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SRPKs is a critical enzyme family that regulates splicing activity in the cell. The first serine-arginine (SR) protein kinase identified is SRPK1, which is isolated from mitotic cells, and it is described to phosphorylate SR proteins and to promote their release from nuclear speckles during the G2/M phase of the cell cycle. SRPK1 is the prototype of the SRPK family, which also includes the two homologous SRPK2 and SRPK3 proteins. SRPKs are characterized by a bipartite catalytic domain separated by a unique spacer sequence and are mainly localized in the cytoplasm of mammalian cells.

SRPKs can translocate into the nucleus of cells under several conditions, such as during the G2/M phase of the cell cycle, or after osmotic stress, or as a consequence of activation of the epidermal growth factor (EGF) signal transduction pathway.

Cat. No. Product Name CAS No. Information
H2276

SRPKIN-1

 		2089226-94-6

SRPKIN-1 is a potent, selective, covalent SRPK1/2 inhibitor with IC50 of 35.6/98 nM, respectively; significantly attenuates SR protein phosphorylation in HeLa cells at 200 nM, switches VEGF splicing to produce the VEGF-A165b isoform (at 100 nM), converts the pro-angiogenic VEGF-A165a to the anti-angiogenic VEGF-A165b isoform, therefore functioning as an antagonist for VEGF-A165a to block angiogenesis; blocks laser-induced neovascularization in a murine retinal model.
H2275

SRPIN-803

 		380572-02-1

SRPIN-803 (SRPIN 803, SRPIN803) is a novel small molecule dual inhibitor of SRPK1 and CK2 with IC50 of 2.4 uM and 0.2 uM, respectively, does not inhibit SRPK2; prevents VEGF production more effectively than SRPIN340, topical administration of SRPIN803 suppresses intraocular neovascularization in mouse model.
H2274

SPHINX31

 		1818389-84-2

SPHINX31 (SPHINX 31) is a potent, selective, ATP competitive inhibitor of Serine/arginine-protein kinase 1 (SRPK1) with IC50 of 5.9 nM, displays no significant activity against other splicing modulating kinases (CLK family, DYRK1A and DYRK2, DYRK5, SRPK-2/3, PIM1, PIM2 kinases); inhibits SRPK1 mediated SRSF1 phosphorylation in PC3 prostate cancer cells with EC50 of 360 nM, dose-dependently switches splicing from VEGF-A165a to VEGF-A165b in RPE cells; potently inhibits blood vessel growth in models of choroidal angiogenesis in vivo.

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