Rabbit anti-Human Furin Polyclonal Antibody | anti-FURIN antibody

Anti-Furin (PACE, SPC-1), Homo-B Domain Antibody

Cat. Num. AAA4157602

• Gene Names: FURIN; FUR; PACE; SPC1; PCSK3
• Reactivity: Human
• Applications: Western Blot
• Purity: Immunogen Affinity Purified
• Synonyms: Furin; Polyclonal Antibody; Anti-Furin (PACE; SPC-1); Homo-B Domain Antibody; anti-FURIN antibody

• Host: Rabbit
• Reactivity: Human
• Clonality: Polyclonal
• Isotype: IgG
• Specificity: The antibody recognizes subtilisin-like serine protease furin.
• Purity/Purification: Immunogen Affinity Purified
• Form/Format: Liquid; PBS, pH 7.4 with 0.05% sodium azide.
• Concentration: 1ug/ul (varies by lot)
• Sequence Length: 794

• Applicable Applications for anti-FURIN antibody: Western Blot (WB)
• Application Notes: WB: 1:1000 when using colorimetric substrates such as BCIP/NBT and 1:5000 for chemiluminescent substrates. Predicted molecular weight: 88 kDa. 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. Dilution optimised using Chromogenic detection.
• Immunogen: Synthetic peptide based on the Homo-B domain of human furin.
• Cellular Localization: Golgi Apparatus; Trans-Golgi Network.
• Preparation and Storage: This product is stable for several weeks at 4 degree C as an undiluted liquid. Dilute only prior to immediate use.; For extended storage, aliquot contents and freeze at-20 degree C or below. Avoid cycles of freezing and thawing. Expiration date is one (1) year from date of receipt.

Testing Data

Related Product Information for anti-FURIN antibody

Description: The antibody 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_recover 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.

Relevance: Furin is a membrane-associated, calcium-dependent, serine protease that belongs to the subtilisin-like prohormone convertase (PC) family. Members of this family of cellular enzymes cleave most prohormones and neuropeptide precursors. Numerous other cellular proteins, some viral proteins, and bacterial toxins that are transported by the constitutive secretory pathway are also targeted for maturation by PCs. Furin and other PC family members share structural similarities which include a heterogeneous ~10 kDa amino-terminal proregion, a highly conserved ~55 kDa subtilisin-like catalytic domain, and carboxyl-terminal domain that is heterogeneous in length and sequence. These enzymes become catalytically active following proregion cleavage within the appropriate cellular compartment. Furin is the only known PC to possess a transmembrane domain. Cleavage of target proteins occurs at the carboxyl-terminus of the furin consensus sequence, RX(K/R)R. It has been shown that the acidic peptide sequence, C771PSDSEEDEG780, localizes furin to the trans-Golgi-network. Phosphorylation of serine residues within this region modulates intracellular routing of Furin protein. An additional signaling domain includes the tetrapeptide sequence, Y759KGL762, which directs internalization from the cell surface.

NCBI and Uniprot Product Information

• NCBI GI #: 577019580
• NCBI GeneID: 5045
• NCBI GenBank Nucleotide #: NP_001276753.1
• UniProt Accession #: P09958
• NCBI Official Full Name: furin preproprotein
• NCBI Official Synonym Full Names: furin, paired basic amino acid cleaving enzyme
• NCBI Official Symbol: FURIN
• NCBI Official Synonym Symbols: FUR; PACE; SPC1; PCSK3
• NCBI Protein Information: furin
• UniProt Protein Name: Furin
• Protein Family: Furin
• UniProt Gene Name: FURIN
• UniProt Synonym Gene Names: FUR; PACE; PCSK3; PACE
• UniProt Entry Name: FURIN_HUMAN

NCBI Description

This gene encodes a member of the subtilisin-like proprotein convertase family, which includes proteases that process protein and peptide precursors trafficking through regulated or constitutive branches of the secretory pathway. It encodes a type 1 membrane bound protease that is expressed in many tissues, including neuroendocrine, liver, gut, and brain. The encoded protein undergoes an initial autocatalytic processing event in the ER and then sorts to the trans-Golgi network through endosomes where a second autocatalytic event takes place and the catalytic activity is acquired. The product of this gene is one of the seven basic amino acid-specific members which cleave their substrates at single or paired basic residues. Some of its substrates include 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. It is also thought to be one of the proteases responsible for the activation of HIV envelope glycoproteins gp160 and gp140 and may play a role in tumor progression. This gene is located in close proximity to family member proprotein convertase subtilisin/kexin type 6 and upstream of the FES oncogene. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2014]

Uniprot Description

FURIN: Furin is likely to represent the ubiquitous endoprotease activity within constitutive secretory pathways and capable of cleavage at the RX(K/R)R consensus motif. Belongs to the peptidase S8 family. Furin subfamily.

Protein type: Cell surface; EC 3.4.21.75; Membrane protein, integral; Protease; Vesicle

Chromosomal Location of Human Ortholog: 15q26.1

Cellular Component: cell surface; endoplasmic reticulum; extracellular space; Golgi lumen; Golgi membrane; lipid raft; membrane; plasma membrane; trans-Golgi network; trans-Golgi network transport vesicle

Molecular Function: endopeptidase activity; nerve growth factor binding; peptidase activity; peptide binding; protease binding; protein binding; serine-type endopeptidase activity; serine-type endopeptidase inhibitor activity

Biological Process: cell proliferation; cellular protein metabolic process; collagen catabolic process; extracellular matrix disassembly; extracellular matrix organization and biogenesis; negative regulation of low-density lipoprotein receptor catabolic process; negative regulation of nerve growth factor production; negative regulation of transforming growth factor-beta1 production; nerve growth factor processing; nerve growth factor production; peptide biosynthetic process; peptide hormone processing; positive regulation of membrane protein ectodomain proteolysis; protein processing; regulation of endopeptidase activity; regulation of protein catabolic process; secretion by cell; signal peptide processing; transforming growth factor beta receptor signaling pathway; viral infectious cycle; viral protein processing