Rabbit Antibody to Furin (PACE, SPC-1); Homo-B domain

RP2-Furin is a rabbit polyclonal antibody made to the subtilisin-like serine protease furin.   The antibody is made to a synthetic peptide based on the Homo-B domain of human furin. 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.

Furin was first identified in an analysis of the upstream elements of the c-fes proto-oncogene, a tyrosine kinase first discovered as the avian proto-oncogene fps. The partial sequence cloned upstream of the c-fes/fps gene had some homology to the insulin receptor, and they named the gene fur ( f es/fps u pstream r egion) and the protein furin, due to the in sulin receptor homology. When the full length gene was cloned it was found to encode a type-II serine membrane proteinase that cleaved after pairs of basic amino acids, and other groups names it PACE ( p aired basic a mino acid residue c leavine e nzyme). The catalytic domain has homology to other PACE enzymes, the prohormone convertase family, which initially was discovered for their role in processing POMC and other pro-hormones, and were later found to process a wider range of precursor proteins. Some have renamed the PCs proprotein convertases, and another group has renamed the entire family with a uniform nomenclature of SPCs ( subtilisin-like p roprotein convertases), with furin getting the SPC1 moniker. Furin has a propeptide domain, a catalytic domain, an RGD containing cystein-rich domain (homo-b), a transmembrane domain and a cytoplasmic 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, the furin becomes a two-chain form, and the propeptide piece is released after a second internal cleavage.   Furin resides mostly in the transgolgi network, but cycles to and from the cell surface, from which it can be shed by cleavage within the cystine rich domain. The shed furin is still proteolytically active, but has different substrate specificity. Furin is ubiquitously expressed at low levels, but found in highest concentration in the liver and kidneys, lower levels in brain, spleen, thymus, and smaller levels in most other tissues. Overexpression of furin accelerates tumor growth in cancer models, blocking furin decreases tumor growth, and furin null mutants are embryonic lethal. Furin cleaves a wide variety of proteins, including growth factors, viral coat proteins, matrix metalloproteinases, mostly activating latent forms of the proteins. The 794 amino acid furin has a predicted mass of 86.68 kDa, and a pI of 6.0, but glycosylation and other post-translational modifications make the pre-pro furin run at 110-104 kDa, the mature furin at 98-95 kDa, and shed furin at 90 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.   Higher concentrations of antibody may be needed for samples from more distantly related species.

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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