Furin Recombinant Rabbit monoclonal Antibody IgG
Fig1: Western blot analysis of Furin on different cell lysates using anti-Furin antibody at 1/500 dilution.
Lane 1: HepG2
Lane 2: Hela
Lane 3: Hela
Lane 4: MCF-7
Fig2: Immunohistochemical analysis of paraffin-embedded human liver tissue using anti-Furin antibody. Counter stained with hematoxylin.
Fig3: Immunohistochemical analysis of paraffin-embedded human colon tissue using anti-Furin antibody. Counter stained with hematoxylin.
Host Species; Species ReactivityRabbit; Human, Mouse, Rat
ImmunogenRecombinant protein within human Furin aa 200-400
Purification; FormulationProA affinity purified; 1*TBS (pH7.4), 1%BSA, 40%Glycerol. Preservative: 0.05% Sodium Azide.; Liquid form.
ALTnamesFurin, Dibasic-processing enzyme, Paired basic amino acid residue-cleaving enzyme
BackgroundFurin (FUR, PACE, PCSK3, SPC1, Kex2p) is a calcium-dependent serine endoprotease that belongs to the subtilisin-like proprotein convertase family. The members of this family process latent precursor proteins into their biologically active products. Furin cleaves at paired basic amino acid processing sites within proparathyroid hormone, transforming growth factor beta 1 precursor, proalbumin, pro-beta-secretase, membrane type-1 matrix metalloproteinase, beta subunit of pro-nerve growth factor and von Willebrand factor. Furin can directly cleave proMMP-2 within the trans-Golgi network leading to an inactive form of matrix metalloproteinase-2 (MMP-2). Furin is synthesized as an inactive zymogen that may minimize the occurrence of premature enzymatic activity that would lead to alternative protein activation or degradation. The inhibitory mechanism is based on the presence of an inactivating prosegment at the NH2 terminal of the Furin. After initial autocatalytic cleavage, the prosegment remains tightly associated until it reaches the trans-Golgi network where the dissociation of the prosegment and activation of furin occurs.(ET7107-37)