| Product Name | Human Serine/threonine-protein kinase RIO1 (RIOK1) ELISA Kit |
|---|---|
| Description | RIOK1 includes two alternatively spliced transcript variants, which encode different isoforms. The function of this gene has not been determined. RioK1, a new interactor of protein arginine methyltransferase 5 (PRMT5), competes with pICln for binding and modulates PRMT5 complex composition and substrate specificity. RioK1 and pICln bind to PRMT5 in a mutually exclusive fashion. This results in a PRMT5-WD45/MEP50 core structure that either associates with pICln or RioK1 in distinct complexes. RioK1 functions in analogy to pICln as an adapter protein by recruiting the RNA-binding protein nucleolin to the PRMT5 complex for its symmetrical methylation. The exclusive interaction of PRMT5 with either pICln or RioK1 thus provides the first mechanistic insight into how a methyltransferase can distinguish between its substrate proteins. This assay has high sensitivity and excellent specificity for detection of Human RIOK1. No significant cross-reactivity or interference between Human RIOK1 and analogues was observed. |
| Synonyms | AD034, FLJ30006, MGC12903, bA288G3.1, RIO kinase 1|prematurely truncated due to insertion of intronic sequence |
| Method | Sandwich ELISA |
| Detection Range | 0.312-20 ng/mL |
| Sensitivity | 0.133 ng/mL |
| Reactivity | Human |
| Sample Types | Serum, Plasma, Other biological fluids. |
| Background | RIOK1 includes two alternatively spliced transcript variants, which encode different isoforms. The function of this gene has not been determined. RioK1, a new interactor of protein arginine methyltransferase 5 (PRMT5), competes with pICln for binding and modulates PRMT5 complex composition and substrate specificity. RioK1 and pICln bind to PRMT5 in a mutually exclusive fashion. This results in a PRMT5-WD45/MEP50 core structure that either associates with pICln or RioK1 in distinct complexes. RioK1 functions in analogy to pICln as an adapter protein by recruiting the RNA-binding protein nucleolin to the PRMT5 complex for its symmetrical methylation. The exclusive interaction of PRMT5 with either pICln or RioK1 thus provides the first mechanistic insight into how a methyltransferase can distinguish between its substrate proteins. |
| Supplier | Abebio |
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