Date published: 2026-4-24

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SRPK1 Inhibitors

Santa Cruz Biotechnology now offers a broad range of SRPK1 Inhibitors for use in various applications. SRPK1 inhibitors are a class of compounds that selectively inhibit the activity of Serine/Arginine-rich Protein Kinase 1 (SRPK1), a kinase involved in the regulation of alternative splicing, a process crucial for generating protein diversity in cells. These inhibitors are essential tools in the field of molecular biology and biochemistry for studying the intricate mechanisms of splicing regulation and the functional roles of SRPK1 in various cellular processes. By modulating SRPK1 activity, researchers can explore the impact on gene expression, protein function, and cellular signaling pathways, providing insights into the fundamental biology of cells. Additionally, SRPK1 inhibitors have been employed in studying the post-transcriptional regulation of gene expression. The availability of high-quality SRPK1 inhibitors enables scientists to conduct precise experiments, enhancing our knowledge of cellular processes and contributing to the development of novel experimental techniques. View detailed information on our available SRPK1 Inhibitors by clicking on the product name.
Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Rottlerin

82-08-6sc-3550
sc-3550B
sc-3550A
sc-3550C
sc-3550D
sc-3550E
10 mg
25 mg
50 mg
1 g
5 g
20 g
$84.00
$166.00
$302.00
$2091.00
$5212.00
$16657.00
51
(2)

Rottlerin is a selective inhibitor of SRPK1, known for its unique ability to disrupt the phosphorylation of serine/arginine-rich proteins. It interacts with the active site of SRPK1, altering the enzyme's conformation and inhibiting its kinase activity. This modulation affects splicing factor activity and downstream signaling pathways. Rottlerin's distinct binding affinity and kinetic profile highlight its role in regulating cellular processes, particularly in the context of RNA metabolism and protein synthesis.

SRPIN 340

218156-96-8sc-394310
10 mg
$226.00
1
(1)

SRPIN 340 is a selective inhibitor of SRPK1 that uniquely alters the phosphorylation dynamics of serine/arginine-rich proteins. It engages with the enzyme's active site, inducing conformational changes that hinder its kinase function. This interaction not only impacts the phosphorylation cascade but also influences the stability and localization of splicing factors. The compound's specific binding characteristics and kinetic behavior underscore its role in modulating cellular signaling networks and RNA processing mechanisms.