{"product_id":"recombinant-neosartorya-fumigata-extracellular-metalloproteinase-mep-mep","title":"Recombinant Neosartorya fumigata Extracellular metalloproteinase mep (mep)","description":"\u003cp\u003e\u003cb\u003eSize\u003c\/b\u003e: 100ug. Other sizes are also available. \u003c\/p\u003e\u003cp\u003e\u003cb\u003eActivity\u003c\/b\u003e: Not tested\u003c\/p\u003e\u003cp\u003e\u003cb\u003eResearch Areas\u003c\/b\u003e: Others\u003c\/p\u003e\u003cp\u003e\u003cb\u003eUniprot ID\u003c\/b\u003e: P46075\u003c\/p\u003e\u003cp\u003e\u003cb\u003eGene Names\u003c\/b\u003e: mep\u003c\/p\u003e\u003cp\u003e\u003cb\u003eAlternative Name(s)\u003c\/b\u003e: (AfuMep)(Allergen Asp f 5)(Elastinolytic metalloproteinase mep)(Fungalysin mep)(allergen Asp f 5.0101)\u003c\/p\u003e\u003cp\u003e\u003cb\u003eAbbreviation\u003c\/b\u003e: Recombinant Neosartorya fumigata Extracellular metalloproteinase mep protein\u003c\/p\u003e\u003cp\u003e\u003cb\u003eOrganism\u003c\/b\u003e: Neosartorya fumigata (strain ATCC MYA-4609 \/ Af293 \/ CBS 101355 \/ FGSC A1100) (Aspergillus fumigatus)\u003c\/p\u003e\u003cp\u003e\u003cb\u003eSource\u003c\/b\u003e: E.coli\u003c\/p\u003e\u003cp\u003e\u003cb\u003eExpression Region\u003c\/b\u003e: 246-634aa\u003c\/p\u003e\u003cp\u003e\u003cb\u003eProtein Length\u003c\/b\u003e: Full Length of Mature Protein\u003c\/p\u003e\u003cp\u003e\u003cb\u003eTag  Info\u003c\/b\u003e: N-terminal 10xHis-tagged and C-terminal Myc-tagged\u003c\/p\u003e\u003cp\u003e\u003cb\u003eTarget Protein Sequence\u003c\/b\u003e: ADYQVYAWGINDPTEGERTVIKDPWDSVASEFTWISDGSTNYTTSRGNNGIAQSNPSGGSSYLNNYRPSSSSLSFKYPYSVSSSPPSSYIDASIIQLFYTANIYHDLLYTLGFTEKAGNFEYNTNGQGGLGNDYVILNAQDGSGTNNANFATPPDGQPGRMRMYVWTESTPYRDGSFEAGIVIHEYTHGLSNRLTGGPANSNCLNALESGGMGEGWSDFMATAIRLKPGDKRSTDYTMGEWASNRAGGIRQYPYSTSLSTNPLTYTSVNSLNAVHAIGTVWASMLYEVLWNLIDKHGKNDAPKPTLRDGVPTDGKYLAMKLVMDGMALQPCNPNFVQARDAILDADTALTGGENQCEIWTAFAKRGLGAGAKYSSRNRVGSTEVPSGVC\u003c\/p\u003e\u003cp\u003e\u003cb\u003eMW\u003c\/b\u003e: 49.6 kDa\u003c\/p\u003e\u003cp\u003e\u003cb\u003ePurity\u003c\/b\u003e: Greater than 85% as determined by SDS-PAGE.\u003c\/p\u003e\u003cp\u003e\u003cb\u003eEndotoxin\u003c\/b\u003e: Not test\u003c\/p\u003e\u003cp\u003e\u003cb\u003eBiological_Activity\u003c\/b\u003e: \u003c\/p\u003e\u003cp\u003e\u003cb\u003eForm\u003c\/b\u003e: Liquid or Lyophilized powder\u003c\/p\u003e\u003cp\u003e\u003cb\u003eBuffer\u003c\/b\u003e: If the delivery form is liquid, the default storage buffer is Tris\/PBS-based buffer, 5%-50% glycerol.\nIf the delivery form is lyophilized powder, the buffer before lyophilization is Tris\/PBS-based buffer, 6% Trehalose, pH 8.0.\u003c\/p\u003e\u003cp\u003e\u003cb\u003eReconstitution\u003c\/b\u003e: We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg\/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃\/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.\u003c\/p\u003e\u003cp\u003e\u003cb\u003eStorage\u003c\/b\u003e: The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. \nGenerally, the shelf life of liquid form is 6 months at -20℃\/-80℃. The shelf life of lyophilized form is 12 months at -20℃\/-80℃.\u003c\/p\u003e\u003cp\u003e\u003cb\u003eNotes\u003c\/b\u003e: Repeated freezing and thawing is not recommended. Store working aliquots at 4℃ for up to one week.\u003c\/p\u003e\u003cp\u003e\u003cb\u003eRelevance\u003c\/b\u003e: Secreted metalloproteinase that allows assimilation of proteinaceous substrates and probably acts as a virulence factor. Catalyzes the hydrolysis of elastin. Hydrolyzes azocasein, synthetic fluorigenic substrate Abz-Ala-Ala-Phe-Phe-pNA, and His-Leu, Ala-Leu, Tyr-Leu, Gly-Phe, and Phe-Phe peptide bonds in the B chain of insulin.\u003c\/p\u003e\u003cp\u003e\u003cb\u003eReference\u003c\/b\u003e: \"Purification and characterization of an elastinolytic metalloprotease from Aspergillus fumigatus and immunoelectron microscopic evidence of secretion of this enzyme by the fungus invading the murine lung.\"\nMarkaryan A., Morozova I., Yu H., Kolattukudy P.E.\nInfect. Immun. 62: 2149-2157(1994)\u003c\/p\u003e\u003cp\u003e\u003cb\u003eFunction\u003c\/b\u003e: \u003c\/p\u003e","brand":"GeneBio Systems","offers":[{"title":"Default Title","offer_id":47777320861796,"sku":"P46075","price":1239.3,"currency_code":"CAD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0558\/8588\/9636\/files\/no_image_default_image-jpeg_862d6e2e-b205-4df2-ba23-de7c973c5510.jpg?v=1769449781","url":"https:\/\/www.genebiosystems.com\/products\/recombinant-neosartorya-fumigata-extracellular-metalloproteinase-mep-mep","provider":"GeneBio ","version":"1.0","type":"link"}