SKALP antibody
- Known as:
- SKALP (anti-)
- Catalog number:
- orb100350
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Biorbyt biorb
- Gene target:
- SKALP antibody
Related genes to: SKALP antibody
- Gene:
- PI3 NIH gene
- Name:
- peptidase inhibitor 3
- Previous symbol:
- -
- Synonyms:
- ESI, SKALP, ELAFIN, WAP3, WFDC14, cementoin
- Chromosome:
- 20q13.12
- Locus Type:
- gene with protein product
- Date approved:
- 1993-07-27
- Date modifiied:
- 2015-12-16
Related products to: SKALP antibody
Related articles to: SKALP antibody
- Phosphoinositide 3-kinase (PI3K) signaling regulates protrusion, polarity, membrane uptake, and multicellular development in Dictyostelium discoideum, but these functions have been interpreted largely through canonical Class I PI3Ks and PI(3,4,5)P₃ production. This framework does not fully explain how PI3K-dependent pathways restrain Ras activity, organize relay signaling, or coordinate the transition from single-cell migration to multicellular aggregation. Here, we show that three atypical PI3K-family enzymes, PikF, PikG, and PikH, define genetically separable functions within this broader PI3K signaling network. PikF attenuates Ras-phosphoinositide-actin signaling, limiting protrusive activity so that chemotactic responses remain spatially and temporally constrained. PikG is required for aggregation and supports ACA-dependent cAMP relay, coupling cellular polarity to the collective signaling needed for streaming and multicellular development. PikH separates uptake from these chemotactic and developmental functions by supporting efficient phagocytosis with little effect on acute cAMP-stimulated signaling. Together, these findings expand the Dictyostelium PI3K framework beyond a Class I PI(3,4,5)P₃-centered pathway and identify atypical PI3Ks as specialized regulators of signal attenuation, cAMP relay organization, and membrane uptake. - Source: PubMed
Publication date: 2026/08/27
Bahlouli LaithZhang ErikJung EricBrentjens TaylorRose ElizabethDrebin HarrisonEdwards BenWischik IsabellaHuynh AlyssaCallahan WillShen JacquelineLi SusannaZhangxu KevinEdwards Marc - Activated PI3 Kinase Delta Syndrome (APDS) is a rare inborn error of immunity. To better classify the contribution of a potential new therapeutic precision agent, leniolisib, medically relevant decision criteria were assessed upon which an outcomes model was built. - Source: PubMed
Publication date: 2026/08/10
Baumann UlrichDeau Marie-CélineFranke KarstenHanitsch Leif GSogkas GeorgiosHerrmann Kirsten HBosch Dos Santos UlrichMinartz ChristofNeubauer Aljoscha SHauck Fabian - Junctional cadherin 5-associated protein (JCAD/KIAA1462) is an endothelial junctional protein encoded by a locus robustly associated with coronary artery disease and myocardial infarction in genome-wide association studies. Initially identified as a structural component of endothelial cell-cell junctions, JCAD has since emerged as a mechanosensor and regulator of key intracellular pathways (i.e. Hippo/YAP, PI3 K/Akt, and MAPK/ERK) with functional consequences for endothelial homeostasis, inflammation, and vascular tone. In this review, we summarise the current understanding of JCAD biology, from its molecular features and pathway interactions to its experimental roles in atherosclerosis, arterial thrombosis, and ischaemic stroke. We further discuss emerging translational evidence suggesting circulating JCAD as an independent predictor of adverse cardiovascular events in patients with acute coronary syndromes, and its prognostic potential in ischaemic stroke. The review also addresses the expanding biology of JCAD within the cardiovascular system, hypothesizing links to conditions such as hypertension, heart failure with preserved ejection fraction, and calcific aortic valve disease, as well as key limitations and therapeutic challenges. Overall, the available evidence highlights JCAD as a biologically plausible and potentially clinically relevant endothelial mediator, though independent validation and substantial mechanistic work remain necessary before its translational potential can be fully realized. - Source: PubMed
Publication date: 2026/08/25
Moriero MargheritaKraler SimonTirandi AmedeoDi Vece DavideLuscher Thomas FCarbone FedericoRamoni DavideBonaventura AldoCamici Giovanni GMontecucco FabrizioMinistrini StefanoWang YifanLiberale Luca - As the second most hematological malignancy, multiple myeloma (MM) is closely associated with dysregulated AKT/mTOR signaling. However, the underlying mechanism remains unclear. In the present study, we find the AKT/mTOR signaling pathway is activated by the ring finger protein RNF6. Acting as a ubiquitin ligase, RNF6 binds to and mediates PTEN polyubiquitination, altering its stability. Further investigations reveal that RNF6 specifically induces K27-linked ubiquitination of PTEN. RNF6 also prevents PTEN from translocalization to the plasma membrane, thereby inhibiting its phosphatase activity. Consistent with this finding, RNF6 promotes the production of PI(3,4,5)P3, and when PTEN is depleted, RNF6 fails to activate AKT/mTOR signaling. Moreover, we find USP39 binds to PTEN and abolishes K27-linked polyubiquitination mediated by RNF6. Furthermore, USP39 suppresses AKT/mTOR signaling transduction activated by RNF6. In addition, RNF6 is found to promote glycolysis in myeloma cells, but this effect is inhibited by USP39. Lastly, we discovered that oleandrin, a natural product, induces K48-linked polyubiquitination of RNF6 and subsequent degradation, thereby suppressing PTEN with K27-linked polyubiquitination and the AKT/mTOR signaling pathway. In conclusion, the study identifies RNF6 and USP39 as novel ubiquitin ligases or deubiquitinases responsible for K27-linked polyubiquitination of PTEN and as novel modulators of the AKT/mTOR pathway. Targeting the RNF6/PTEN/AKT/mTOR signaling axis might represent a novel therapeutic strategy for myeloma treatment. - Source: PubMed
Publication date: 2026/08/21
Zhong Yue-YaZhang Li-HuanLiu Zi-YangTao NaFan Zi-FuLi KeZhang Hong-XiaCui Yao-LiWang Ya-LiMao Xin-Liang - We present a computational investigation into the anion states of 2,4-dichloro-5-nitropyrimidine (NDP), focusing on dissociative electron attachment pathways motivated by recent mass spectrometry experiments. The molecule exhibits a unique combination of low-energy electron-induced mechanisms potentially relevant to synergistic effects in concurrent chemo-radiation cancer therapy. Our calculations reveal two bound states (π1* and π2*), three shape resonances (π3*, σCCl1*, and σCCl2*), and a π4* resonance of mixed shape and core-excited character. We attribute the intense fragmentation, [M-NO]- and [M-NO2]-, and the parent anion state at 0 eV mainly to the π3* state, characterized as either a weakly bound state or a resonance slightly above threshold. While such processes could in principle occur via vibrational Feshbach resonances, the π2* state is too deeply bound (at least by 0.71 eV) to enable this mechanism. The complex fragmentation induced by nearly zero energy electrons would instead arise from nonadiabatic interactions between the π3* state and the lower-lying bound states π1* and π2*. This coupling between bound anion states and a low-energy resonance creates pathways for internal conversion and dissociation and could be viewed as a target property for radiosensitization. - Source: PubMed
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