产品详情
查看大图

  • 产品名称：Furin(PairedBasicAminoAcidCleavingEnzyme)(FURIN)(Active)protein(Histag)

  • 产品型号：
  • 产品厂商：ACROBiosystems
  • 产品文档：
你添加了1件商品 查看购物车
简单介绍：
Furin(PairedBasicAminoAcidCleavingEnzyme)(FURIN)(Active)protein(Histag)
详情介绍：
Characteristics This protein carries a polyhistidine tag at the C-terminus. The protein has a calculated MW of 61.5 kDa. The protein migrates as 55-66 kDa under reducing (R) condition (SDS-PAGE).
Purity >95 % as determined by SDS-PAGE.
Endotoxin Level Less than 1.0 EU per μg by the LAL method.
ProductDetails: Biological Activity Comment Measured by its ability to cleave the fluorogenic peptide substrate p - Glu - Arg - Thr - Lys - Arg - AMC. The bioactivity was measured in 100μL reaction mixture containing 4 μg/mL of rhFurin, 50 μM substrate, 25 mM Tris, 1 mM CaCl2, 0. 5% (w/v) Brij-35, pH 9. 0. The specific activity is >130 pmol/min/μg.
Background Furin is 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.
Molecular Weight 61.5 kDa
UniProt P09958
Research Area Proteolysis / Ubiquitin, Metabolism, Amino Acids
Pathways Notch Signaling, Neurotrophin Signaling Pathway
Restrictions For Research Use only
Format Lyophilized
Reconstitution Please see Certificate of Analysis for specific instructions. For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
Buffer 20 mM Tris, 150 mM NaCl, 1 mM CaCl2, 0.01 % Birj-35, pH 9.0
Handling Advice Avoid repeated freeze-thaw cycles.
Storage -20 °C
Storage Comment Lyophilized Protein should be stored at -20 °C or lower for long term storage. Upon reconstitution, working aliquots should be stored at -20 °C or -70 °C. Avoid repeated freeze-thaw cycles.
Supplier Images
SDS-PAGE (SDS) image for Furin (Paired Basic Amino Acid Cleaving Enzyme) (FURIN) (Active) protein (His tag) (ABIN2181123) Human Furin, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained ov...
Background publications Chollet, DiPiero, Wise, Brooks, Dolan, Frackowiak: "The functional anatomy of motor recovery after stroke in humans: a study with positron emission tomography." in: Annals of neurology, Vol. 29, Issue 1, pp. 63-71, 1991 (PubMed).

Wise, Barr, Wong, Kiefer, Brake, Kaufman: "Expression of a human proprotein processing enzyme: correct cleavage of the von Willebrand factor precursor at a paired basic amino acid site." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 87, Issue 23, pp. 9378-82, 1991 (PubMed).