SRPK1 Antibody (YA6780)

SRPK1 (serine/arginine protein kinase 1) is a highly RS-domain-specific protein kinase that phosphorylates serine/arginine-rich splicing factors, particularly SRSF1 (ASF/SF2), thereby regulating constitutive and alternative pre-mRNA splicing through control of splicing-factor localization and activity^[1][2]. Mechanistically, SRPK1 functions as a central regulator of RNA-processing networks by directing phosphorylation-dependent splicing programs that influence gene expression and cellular behavior^[1][2]. Among the biological pathways linked to SRPK1, regulation of VEGF alternative splicing is one of the most extensively characterized, where SRPK1-mediated activation of splicing factors favors pro-angiogenic VEGF isoforms, whereas reduced SRPK1 activity shifts splicing toward anti-angiogenic variants such as VEGF165b^[3][4]. Consequently, SRPK1 has been implicated in tumor angiogenesis, cancer progression, and therapeutic resistance across multiple malignancies, including prostate cancer, non-small cell lung cancer, lymphoma, and other solid tumors^[3][5][6]. In experimental cancer models, suppression of SRPK1 reduced tumor growth, decreased microvessel density, induced apoptosis, or enhanced sensitivity to anticancer therapies, supporting its functional importance in disease-associated splicing programs^[3][5][6]. Compared with the closely related isoform SRPK2, SRPK1 is frequently investigated as a distinct therapeutic target because selective modulation of SRPK1-dependent splicing events has demonstrated measurable effects on angiogenic signaling and tumor phenotypes in preclinical systems^[4]. For experimental applications, small-molecule inhibitors including SRPIN340, SPHINX, SPHINX31, and SRPKIN-1 have been widely used to inhibit SRPK1 activity and to evaluate the consequences of splice-switching and anti-angiogenic responses in disease models^[4].