Type:MouseIgG
Applications:IF;WB
E=ELISA;FACS;FC=FlowCytometry;FPLC=FastProteinLiquidChromatography;GF=GravityFlow;HPLC=HighPerformanceLiquidChromatography;ICC=Immunocytochemistry;IF=Immunofluorescence;IHC=Immunohistochemistry;IP=Immunoprecipitation;NAC=Non-adherentCellAssays;NB=NeutralizationofBioactivity;SE=SandwichELISA;TPE=TargetedProteinExpression;WB=Westernblotting;;AC=AdherentCellAssays;FM=FluorescentMicsroscopy;;;BSC-CM5=BiacoreSensorChipCM5;BSM=BiosactiveSmallMoleculeorPeptide;CDM=CellDifferentiationMedia;;;;;;HealthandFitness;;;DNAExtraction/Purification;;InvivoLikeAssaysSpeciesReactivity:B;H;M;P;R
B=Bovine;Ca=Cat;Ch=Chicken;D=Dog;EQ=Equine;GP=GuineaPig;H=Human;M=Mouse;P=Porcine;Pr=Primate;R=Rat;Rb=Rabbit;Y=Yeast;Xe=Xenopus;Ze=Zebrafish;;;;NA-NotApplicable;STP=Step-TactinProteins;AllFormat:Supernatant-liquid
Immunogen:Purified,fulllengthE.ColiderivedrecombinanthumanHSP27protein.
Theheatshockproteinswerediscovered,asthenamesuggests,sincetheyareheavilyupregulatedwhencellsarestressedbytemperaturesabovethenormalphysiologicalrange.Theyareexpressedinunstressedcellsalsoandhaveanormalfunctionaschaperones,helpingotherproteinstofoldcorrectly,andarerequiredinmuchgreateramountsifthecellortissueisstressedbyheat.Theincreasedlevelsaregeneratedtranscriptionallyundertheinfluenceofapowerfultranscriptionfactor,theheatshockfactor1(HSF1).ThedifferentheatshockproteinswereoriginallynamedbasedontheirSDS-PAGEmobility,soHSP27hasananapparentmolecularweightof27kDa.
Image:HeLacellsstainingwithHSP27(red),andcounterstainedwithourchickenpolyclonalVimentinAntibodyto(green)andDNA(blue)TheHSP27antibodyrevealsstrongcytoplasmicstainingandpenetratesintotheactinrichruffledmargins,whiletheVimentinantibodyrevealscytoplasmicintermediatefilaments.ProtocolonDatasheet.
HSP27isanabundantproteinevenundernon-stressconditionsandfrequentlyshowsupasamajorspoton2dimensionalgelsofcellsortissues.Itisknowntoassociatewithavarietyofotherproteinssuchasactin,intermediatefilamentsubunitsandubiquitinandisfoundbothinthecytoplasmandthenucleusofcells.Itcanbecomeheavilyphosphorylatedundertheinfluenceofmultipleproteinkinasesparticularlyasaresultofactivationofthep38/SAPKpathway.Upregulationofthisproteinisprotectiveagainstneurodegenerativediseasesatleastincertainmousemodels.PointmutationsintheHSP27geneareassociatedwithtwoneurologicaldiseases,Charcot-Marie-Toothdiseasetype2FanddistalhereditarymotorneuropathyIIB(2).Thesediseasesareassociatedwithaxonallossapparentlyfollowingdefectsinthetransportofneurofilaments.
