{"product_id":"furinpcsk3-his-tag-protein-human-ua011272","title":"Furin\/PCSK3 His Tag Protein, Human","description":"\u003ch4\u003eProduct Specification\u003c\/h4\u003e\u003cdiv class=\"responsive-table product-detail-table details-table\"\u003e\n\u003cbr\u003e\u003ctable style=\"width: 100%; height: auto;\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 22%;\"\u003e\u003cstrong\u003eSpecies\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 78%;\"\u003eHuman\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 22%;\"\u003e\u003cstrong\u003eSynonyms\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 78%;\"\u003eFUR,PCSK3,SPC1,PACE\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 22%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 78%;\"\u003eP09958-1\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 22%;\"\u003e\u003cstrong\u003eAmino Acid Sequence\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 78%;\"\u003e\u003cp\u003eGln27-Ala574 with His Tag at the C-Terminus\u003c\/p\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 22%;\"\u003e\u003cstrong\u003eExpression System\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 78%;\"\u003eHEK293\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 22%;\"\u003e\u003cstrong\u003eMolecular Weight\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 78%;\"\u003e\u003cp style=\"margin-bottom: 0px;\"\u003e55-72kDa (Reducing)\u003c\/p\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 22%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 78%;\"\u003e＞90% by SDS-PAGE \u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 22%;\"\u003e\u003cstrong\u003eConjugation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 78%;\"\u003eUnconjugated\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 22%;\"\u003e\u003cstrong\u003eTag\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 78%;\"\u003eHis Tag\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 22%;\"\u003e\u003cstrong\u003ePhysical Appearance\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 78%;\"\u003eLyophilized powder\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 22%;\"\u003e\u003cstrong\u003eStorage Buffer\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 78%;\"\u003e\u003cp\u003ePBS, PH7.4, 5% trehalose\u003c\/p\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 22%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 78%;\"\u003e\u003cp style=\"margin-bottom: 0px;\"\u003eReconstitute at 0.1-1 mg\/ml according to the size in ultrapure water after rapid centrifugation. \u003c\/p\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 22%;\"\u003e\u003cstrong\u003eStability \u0026amp; Storage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 78%;\"\u003e\u003cp\u003e· 12 months from date of receipt, lyophilized powder stored at -20 to -80℃.\u003cbr\u003e· 3 months, -20 to -80℃ under sterile conditions after reconstitution.\u003cbr\u003e· Please do not repeated freeze-thaw cycles.\u003c\/p\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 22%;\"\u003e\u003cstrong\u003eReference\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 78%;\"\u003e\u003cp\u003e1.Anderson ED, Molloy SS, Jean F, Fei H, Shimamura S, Thomas G. The ordered and compartment-specfific autoproteolytic removal of the furin intramolecular chaperone is required for enzyme activation. J Biol Chem. 2002 Apr 12;277(15):12879-90.\u003cbr\u003e2.Dahms SO, Hardes K, Becker GL, Steinmetzer T, Brandstetter H, Than ME. X-ray structures of human furin in complex with competitive inhibitors. ACS Chem Biol. 2014 May 16;9(5):1113-8.