{"product_id":"recombinant-human-josephin-1josd1","title":"Recombinant Human Josephin-1(JOSD1)","description":"\u003cp\u003e\u003cb\u003eSize\u003c\/b\u003e: 200ug. Other sizes are also available. Please Inquire.\u003c\/p\u003e\u003cp\u003e\u003cb\u003eIn Stock\u003c\/b\u003e: No\u003c\/p\u003e\u003cp\u003e\u003cb\u003eLead time\u003c\/b\u003e: 10-20 working days\u003c\/p\u003e\u003cp\u003e\u003cb\u003eResearch Topic\u003c\/b\u003e: Cell Biology\u003c\/p\u003e\u003cp\u003e\u003cb\u003eUniprot ID\u003c\/b\u003e: Q15040\u003c\/p\u003e\u003cp\u003e\u003cb\u003eGene Names\u003c\/b\u003e: JOSD1\u003c\/p\u003e\u003cp\u003e\u003cb\u003eOrganism\u003c\/b\u003e: Homo sapiens (Human)\u003c\/p\u003e\u003cp\u003e\u003cb\u003eAA Sequence\u003c\/b\u003e: MSCVPWKGDKAKSESLELPQAAPPQIYHEKQRRELCALHALNNVFQDSNAFTRDTLQEIFQRLSPNTMVTPHKKSMLGNGNYDVNVIMAALQTKGYEAVWWDKRRDVGVIALTNVMGFIMNLPSSLCWGPLKLPLKRQHWICVREVGGAYYNLDSKLKMPEWIGGESELRKFLKHHLRGKNCELLLVVPEEVEAHQSWRTDV\u003c\/p\u003e\u003cp\u003e\u003cb\u003eExpression Region\u003c\/b\u003e: 1-202aa\u003c\/p\u003e\u003cp\u003e\u003cb\u003eSequence Info\u003c\/b\u003e: Full Length\u003c\/p\u003e\u003cp\u003e\u003cb\u003eSource\u003c\/b\u003e: E.coli\u003c\/p\u003e\u003cp\u003e\u003cb\u003eTag Info\u003c\/b\u003e: N-terminal 6xHis-SUMO-tagged\u003c\/p\u003e\u003cp\u003e\u003cb\u003eMW\u003c\/b\u003e: 39.2 kDa\u003c\/p\u003e\u003cp\u003e\u003cb\u003eAlternative Name(s)\u003c\/b\u003e: Josephin domain-containing protein 1\u003c\/p\u003e\u003cp\u003e\u003cb\u003eRelevance\u003c\/b\u003e: Deubiquitinates monoubiquitinated probes (in vitro). When ubiquitinated, cleaves 'Lys-63'-linked and 'Lys-48'-linked poly-ubiquitin chains (in vitro), hence may act as a deubiquitinating enzyme. May increase macropinocytosis and suppress clathrin- and caveolae-mediated endocytosis. May enhance mbrane dynamics and cell motility independently of its catalytic activity.\u003c\/p\u003e\u003cp\u003e\u003cb\u003eReference\u003c\/b\u003e: The DNA sequence of human chromosome 22.Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.  , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.Nature 402:489-495(1999)\u003c\/p\u003e\u003cp\u003e\u003cb\u003ePurity\u003c\/b\u003e: Greater than 90% as determined by SDS-PAGE.\u003c\/p\u003e\u003cp\u003e\u003cb\u003eStorage Buffer\u003c\/b\u003e: Tris-based buffer，50% glycerol \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","brand":"Gene Bio Systems","offers":[{"title":"Default Title","offer_id":39766937763940,"sku":"CSB-EP624012HU","price":680.95,"currency_code":"EUR","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0558\/8588\/9636\/products\/no_image_default_image-jpeg_f45b4108-3bd6-429d-9101-0e4f59de071b.jpg?v=1659197702","url":"https:\/\/www.genebiosystems.com\/en-de\/products\/recombinant-human-josephin-1josd1","provider":"GeneBio ","version":"1.0","type":"link"}