{"product_id":"recombinant-human-heat-shock-70kda-protein-6hspa6-partial","title":"Recombinant Human Heat shock 70KDA protein 6(HSPA6) ,partial","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: Cancer\u003c\/p\u003e\u003cp\u003e\u003cb\u003eUniprot ID\u003c\/b\u003e: P17066\u003c\/p\u003e\u003cp\u003e\u003cb\u003eGene Names\u003c\/b\u003e: HSPA6\u003c\/p\u003e\u003cp\u003e\u003cb\u003eOrganism\u003c\/b\u003e: Homo sapiens (Human)\u003c\/p\u003e\u003cp\u003e\u003cb\u003eAA Sequence\u003c\/b\u003e: MQAPRELAVGIDLGTTYSCVGVFQQGRVEILANDQGNRTTPSYVAFTDTERLVGDAAKSQAALNPHNTVFDAKRLIGRKFADTTVQSDMKHWPFRVVSEGGKPKVRVCYRGEDKTFYPEEISSMVLSKMKETAEAYLGQPVKHAVITVPAYFNDSQRQATKDAGAIAGLNVLRIINEPTAAAIAYGLDRRGAGERNVLIFDLGGGTFDVSVLSIDAGVFEVKATAGDTHLGGEDFDNRLVNHFMEEFRRKHGKDLSGNKRALRRLRTACERAKRTLSSSTQATLEIDSLFEGVDFYTSITRARFEELCSDLFRSTLEPVEKALRDAKLDKAQIHDVVLVGGSTRIPKVQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAVLMGDKCEKVQDLLLLDVAPLSLGLETAGGVMTTLIQRNATIPTKQTQTFTTYSDNQPGVFIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTFDIDANGILSVTATDRSTGKANKITITNDKGRLSKEEVERMVHEAEQYKAEDEAQRDRVAAKNSLEAHVFHVKGSLQEESLRDKIPEEDRRKMQDKCREVLAWLEHNQLAEKEEYEHQKRELEQICRPIFSRLYGGPGVPGGSSCGTQARQGDPSTGP\u003c\/p\u003e\u003cp\u003e\u003cb\u003eExpression Region\u003c\/b\u003e: 1-637aa\u003c\/p\u003e\u003cp\u003e\u003cb\u003eSequence Info\u003c\/b\u003e: Partial\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-tagged\u003c\/p\u003e\u003cp\u003e\u003cb\u003eMW\u003c\/b\u003e: 74.3 kDa\u003c\/p\u003e\u003cp\u003e\u003cb\u003eAlternative Name(s)\u003c\/b\u003e: Heat shock 70KDA protein B'\u003c\/p\u003e\u003cp\u003e\u003cb\u003eRelevance\u003c\/b\u003e: In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and mbrane translocation, or following stress-induced damage .\u003c\/p\u003e\u003cp\u003e\u003cb\u003eReference\u003c\/b\u003e: NIEHS SNPs programThe DNA sequence and biological annotation of human chromosome 1.Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.  , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.Nature 441:315-321(2006)\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":39766968303716,"sku":"CSB-EP863082HU","price":126700.0,"currency_code":"JPY","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0558\/8588\/9636\/products\/no_image_default_image-jpeg_7383dd9e-be99-4895-bd81-49171c63338f.jpg?v=1659197405","url":"https:\/\/www.genebiosystems.com\/en-jp\/products\/recombinant-human-heat-shock-70kda-protein-6hspa6-partial","provider":"GeneBio ","version":"1.0","type":"link"}