Lucerna/Diglycyl-Lysine Antibody, clone GX41 (100 µg)/30-0100/0100

OTHERTOOLSANDRESOURCES 

REFERENCEFORTHEPRODUCT: 

Globalanalysisoflysineubiquitinationbyubiquitinremnantimmunoaffinityprofiling. XuG,PaigeJS,JaffreySR.NatureBiotechnology. 2010Aug;28(8)868-73.

THISPRODUCTWASCITEDIN: 

A proteome-wide, quantitative survey ofinvivo ubiquitylation sites reveals widespread regulatory roles. WagnerSA, etal. Molecular&CellularProteomics. 2011Sep.  

  
Proteomicanalysesrevealdivergentubiquitylationsitepatternsinmurinetissues.WagnerSA,etal. Molecular&CellularProteomics.2012Jul.

Systems-wideanalysisofubiquitylationdynamicsrevealsakeyroleforPAF15ubiquitylationinDNA-damagebypass.PovlsenLK,etal. NatureCellBIOLOGy. 2012Sep.

QUALITYASSURANCE:EachantibodybatchismeasuredforitsABIlitytobindtoproteinscontainingdiglycyl-lysineandtorecoverdiglycyl-lysine-containingpeptidesfromtrypticdigestsofHEK293cells.

USAGESTATEMENT:Thisproductisintendedforresearchuseonlyandarenottobeusedforanyotherpurpose,whichincludesbutisnotlimitedto,unauthorizedcommercialuses,invitrodiagnosticuses,exvivoorinvivotherapeuticusesoranytypeofconsumptionorapplicationtohumansoranimals.Duetothehighlyspecificnatureofantibodiesandantigens,wecannotpredictorbeheldresponsIBLewithrespecttohowLucerna^TMproductswillbehaveinitscustomers"systems.ResearchersusingLucerna^TMproductsshouldconductoptimizationstudiestoachievetheoptimalresultpossiblefortheirintendedapplication.

LICENSING:CornellUniversityhasfiledausepatentonproteomicmethodsthatusethediglycyl-lysineantibodytoidentifyubiquitinatedproteins.Allcommercial usersshouldcontactCornellUniversityforauselicense.

GX41antibodyrecognizesthediglycyl-lysinemoietyatubiquitinatedsitesaftertrypsindigestion

Specificityofanti-diglycyl-lysine(cloneGX41)isverifiedbywesternblotanalysisofbeta-lactoglobulin,lysozyme,orratbrainlysate,inwhichthelysineswereeitherunmodified(A)ormodifiedwithGly-Gly(B),respectively. Asshownabove,theGX41exhibitsnodetectablereactivitywithproteinsunlessthelysinesaremodifiedwithGly-Gly.

Equimolaramountsofthetwopeptides(GGDRVYIHPFHLandAc-SYSMEHFRWGK*PV-NH2)wereimmunoprecipitatedwithimmobilizedGX41antibodyandanalyzedbyMALDI-TOFMS.K*referstoalysinewithaGly-Glymodification. Asshownabove,theunmodifiedpeptideisabsentfromtheimmunoprecipitate,whilethepeptidecontainingtheGly-Glymodificationisimmunoprecipitated.