Furin Recombinant Protein | PACE recombinant protein

Human CellExp Furin, human recombinant

Cat. Num. AAA844953

• Gene Names: FURIN; FUR; PACE; SPC1; PCSK3
• Applications: SDS-Page
• Purity: >=95% by SDS-PAGE gel
• Synonyms: Furin; Human CellExp Furin; human recombinant; FURIN; FUR; PACE; PCSK3; SPC1; PACE recombinant protein

• Host: HEK 293 cells
• Purity/Purification: >=95% by SDS-PAGE gel
• Form/Format: Lyophilized from 0.22 mum filtered solution in MES, Brij-35. Generally 5-8% Mannitol or trehalose is added as a protectant before lyophilization.; Appearance: Lyophilized powder
• Sequence Positions: Asp108 -Glu 715

• Applicable Applications for PACE recombinant protein: SDS-PAGE; HPLC
• Endotoxin: <1 EU/ug by LAL method
• Reconstitution: Centrifuge the vial prior to opening. Reconstitute in sterile PBS, pH 7.4toa concentration of 50?g/ml. Do not vortex. This solution can be stored at 2-8°C for up to 1 month. For extended storage, it is recommended to store at -20°C
• Preparation and Storage: Store at -20 degree C. After reconstitution, aliquot and store at -20 degree C and use within 3 months. Avoid repeated freezing and thawing cycles.

Testing Data

Related Product Information for PACE recombinant protein

Background: Furin also known as paired basic Amino acid Cleaving Enzyme (PACE), is an enzyme which belongs to the subtilisin-like proprotein convertase family. The members of this family are proprotein convertases that process latent precursor proteins into their biologically active products. Furin is enriched in the Golgi apparatus, where it functions to cleave other proteins into their mature/active forms. The expression of furin in T-cells is required for maintenance of peripheral immune tolerance. Furin cleaves proteins just downstream of a basic amino acid target sequence (canonically, Arg-X-(Arg/Lys) -Arg'). PACE is a calcium-dependent serine endoprotease that can efficiently cleave precursor proteins at their paired basic amino acid processing sites. In addition to processing cellular precursor proteins, furin is also utilized by a number of pathogens. For example, the envelope proteins of viruses such as HIV, influenza and dengue fever viruses must be cleaved by furin or furin-like proteases to become fully functional. PACE also play a role in tumor progression.

Product Categories/Family for PACE recombinant protein

Cytokines; Growth Factors & Hormones; Human cell expressed recombinant proteins Cytokines; Growth Factors & Hormones; Cytokines & Growth Factors (A-Z) Proteins and Enzymes; Human cell expressed recombinant proteins Proteins and Enzymes; Cytokines; Growth

NCBI and Uniprot Product Information

• NCBI GI #: 577019578
• NCBI GeneID: 5045
• NCBI Accession #: NP_001276752.1
• NCBI GenBank Nucleotide #: NM_001289823.1
• UniProt Accession #: P09958; Q14336; Q6LBS3; Q9UCZ5
• Molecular Weight: This protein is fused with 6×His tag at the C-terminus, has a calculated MW of 66.5 kDa. The predicted N-terminus is Asp 108. DTT-reduced Protein migrates as 55-66 kDa.
• 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: Membrane protein, integral; EC 3.4.21.75; Vesicle; Cell surface; Protease

Chromosomal Location of Human Ortholog: 15q26.1

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

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

Biological Process: extracellular matrix organization and biogenesis; viral reproduction; nerve growth factor receptor signaling pathway; peptide hormone processing; regulation of signal transduction; pathogenesis; viral infectious cycle; proteolysis; positive regulation of membrane protein ectodomain proteolysis; peptide biosynthetic process; nerve growth factor processing; extracellular matrix disassembly; transforming growth factor beta receptor signaling pathway; regulation of endopeptidase activity; negative regulation of nerve growth factor production; secretion by cell; Notch signaling pathway; signal peptide processing; virus assembly; post-translational protein modification; peptidyl-glutamic acid carboxylation; nerve growth factor production; negative regulation of transforming growth factor-beta1 production; cell proliferation; collagen catabolic process; cellular protein metabolic process; viral protein processing; regulation of protein catabolic process; protein processing; negative regulation of low-density lipoprotein receptor catabolic process