Lane 1: HepG2
Lane 2: Hela
Lane 3: Hela
Lane 4: MCF-7
Recombinant Rabbit monoclonal primary
Recombinant Furin Monoclonal Antibody (ET7107-37)
Recombinant protein within human furin aa 200-400
HepG2, Hela, MCF-7, human liver tissue, human colon tissue, human placenta tissue, mouse brain tissue.
Store at +4C after thawing. Aliquot store at -20C or -80C. Avoid repeated freeze / thaw cycles.
1*TBS (pH7.4), 0.05% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.
Protein A purified.
Dibasic processing enzyme antibody; Dibasic-processing enzyme antibody; FES upstream region antibody; FUR antibody; FURIN antibody; Furin membrane associated receptor protein antibody; FURIN_HUMAN antibody; PACE antibody; Paired basic amino acid residue cleaving enzyme antibody; Paired basic amino acid residue-cleaving enzyme antibody; PCSK3 antibody; Proprotein convertase subtilisin/kexin type 3 antibody; SPC1 antibody
Belongs to the peptidase S8 family. Furin subfamily.
Seems to be expressed ubiquitously.
The inhibition peptide, which plays the role of an intramolecular chaperone, is autocatalytically removed in the endoplasmic reticulum (ER) and remains non-covalently bound to furin as a potent autoinhibitor. Following transport to the trans Golgi, a second cleavage within the inhibition propeptide results in propeptide dissociation and furin activation.; Phosphorylation is required for TGN localization of the endoprotease. In vivo, exists as di-, mono- and non-phosphorylated forms.
Secreted. Plasma membrane. Golgi apparatus. Endosome.
Furin (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.