker. PC2 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, PC2 becomes a two-chain form, and the propeptide piece is released after a second internal cleavage. PC2 resides along with PC1, mainly in the dense core secretory vesicles and the TGN, and is cycled to the surface, with some of the PC2 being secreted from the cells. PC2 has been reported to be elevated in tumor cell lines and to increase tumor progression. PC2 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. PC2 cleaves a wide variety of proteins, including growth factors, viral coat proteins, matrix metalloproteinases, mostly after PC1 cleavage. The maturation of PC2 appears to require association with the 7B2 protein, which both helps fold PC2 properly and keeps the PC2 latent until the 7B2 protein is clipped by a PC enzyme.
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Storage buffer
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Preservative: None
Constituents: 0.001% Tween 20, 30mM HEPES, 2mM EDTA, 150mM Sodium chloride, pH 6.75
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