SRPK1 antibody
- Known as:
- SRPK1 (anti-)
- Catalog number:
- orb100678
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Biorbyt biorb
- Gene target:
- SRPK1 antibody
Related genes to: SRPK1 antibody
- 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 antibody
Related articles to: SRPK1 antibody
- 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 - Gapmer antisense oligonucleotides (ASOs) enable sequence-specific degradation of target mRNAs, offering therapeutic access to previously "undruggable" genes and holding great promise for treating chronic and genetic diseases. However, the rapid development of ASO therapeutics remains limited by challenges in rational sequence design and translational validation. Here, we present ClinASO, an integrated computational-experimental platform that unifies key determinants of ASO efficacy-including RNase H1 cleavage preference, SNP avoidance, off-target filtering, and cross-species conservation-into a single, data-driven workflow. This system enables rapid identification of potent ASO leads and direct validation in wild-type animal disease models. Using ClinASO, we efficiently identified potent ASOs against and , both exhibiting superior silencing activity compared to their clinical counterparts. Furthermore, ClinASO generated a potent ASO targeting genes implicated in metabolic dysfunction-associated liver disease (MASLD). In multiple human cells, the ASO achieved robust silencing effect. Notably, by conjugating GalNAc, this ASO demonstrated durable, liver-specific knockdown, significantly ameliorating hepatic steatosis and normalizing systemic lipid profiles in MASLD mouse model. Together, these findings establish ClinASO as an efficient, experimentally validated online tool for the rational design and rapid development of translatable ASO therapeutics. - Source: PubMed
Publication date: 2026/04/16
Chen ShunkaiLiu HaoCong DeziDong AoWang YuhangBi JingyiGuo ShijieYang JuanWang XiaoleiRen GuipingZhang KeWang HaishengLai FanDang Yunkun - Early detection of colon adenocarcinoma (COAD) remains suboptimal. Fecal tests fail to diagnose 30% of stage I cancer, and serum CEA lacks sensitivity (< 40%). Extracellular vesicles (EVs) circulate systemically and package tumor-related cargo, making them attractive non-invasive biomarkers for cancer diagnosis. We profiled the EV proteome from 233 human patients using LC-MS/MS, including stage I‑IV tumors with matched non‑tumor colon tissues (n = 50 each; n = 100), paired pre‑/post‑operative plasma (n = 90) and healthy plasma (n = 43). Circulating EVs contained both tumor-specific and stromal/immune cell-derived proteins, reflecting the systemic nature of EV biology in the cancer setting. Proteomic analysis identified 745 proteins enriched in tumor-derived EVs (e.g., SRPK1, THBS2) and 127 proteins enriched in adjacent tissues. Plasma EVs revealed 166 proteins enriched in COAD (e.g., UBA1, FCN1) and 233 enriched in healthy controls. Pathway analysis linked tumor EV cargo to angiogenesis, mRNA splicing, TGF‑β signalling and RNA translation. Notably, a cross-cancer comparison (pancreatic = 10, lung = 14 cases) revealed that 76% of tumor EV proteins were COAD-specific, highlighting tissue of origin specificity. We further developed a 10-protein EV panel comprising seven tumor-associated and three healthy-enriched EV proteins, which effectively distinguished COAD patients from healthy controls in the two validation cohorts (n = 104 and n = 215), achieving > 90% sensitivity for differentiating COAD from healthy and non-COAD colorectal conditions. Six weeks after curative resection, tumor-associated EV proteins decreased by > 70%, whereas healthy-associated proteins rebounded to baseline, indicating surgical responsiveness. Collectively, EV protein signatures provide a sensitive and tissue-specific window into tumor-host communication, further supporting blood-based early detection of COAD. - Source: PubMed
Seo YuraHan Yoon DaeBojmar LindaKim Kyung-ASeo YurinKim Taeyul KLee SuhoKim YeleemChoi Hye BinLim Yujin HKim Chae HyunSandberg AlexanderFan ChuanwenLauritzen PernilleMolina HenrikPeralta ChristopherGeri Jacob BBurdette ColinHan Dai HoonGee Heon YungLee InsukShin Jeon-SooKim HyunwookLi LeonTobias Gabriel CWortzel InbalShin Sang JoonJung Hyo-IlLee Min GooPaik SoonmyungSchwartz Robert EAhn Joong BaeLyden DavidKim Han Sang - Resistance to lenvatinib remains a major barrier in the treatment of advanced hepatocellular carcinoma (HCC), underscoring the urgent need to elucidate the underlying mechanisms and identify actionable therapeutic targets. In this study, we identified a neurosecretory factor derived from HCC cells, Nerve Growth Factor (NGF), as a critical mediator of lenvatinib resistance. Utilizing an innovative in vivo-in vitro cross-circulated strategy, we established a phenotypically stable lenvatinib-resistant HCC cell