|Datasheet||Specific References||Reviews||Related Products||Protocols|
|A DNA sequence encoding the human RIOK1 (Q9BRS2) (Met1-Lys568) was expressed with the N-terminal polyhistidine-tagged GST tag at the N-terminus.|
|Kinases are highly recommended to be shipped at frozen temperature with blue ice or dry ice.|
Shipment made at ambient temperature may seriously affect the activity of the ordered products.
|> 85 % as determined by SDS-PAGE|
|Kinase activity untested|
|< 1.0 EU per μg of the protein as determined by the LAL method|
|Samples are stable for up to twelve months from date of receipt at -70℃|
|The recombinant human RIOK1/GST chimera consists of 805 amino acids and has a calculated molecular mass of 93.4 kDa. The recombinant protein migrates as an approximately 94 kDa band in SDS-PAGE under reducing conditions.|
|Lyophilized from sterile 20mM Tris, 500mM NaCl, 10% glycerol, pH 7.4.|
1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
2. Please contact us for any concerns or special requirements.
|Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.|
|A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.|
RIOK1, also known as RIO kinase 1, is a member of the RIO family of atypical serine protein kinases first characterized in yeast. RIOK1 and RIOK2 proteins are present in organisms from Archaea to humans. RIOK1 functios as 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 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.