Anti-Human SRPK2 Antibody Pair

Product Description: SRSF protein kinase 2 (SRPK2) is a serine/arginine-rich protein kinase that plays a critical role in pre-mRNA splicing by phosphorylating serine/arginine (SR) proteins, which are essential for spliceosome assembly and function. SRPK2 is highly expressed in the brain and is involved in the regulation of alternative splicing, influencing various cellular processes such as cell proliferation, differentiation, and apoptosis. It has been shown to interact with several signaling pathways, including the mTORC1 pathway, which regulates lipid metabolism and affects cancer cell growth. Dysregulation of SRPK2 has been implicated in various diseases, particularly cancer, its overexpression has been associated with poor prognosis in melanoma and other malignancies due to its role in promoting cell migration and invasion. Protein Function: Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing (PubMed:18559500, PubMed:21056976, PubMed:9472028). Promotes neuronal apoptosis by up-regulating cyclin-D1 (CCND1) expression (PubMed:19592491). This is done by the phosphorylation of SRSF2, leading to the suppression of p53/TP53 phosphorylation thereby relieving the repressive effect of p53/TP53 on cyclin-D1 (CCND1) expression (PubMed:21205200). Phosphorylates ACIN1, and redistributes it from the nuclear speckles to the nucleoplasm, resulting in cyclin A1 but not cyclin A2 up-regulation (PubMed:18559500). Plays an essential role in spliceosomal B complex formation via the phosphorylation of DDX23/PRP28 (PubMed:18425142). Probably by phosphorylating DDX23, leads to the suppression of incorrect R-loops formed during transcription, R-loops are composed of a DNA:RNA hybrid and the associated non-template single-stranded DNA (PubMed:28076779). Can mediate hepatitis B virus (HBV) core protein phosphorylation (PubMed:12134018). Plays a negative role in the regulation of HBV replication through a mechanism not involving the phosphorylation of the core protein but by reducing the packaging efficiency of the pregenomic RNA (pgRNA) without affecting the formation of the viral core particles (PubMed:16122776) [The Uniprot Consortium]