SRPK1 Active Human Recombinant Protein
- Known as:
- SRPK1 Active Human Recombinant Protein
- Catalog number:
- 40277
- Product Quantity:
- 10
- Category:
- -
- Supplier:
- BPS Bioscience
- Gene target:
- SRPK1 Active Human Recombinant Protein
Related genes to: SRPK1 Active Human Recombinant Protein
- Gene:
- SRPK1 NIH gene
- Name:
- SRSF protein kinase 1
- Previous symbol:
- -
- Synonyms:
- SFRSK1
- Chromosome:
- 6p21.31
- Locus Type:
- gene with protein product
- Date approved:
- 1998-03-02
- Date modifiied:
- 2014-11-19
Related products to: SRPK1 Active Human Recombinant Protein
Related articles to: SRPK1 Active Human Recombinant Protein
- Cholangiocarcinoma (CCA) is an aggressive bile duct malignancy with a high incidence and mortality rate in Southeast Asia, particularly in Thailand. However, current treatments offer only limited clinical benefit. Aberrant mRNA splicing, driven by hyperactivation of serine/arginine-rich splicing factors (SRSFs) and their upstream kinases SRPK1 and SRPK2, contributes to the progression of CCA. Although SRPK inhibitors suppress tumor growth, their effects remain incomplete, highlighting the need for rational combination strategies. - Source: PubMed
Inpad ChaturongKhamsuwan PrakasitVongkaewpothong PhuwapatSusena WaritsaraKotanart KanyanutJanvilisri TavanImpheng HathaichanokSilsirivanit AtitRoytrakul SittirukKaewkong Worasak - Serine/arginine-protein kinase 1 (SRPK1) is a central regulator of alternative splicing whose overexpression drives oncogenic reprogramming in multiple cancers. To understand the phosphorylation dynamics of SRPK1 activity, we performed a systematic integrative phosphoproteomic meta-analysis of 798 profiling and 232 differential human datasets. We identified S51, S309, and S311 as the three predominant Class I phosphosites on SRPK1. High-confidence co-phosphoregulated proteins (Fisher's Exact Test < 0.05, ≥3 independent studies, ≥3 experimental conditions) revealed an extensive network of splicing factors (SRRM1, SRRM2, GPATCH8) and noncanonical RS-domain proteins (LBR) that function as both substrates and binary interactors, preferentially linked to S309 and S311. Proteogenomic interrogation via cProSite demonstrated significant upregulation of phosphorylation at these sites in breast, ovarian cancer and lung adenocarcinoma cohorts. Downstream substrates and co-regulated proteins further intersected with apoptosis regulators like SIRT2, BAD, FOXO3, and PI3K/Akt pathway components, mechanistically hinting at SRPK1 phosphorylation in apoptosis suppression and uncontrolled proliferation. These co-phosphorylation signatures therefore position SRPK1 as a potential orchestrator of splicing condensates that rewire oncogenic pathways, offering a phosphosite-specific blueprint for targeted splicing modulators and combination immunotherapies in splicing-related malignancies. - Source: PubMed
Publication date: 2026/09/24
Vijayan JishnaSubair SuhailGopalakrishnan Athira PerunellySambreena AlimathRaju RajeshRajeev Athira C - [This retracts the article DOI: 10.3727/096504018X15180508535835.]. - Source: PubMed
Publication date: 2026/09/14
- Splicing targeting drugs have emerged as promising anticancer drugs. However, their mechanisms of action remain largely unknown, notably in Non-Small Cell Lung Carcinoma (NSCLC). In this study, we demonstrated that SPHINX31, which targets SRPK1, inhibits the ATR/CHK1 signaling pathway, a cornerstone of the replicative stress response, leading to decreased cell proliferation, increased DNA damage and apoptosis, notably in NSCLC cells resistant to platinum salts. Mechanistically, we found that SRPK1 is recruited at stalled replication forks upon replicative stress, co-immunoprecipitates with the ATR/ATRIP/TOPBP1 complex, directly interacts with TOPBP1 BRCT4/5 and BRCT7/8 domains, and contributes to the accumulation of TOPBP1 nuclear foci. We further showed that SRPK1 controls the splicing of genes previously related to ATR signaling, notably WIZ. All these events are prevented by SPHINX31. Lastly, we showed that the inhibitory effects of SPHINX31 on ATR are counterbalanced by the activation of DNA-PKcs. Altogether, this study uncovers SRPK1 as a new component of the ATR/DNA-PKcs/CHK1 replicative checkpoint. SRPK1 inhibitors, alone or in combination with DNA-PKcs or CHK1 inhibitors, could provide therapeutic benefit in NSCLC patients including those who relapse after platinum-based chemotherapy. - Source: PubMed
Publication date: 2026/09/17
Shreim AmaniGenoux AurelieZubchuk NadiiaZheng HaoyangSalameh PerlaZiegelmeyer TheoDalonneau FabienRouchette MargotOddou ChristianeMiron SimonaPolveche HeleneMamode Cassim AdiilahGarrido CarmenNikolakaki EleniAuboeuf DidierJia TaoZinn-Justin SophieEymin Beatrice - Interleukin enhancer-binding factor 3 (ILF3/NF90) is a multifunctional nuclear factor implicated in diverse malignancies, yet whether ILF3 engages functionally relevant protein-protein interactions within hepatocellular carcinoma (HCC) signaling networks remains incompletely defined. Here, we show that ILF3 is upregulated in HCC across public cohorts and local tissue specimens and that higher ILF3 abundance is associated with adverse clinical features. ILF3 depletion suppresses HCC cell proliferation, migration, invasion, and xenograft growth. Unbiased immunoprecipitation-mass spectrometry identifies serine/arginine-rich protein-specific kinase 1 (SRPK1) as an endogenous interaction partner of ILF3. ILF3 knockdown reduces SRPK1 abundance by accelerating SRPK1 mRNA decay, whereas SRPK1 reconstitution restores STAT3 phosphorylation and substantially rescues the impaired malignant phenotypes. Conversely, SRPK1 knockdown phenocopies ILF3 depletion and reduces p-STAT3 (Tyr705) without materially altering total STAT3. RNA-seq and qPCR validation show coordinated disruption of JAK-STAT-related transcriptional programs after ILF3 loss, and tissue immunohistochemistry supports reduced ILF3, SRPK1, p-STAT3 (Tyr705), Bcl-2, and Ki67 in ILF3-depleted xenografts. These findings establish a functional ILF3-SRPK1-STAT3 relationship in HCC and indicate that ILF3 supports malignant progression partly by maintaining SRPK1 abundance and STAT3 signaling competence. - Source: PubMed
Publication date: 2026/07/02
Yu JianjianYang YushanGuo ZhuangyaoChen YuyiLei ShaokunDeng Xiaofang