SRPK2 Protein, Human (Sf9)

SRPK2 is a serine/arginine-rich protein-specific kinase that phosphorylates serine residues within the arginine/serine-rich domain (RS domain) and plays a critical role in regulating the splicing process effect. SRPK2 promotes neuronal apoptosis by upregulating cyclin-D1 (CCND1) expression and inhibiting the inhibitory effect of p53/TP53. SRPK2 Protein, Human (Sf9) is the recombinant human-derived SRPK2 protein, expressed by Sf9 insect cells , with tag free. The total length of SRPK2 Protein, Human (Sf9) is 687 a.a., .

SRPK2, a serine/arginine-rich protein-specific kinase, exhibits a specific penchant for phosphorylating serine residues within arginine/serine-rich domains, known as RS domains. Functionally, SRPK2 is integral to the phosphorylation of SR splicing factors, intricately regulating splicing processes. Notably, SRPK2 contributes to neuronal apoptosis by up-regulating cyclin-D1 (CCND1) expression, achieved through the phosphorylation of SRSF2. This phosphorylation event suppresses p53/TP53 phosphorylation, thus alleviating p53/TP53's repressive impact on cyclin-D1 (CCND1) expression. Additionally, SRPK2 plays a crucial role in spliceosomal B complex formation by phosphorylating DDX23/PRP28, and its phosphorylation of ACIN1 leads to the redistribution of ACIN1 from nuclear speckles to the nucleoplasm, resulting in up-regulation of cyclin A1. Furthermore, SRPK2 participates in modulating hepatitis B virus (HBV) replication, impacting HBV core protein phosphorylation and pregenomic RNA (pgRNA) packaging efficiency, revealing its multifaceted regulatory roles in cellular and viral processes.

Human

Sf9 insect cells

Tag Free

P78362 (S2-N688)

6733

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.