Perfringolysin O Protein, Clostridium perfringens, Recombinant (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 68.7 kDa and the accession number is P0C2E9.
Pack Size | Availability | Price/USD | Quantity |
---|---|---|---|
20 μg | 20 days | $ 360.00 | |
100 μg | 20 days | $ 678.00 | |
1 mg | 20 days | $ 2,300.00 |
Description | Perfringolysin O Protein, Clostridium perfringens, Recombinant (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 68.7 kDa and the accession number is P0C2E9. |
Species | C.perfringens |
Expression System | E. coli |
Tag | N-6xHis-SUMO |
Accession Number | P0C2E9 |
Amino Acid | KDITDKNQSIDSGISSLSYNRNEVLASNGDKIESFVPKEGKKTGNKFIVVERQKRSLTTSPVDISIIDSVNDRTYPGALQLADKAFVENRPTILMVKRKPININIDLPGLKGENSIKVDDPTYGKVSGAIDELVSKWNEKYSSTHTLPARTQYSESMVYSKSQISSALNVNAKVLENSLGVDFNAVANNEKKVMILAYKQIFYTVSADLPKNPSDLFDDSVTFNDLKQKGVSNEAPPLMVSNVAYGRTIYVKLETTSSSKDVQAAFKALIKNTDIKNSQQYKDIYENSSFTAVVLGGDAQEHNKVVTKDFDEIRKVIKDNATFSTKNPAYPISYTSVFLKDNSVAAVHNKTDYIETTSTEYSKGKINLDHSGAYVAQFEVAWDEVSYDKEGNEVLTHKTWDGNYQDKTAHYSTVIPLEANARNIRIKARECTGLAWEWWRDVISEYDVPLTNNINVSIWGTTLYPGSSITYN |
Construction | 29-500 aa |
Protein Purity | > 90% as determined by SDS-PAGE. |
Molecular Weight | 68.7 kDa (predicted) |
Formulation | Tris-based buffer, 50% glycerol |
Reconstitution | A Certificate of Analysis (CoA) containing reconstitution instructions is included with the products. Please refer to the CoA for detailed information. |
Stability & Storage |
Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at-80℃. For reconstituted proteinsolutions, the solution can be stored at -20°c to -80'c for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots. |
Shipping |
In general, Lyophilized powders are shipping with blue ice. Solutions are shipping with dry ice. |
Research Background | A cholesterol-dependent toxin that causes cytolysis by forming pores in cholesterol-containing host membranes. After binding to target membranes, the protein assembles into a pre-pore complex. A major conformational change leads to insertion in the host membrane and formation of an oligomeric pore complex. Cholesterol is required for binding to host cell membranes, membrane insertion and pore formation; cholesterol binding is mediated by a Thr-Leu pair in the C-terminus. Can be reversibly inactivated by oxidation. |
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