\u003c\/p\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e\n\u003c\/div\u003e\u003ch4\u003eBackground\u003c\/h4\u003e\u003cdiv\u003e\u003cp\u003eFurin, also known as Paired Basic Amino Acid Cleaving Enzyme (PACE), is a key member of the subtilisin-like proprotein convertase family. Functioning as a calcium-dependent serine protease, its structure includes an N-terminal signal peptide, a prodomain, a catalytic domain, a P-domain responsible for maintaining enzymatic activity and calcium\/pH sensitivity, a transmembrane region, and a cytoplasmic tail. Primarily localized within the Golgi apparatus\/endosomal system, it activates a wide range of proprotein substrates—such as growth factors, receptors, extracellular matrix proteins, and pathogen proteins (e.g., envelope proteins of HIV and influenza virus)—by specifically cleaving after the Arg-X-(Arg\/Lys)-Arg sequence motif. It plays a critical role in embryogenesis, peripheral immune tolerance, and cellular homeostasis. Dysregulation of its function is closely linked to tumor progression, neurodegenerative diseases, and various pathogen infections, making it a significant therapeutic target in clinical applications.\u003c\/p\u003e\u003c\/div\u003e\u003ch4\u003eProtocol\u003c\/h4\u003e\u003cdiv\u003e\u003cp\u003eAssay protocol\u003cbr\u003ePrinciple: Measured by its ability to cleave the fluorogenic peptide substrate, Pyr-Arg-Thr-Lys-Arg-AMC.\u003cbr\u003eMaterials\u003cbr\u003eAssay buffer: 25 mM Tris, 1 mM CaCl2, pH 9.0\u003cbr\u003eFurin\/PCSK3 His Tag Protein, Human (UA011272)\u003cbr\u003eSubstrate: Pyr-Arg-Thr-Lys-Arg-AMC (abs45133051) \u003cbr\u003e96 ELISA Removable Plate, Black, High binding (GENEVER, Catalog # GMO2-96H)\u003cbr\u003ePlate Reader (PerkinElmer, excitation 380 nm and emission 460 nm)\u003cbr\u003eProduce\u003cbr\u003eDilute Human Furin Protein to 2 µg\/mL\/4 µg\/mL\/8 µg\/mL in Assay Buffer.\u003cbr\u003eDilute Substrate to 100 µM in Assay Buffer.\u003cbr\u003eLoad into a black well plate 50 µL of 2 µg\/mL\/4 µg\/mL\/8 µg\/mL of Human Furin Protein, and start the reaction by adding 50 µL of 100 µM Substrate. Include a Substrate Blank containing 50 µL of Assay Buffer and 50 µL of 100 µM Substrate.\u003cbr\u003eRead at excitation and emission wavelengths of 380 nm and 460 nm, respectively in kinetic mode for 10 minutes.\u003cbr\u003eCalculate specific activity:\u003cbr\u003e*Adjusted for Substrate Blank\u003cbr\u003e**Derived using calibration standard 7-amino-4-Methyl Coumarin\u003cbr\u003eConversion Factor (pmol\/RFU)\u003cbr\u003eProduce\u003cbr\u003eBuffer: Assay buffer\u003cbr\u003eCalibration standard: standard 7-amino-4-Methyl Coumarin (Enzo, Catalog # BML-KI107-0001).\u003cbr\u003eAdd 100 µL Dilute Calibration standard, Standard curve 1500\/750\/375\/188\/94\/47\/24\/12\/6\/3 pmol per well or blank (Assay buffer) per well.\u003cbr\u003eRead at excitation and emission wavelengths of 380 nm and 460 nm, respectively in endpoint mode.\u003cbr\u003eLinear Regression of 7-amino-4-Methyl Coumarin (pmol) (y)—RFU-Blank(x).\u003cbr\u003eNote\u003cbr\u003eStorage Conditions: After reconstitution, aliquot and store at -80°C. Please do not\u003cbr\u003erepeated freeze-thaw cycles.\u003cbr\u003e\u003c\/p\u003e\u003c\/div\u003e","brand":"UA BIOSCIENCE","offers":[{"title":"25μg","offer_id":42332756148299,"sku":null,"price":570.0,"currency_code":"USD","in_stock":true},{"title":"100μg","offer_id":42332756181067,"sku":null,"price":1135.0,"currency_code":"USD","in_stock":true},{"title":"500μg","offer_id":42332756213835,"sku":null,"price":3175.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0590\/8375\/1499\/files\/AntBioImage_9c8ec2e0-946f-465d-a2f3-cb77888704ed.png?v=1776073430","url":"https:\/\/www.antbioinc.com\/products\/furinpcsk3-his-tag-protein-human-ua011272","provider":"AntBio","version":"1.0","type":"link"}