Human Ribonuclease P/MRP protein subunit POP5 (POP5) ELISA Kit
| Product Name | Human Ribonuclease P/MRP protein subunit POP5 (POP5) ELISA Kit |
|---|---|
| Description | POP5. The deduced 163-amino acid protein has a calculated molecular mass of 18.8 kD. Western blot analysis of HeLa cells detected endogenous POP5 at an apparent molecular mass of 19 kD. HeLa cell POP5 associated with RNase MRP and RNase P RNAs. The immunoprecipitated RNase P complex was able to cleave pre-tRNA into mature tRNA and its 5-prime leader sequence, indicating that POP5 is part of the catalytically active RNase P complex. Mutation analysis showed that the C terminus of POP5 was not required for association with RNase MRP or RNase P complexes or for RNase P activity. This assay has high sensitivity and excellent specificity for detection of Human POP5. No significant cross-reactivity or interference between Human POP5 and analogues was observed. |
| Synonyms | HSPC004, RPP2, RPP20, RNase MRP/RNase P protein-like|processing of precursor 5 |
| Method | Sandwich ELISA |
| Detection Range | Request Information |
| Sensitivity | Request Information |
| Reactivity | Human |
| Sample Types | Serum, Plasma, Other biological fluids. |
| Background |
POP5. The deduced 163-amino acid protein has a calculated molecular mass of 18.8 kD. Western blot analysis of HeLa cells detected endogenous POP5 at an apparent molecular mass of 19 kD. HeLa cell POP5 associated with RNase MRP and RNase P RNAs. The immunoprecipitated RNase P complex was able to cleave pre-tRNA into mature tRNA and its 5-prime leader sequence, indicating that POP5 is part of the catalytically active RNase P complex. Mutation analysis showed that the C terminus of POP5 was not required for association with RNase MRP or RNase P complexes or for RNase P activity. |
| Supplier | Abebio |
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