VRK1 Protein, Human (sf9)

The VRK1 protein is a serine/threonine kinase that complexly regulates the cell cycle, nuclear condensation, and transcription. It critically induces Golgi disassembly during the cell cycle via PLK3 phosphorylation, thereby affecting Golgi fragmentation. VRK1 Protein, Human (sf9) is the recombinant human-derived VRK1 protein, expressed by Sf9 insect cells, with tag free.

VRK1, a serine/threonine kinase, intricately participates in cell cycle regulation, nuclear condensation, and transcriptional control. Through its diverse functions, VRK1 exhibits a multifaceted impact on cellular processes. Notably, it plays a crucial role in Golgi disassembly during the cell cycle, a process initiated by phosphorylation from PLK3 during mitosis, ultimately leading to Golgi fragmentation. VRK1 further modulates the intricate network of p53/TP53, phosphorylating 'Thr-18' and potentially impeding the interaction between p53/TP53 and MDM2. In response to DNA damage, VRK1 phosphorylates KAT5, fostering its association with chromatin and enhancing histone acetyltransferase activity. Moreover, VRK1 influences nuclear dynamics by phosphorylating BANF1, disrupting its DNA-binding capability, reducing its interaction with LEM domain-containing proteins, and triggering its relocalization from the nucleus to the cytoplasm. Additionally, VRK1 targets ATF2, activating its transcriptional activity and further expanding the regulatory repertoire of this versatile kinase.

Human

Sf9 insect cells

Tag Free

Q99986 (N-G&P, M1-K396)

7443  [NCBI]

Full Length

MPRVKAAQAGRQSSAKRHLAEQFAVGEIITDMAKKEWKVGLPIGQGGFGCIYLADMNSSESVGSDAPCVVKVEPSDNGPLFTELKFYQRAAKPEQIQKWIRTRKLKYLGVPKYWGSGLHDKNGKSYRFMIMDRFGSDLQKIYEANAKRFSRKTVLQLSLRILDILEYIHEHEYVHGDIKASNLLLNYKNPDQVYLVDYGLAYRYCPEGVHKEYKEDPKRCHDGTIEFTSIDAHNGVAPSRRGDLEILGYCMIQWLTGHLPWEDNLKDPKYVRDSKIRYRENIASLMDKCFPEKNKPGEIAKYMETVKLLDYTEKPLYENLRDILLQGLKAIGSKDDGKLDLSVVENGGLKAKTITKKRKKEIEESKEPGVEDTEWSNTQTEEAIQTRSRTRKRVQK

Approximately 47 kDa, based on SDS-PAGE under reducing conditions, due to the glycosylation.

≥ 95%, as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.