

Specifications
The26Sproteasomeplaysacentralroleintheubiquitin-mediateddegradationofcellularproteins.Itconsistsofa20Scatalyticcorecappedbyoneortwo19Sregulatoryparticles.Therepeat-containingdomainsofribophorins1and2(Rpn1andRpn2,110and104kDa,respectively)representthelargestsubunitsofthe26Sproteasomeandmayalsobeinvolvedinribosomebinding.Deletionofeithersubunitislethal,andmutationsinyeastresultinimpairedproteasomefunctionandaccumulationofpolyubiquitinatedproteins.Rpn1isacomponentofthe26Sproteasomebase.Inhuman,theRpn1subunitinteractswiththeubiquitinproteinligase(E3)KIAA10.RPN1andRPN2formthereceptorsfortheubiquitin-likeproteinsRad23andDsk2.Theleucine-rich-repeat-likedomainofRPN1mayparticipateintherecognitionofthecargoproteinscarriedbyRad23forunfoldingandsubsequentdegradation.ThedeubiquitinatingenzymeUbp6/USP14recognizestheproteasomebaseviatheRpn1subunit.DeubiquitinationbyUbp6preventsRpn-mediatedtranslocationtothe20Sparticle.
Info
Source | Yeastrecombinant |
Buffer | 20mMsodiumphosphatepH7.4,500mMNaCl,200mMimidazole,1mMβ-mercaptoethanol |
Molecularweight | 109.5kDa |
Expressionhost | E.coli |
Tag | His6 |
Storage | -80°C.Avoidrepeatedfreeze/thawcycles |