SKALP antibody Polyclonal Antibodies Primary antibodies
- Known as:
- SKALP (anti-) Polyclonal Antibodies Primary antibodies
- Catalog number:
- orb100350
- Product Quantity:
- 100
- Category:
- -
- Supplier:
- Biorb
- Gene target:
- SKALP antibody Polyclonal Antibodies Primary antibodies
Related genes to: SKALP antibody Polyclonal Antibodies Primary antibodies
- 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 Polyclonal Antibodies Primary antibodies
Related articles to: SKALP antibody Polyclonal Antibodies Primary antibodies
- The aim of this review is to synthesize current evidence on the interaction between Hippo-YAP signaling and EMT in the malignant transformation of oral potentially malignant disorders (OPMDs) to oral squamous cell carcinoma (OSCC) and to examine their potential utility as biomarkers and therapeutic targets. Design: Following PRISMA 2020 guidelines, five electronic databases (PubMed, Web of Science, Scopus, LIVIVO, and Embase) were utilized for this search. Eligible studies included human tissue-based investigations and complementary experiments evaluating YAP/TAZ or EMT markers in OPMDs and OSCC. Risk of bias was assessed using QUIN, SYRCLE, and JBI tools. - Source: PubMed
Publication date: 2026/05/25
Kazemi Kimia Sadatde Castro Costa Matheusde Carli Marina LaraLeask AndrewFranca Cristiane MirandaSperandio Felipe Fornias - Addiction is a chronic, relapsing neuropsychiatric disorder despite adverse consequences. Addiction involves neurobiological changes in the reward, motivation, and memory systems, particularly affecting the dopaminergic pathways due to a complex interaction between inherited traits and life experiences. - Source: PubMed
Publication date: 2026/05/22
Hossain Waheeda AButler Merlin G - Energy loss through windows significantly contributes to building energy consumption, highlighting the demand for transparent thermal-insulating materials. Colorless, transparent polyimide (PI) aerogels are a promising class of candidate materials, but their development has been hindered by the challenging balance among optical transparency, color quality, and thermomechanical properties. Herein, we report a colorless and transparent PI aerogel through molecular engineering of the polymer network. Optimized aerogel (PI-2) with exceptional combined properties has been fabricated via copolymerization of 4,4'-(hexafluoroisopropylidene)-diphthalic anhydride (6FDA), 4,4'-oxydianiline (ODA), and p-phenylenediamine (p-PDA), cross-linked with 1,3,5-tris-(4-aminophenoxy)-benzene (TAB) and processed via supercritical drying. The introduction of p-PDA enhances molecular chain rigidity and optimizes the nanoporous structure (peak pore size of 19.1 nm), simultaneously reducing light scattering and suppressing heat transfer. Compared to control samples without p-PDA (PI-1) or with 2,2'-dimethyl-4,4'-diaminobiphenyl (DMBZ, PI-3), PI-2 achieves colorlessness and high optical transmittance (57.1% at 800 nm) while maintaining superior thermal and mechanical performance. This work provides a strategy for developing colorless, transparent PI aerogels with potential applications for energy-efficient windows and optoelectronic devices. - Source: PubMed
Publication date: 2025/12/04
Xue TiantianTian JingLiu YanFan WeiLiu Tianxi - As frontline defenders in the innate immune system, neutrophils traffic to sites of infection by detecting chemical gradients, polarizing, and migrating towards foreign pathogens. This requires communication between small GTPases, phosphatidylinositol phosphate (PIP) lipids, and the actin cytoskeleton to generate forces that drive leading-edge membrane protrusions. Central to the coordination of these signaling events is the hematopoietic-cell-specific 5-inositol lipid phosphatase SHIP1 (or INPP5D), which shapes PIP lipid domains by dephosphorylating phosphatidylinositol-(3,4,5)-trisphosphate (PIP ) to generate PI(3,4)P . To decipher mechanisms controlling SHIP1 membrane localization during neutrophil chemotaxis, we combined genetic manipulation of SHIP1 with live cell Total Internal Reflection Fluorescence (TIRF) microscopy. Our results reveal two modes of SHIP1 localization: (1) cortical oscillations regulated by the membrane curvature sensing protein FBP17, and (2) dynamic membrane puncta organized by the adaptor protein Nck1. Localization to both membrane structures requires the proline-rich C-terminal domain (CTD) of SHIP1. Neutrophil-differentiated HL60 cells solely expressing a cytoplasmic localized SHIP1 CTD deletion mutant exhibit chemotaxis defects that phenocopy complete SHIP1 loss of function. Overall, this work reveals a dual mechanism by which SHIP1 integrates signals from membrane curvature sensing and adaptor proteins to control neutrophil cell migration. - Source: PubMed
Publication date: 2026/05/28
Amaris AltheaWaddell Grace LNoteboom Asa JDoerr SophiaDrew Emma ECollins Sean RHansen Scott D - Phosphatidylinositol 3,5-bisphosphate [PI(3,5)P] is a lysosomal signaling lipid whose deficiency, caused by mutations in the PIKfyve complex subunits FIG4 or VAC14, underlies a spectrum of fatal neurologic diseases including Charcot-Marie-Tooth type 4J (CMT4J) and amyotrophic lateral sclerosis (ALS). To map the molecular consequences of PI(3,5)P insufficiency in the brain, we performed quantitative proteomic and transcriptomic analyses of three mouse lines bearing distinct loss-of-function mutations in Fig4 or Vac14, examining the brain at the presymptomatic and end stages. Strikingly, profound neuroinflammation was already present at postnatal day 5 (before significant neurodegeneration), characterized by complement activation, interferon signaling, and parenchymal infiltration of peripheral myeloid cells and T-cells. Isolated mutant microglia exhibited a markedly pro-oxidative transcriptional state with elevated reactive oxygen species, a partly non-cell-autonomous phenotype, being present in microglia from mice with conditional Fig4 inactivation in just neurons and astrocytes. Comparison of early (P5) and late (P25) proteomics data revealed that PI(3,5)P insufficiency impairs developmental remodeling of the brain proteome: proteins typically upregulated during postnatal maturation failed to accumulate, implicating lysosomal function in neurodevelopment. We identify coordinated elevation of p53, Fas receptor, inflammatory caspases, Gasdermin D, RIPK1, and ZBP1, consistent with multifactorial inflammatory cell death with features of apoptosis, pyroptosis, and necroptosis. Many of the dysregulated proteins are encoded by genes mutated in lysosomal storage disorders, ALS, CMT, Alzheimer's and Parkinson diseases, extending the pathogenic relevance of PI(3,5)P insufficiency. Together, these findings establish that early neuroinflammation is a defining - and likely initiating - feature of neurodegeneration caused by disruption of lysosomal PI(3,5)P. - Source: PubMed
Publication date: 2026/06/03
Wong BridgetPayne MorganSilva AlexanderKurniawan EmmaEidman Alison SPizzo DonaldRajupalem RachanaLenk Guy MPaulo Joao AKhan TaimurEskelinen Eeva-LiisaGygi Steve PBrown Nicholas GMeisler Miriam HMendiola Andrew SGassaway Brandon MFerguson Cole J