(Suc-LLVY)2-Rhodamineisafluorogenicsubstrateforthechymotrypsin–likeactivityofthe20Sand26Sproteasomes.Workingconcentrationsofthissubstrateis20-100µM.ThereleasedRhodamine110fluorescencecanbedetectedbyafluorimeterorplatereaderatexcitation/emissionof495nm/520nm,respectively.ComparedtoAMC,Rhodamine110isexcitedatlongerwavelengththatcansignificantlyenhancethesignal/noiseratio.ThissubstrateisextremlyvaluableforscreeningsmallchemicalinhibitorsofproteasomesbyavoidingtheinterferencefromchemicalcompoundautofluorescencethatoftenoccursatshorterwavelengthsaroundUVornear-UVregions.
Whenusedtodetermineproteasomeactivityincelllysates,celllysatesthatarepre-treatedwithaproteasomeinhibitorsuchasMG132,PS341orepoxomicincanbeusedtodeterminethefluorescencecontributedbyothercellularproteasesthatcleavethissubstrate.Re
ADIngsfromproteasomeinhibitor-treatedlysatesshouldbesubtracted.
ProductName: | (Suc-Leu-Leu-Val-Tyr)2-Rhodamine110 |
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AlsoKnownAs: | (Suc-LLVY)2-Rhodamine110 |
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CatalogNo.: | G1110 |
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Size: | 2mg |
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MolecularWeight: | 1507.7Da |
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Species: | N/A |
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Source: | Synthetic |
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Stock: | Powder |
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Concentration: | N/A |
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QualityAssurance: | >98%byHPLCandNMR |
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Storage: | EligIBLeforroomtemperatureshipping.Storeat-80°Cuponreceiving;avoidmultiplefreeze-thawcyclesafterdissolvinginDMSO. |
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PDFDataSheet: | DownloadPDFdatasheet,MSDS |
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NCBIRefSeq: | N/A |
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Image(s): | No |
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ShippingMethod: | Roomtemperatureshipping |
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References: | No |
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Details
(Suc-LLVY)2-Rhodamineisafluorogenicsubstrateforthechymotrypsin–likeactivityofthe20Sand26Sproteasomes.Theworkingconcentrationsofthissubstrateis20-100µM.ThereleasedRhodamine110fluorescencecanbedetectedbyafluorimeterorplatereaderatexcitation/emissionof495nm/520nm,respectively.ComparedtoAMC,Rhodamine110isexcitedatlongerwavelengththatcansignificantlyenhancethesignal/noiseratio.ThissubstrateisextremlyvaluableforscreeningsmallchemicalinhibitorsofproteasomesbyavoidingtheinterferencefromchemicalcompoundautofluorescencethatoftenoccursatshorterwavelengthsaroundUVornearUVregions.Whenusedtodetermineproteasomeactivityincelllysates,celllysatesthatarepre-treatedwithaproteasomeinhibitorsuchasMG132,PS341orepoxomicinshouldbeusedtodeterminethefluorescencecontributedbyothercellularproteasesthatcleavethissubstrate.Readingsfromproteasomeinhibitor-treatedlysatescanbesubtractedasbackground.
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