line (LenR-cells). Through proteomic screening of conditioned media and subsequent functional validation, we demonstrated that NGF secretion progressively increases with the acquisition of resistance. Mechanistically, we uncovered that the SRPK1-SRSF1 axis drives enhanced NGF production by regulating alternative splicing of its precursor transcript, specifically promoting the expression of a shorter, translationally efficient isoform (proNGF-B). Elevated NGF subsequently activates the non-canonical MAPK pathway (MEK5-ERK5) via its high-affinity receptor TrkA, thereby sustaining tumor cell viability and proliferation under sustained tyrosine kinase inhibitor pressure. Critically, pharmacological co-targeting of TrkA with the clinically approved inhibitor larotrectinib restored lenvatinib sensitivity in both patient-derived organoids and xenograft models, producing marked synergistic anti-tumor effects without evidence of exacerbated toxicity. Clinical analyses of two independent patient cohorts further confirmed that elevated NGF expression is significantly associated with poor response to lenvatinib, shorter recurrence-free survival, and worse overall survival. Our findings unveil a critical and previously underappreciated role for tumor-derived NGF in orchestrating adaptive signaling through a precise post-transcriptional regulatory circuit and propose a readily translatable, biomarker-guided combination strategy to overcome lenvatinib resistance in HCC. - Source: PubMed
Publication date: 2026/04/05
Xu MinghaoZheng YiminZhao LongtaoWang SiweiChen JunboFu ZhongchiMa AyingLiang BugangHuang YilanXu HaihanWang YueAi YingjieZeng HaiyingGao ChaoCai JiabinKe AiwuFan Jia - Protein phosphorylation regulates key events of male germ cell differentiation. In the testis, SRPK1 and PP1γ are involved in protamine phosphorylation and dephosphorylation, respectively, and their deregulation is linked to defective chromatin structure and male infertility. The aim of this study was to expand our knowledge on the molecular role of these phosphorylation-modulating proteins through the identification of novel partners in the testis, potentially supporting additional roles in sperm development. Using immunoprecipitation followed by LC-MS/MS, we identified yet undescribed interactions of SRPK1 and PP1γ with proteins involved in sperm formation and regulation of spermatogenic gene expression. We reported that SRPK1 interacts with the key splicing regulator ASF/SF2, as well as with other proteins involved in posttranscriptional regulation such as PABP1 or IGF2BP3. We showed that the testis-enriched isoform 2 of PP1γ (PP1γ2) interacts with PIHI1D1, part of the R2TP chaperone complex, and predicted that ZFR, NDUFB10 and ILF2 interactions with PP1γ2 happen within the C-terminal sequence which is specific of PP1γ2 proteoform. Both SRPK1 and PP1γ interactomes include ILF2 and TBLX1R1, with roles in gene expression regulation. Most of the identified proteins are known phosphoproteins in male germ cells, supporting a functional interaction. Overall, our results suggest additional roles for SRPK1 and PP1γ during spermatogenesis, shedding light into the orchestrated regulation of the complex mechanisms driving sperm formation. Data are available via ProteomeXchange with identifiers PXD054959 and PXD054960. SIGNIFICANCE OF THE STUDY: In the present work, we report the first testicular protein interactome of two broad phosphorylation-modulating proteins, the kinase SRPK1 and the phosphatase PP1γ, known to be essential regulators of chromatin remodeling during male germ cell development. Our novel protein-protein interactions reveal additional roles for SRPK1 and PP1γ in male germ cells, in key processes including splicing, gene expression, protein homeostasis, or formation of sperm-specific structures. Our data will therefore contribute to a better understanding of the complex and orchestrated molecular mechanisms controlling testicular activity and proper sperm formation. The lack of male germ cell-specific protein-protein interaction datasets currently challenges the research on the still largely unknown molecular mechanisms driving male germ cell differentiation. This jeopardizes exploratory approaches and in silico validations in a testis-specific manner, as most available datasets have been obtained in somatic cells. Thus, our protein-protein interaction data will be a useful resource to those interested in identifying the origins of male reproductive health problems related to protein phosphorylation. Furthermore, our analyses suggesting that some of these interactions may also occur in other organs extend the relevance of our findings to the broader scientific community. - Source: PubMed
Publication date: 2026/03/30
de la Iglesia AlbertoBlanco MélinaJodar MeritxellFeudjio OlivierLeduc MarjorieCastillo JuditCocquet JulieOliva Rafael