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
- Two-pore channel 1 (TPC1) is an endosomal Na/Ca-selective channel implicated in membrane trafficking, endosome tubulation, and excitability, but how TPC1 regulates membrane trafficking is unknown. Using TPC1-null human cells, we demonstrate that TPC1 drives transferrin receptor (TfR) trafficking and recycling via Ca, and not Na fluxes or endosomal pH changes, since channel-targeted Ca-buffers inhibited trafficking, whereas a Na-deficient Ca-permeable TPC1 mutant fully supported trafficking. TPC1 was unique since other Ca sources did not support TfR trafficking. TPC1 activity depended on the lipid PI(3,5)P, since trafficking was impaired by a lipid-insensitive TPC1 or inhibitors of lipid synthesis. Finally, a corollary of this reduced TfR trafficking is an iron-deficiency and storage phenotype in TPC1-deficient HeLa cells and mice. Our findings highlight endosomes as unique Ca stores mobilized by a phosphoinositide-induced TPC1 channel that generates local Ca nanodomains crucial for maintaining TfR trafficking and consequent iron homeostasis. - Source: PubMed
Publication date: 2026/07/15
Burton William JLin AliceMorgan Anthony JDavis Lianne CChen Cheng-ChangGalione Antony - Cryogenic environments impose severe thermal and mechanical stresses on polymer components, yet the effects of long-term cryogenic cycling on their subsequent room-temperature performance remain insufficiently understood. This study investigated the influence of cryogenic cyclic aging on the mechanical and tribological behaviour of polyimide (PI)-based materials, including neat PI and composites reinforced with MoS, graphite, and/or PTFE. Repeated cryogenic cycling was followed by mechanical characterisation and tribological testing at 25 °C in air and vacuum. This work systematically compares neat and filled PI materials after cryogenic cyclic aging and correlates mechanical changes with transfer-film formation and wear behaviour. Cryogenic cyclic aging had only minor effects on weight and thermal stability but significantly altered the viscoelastic behaviour, increasing creep and residual strain, with variations depending on the polymer structure and filler content. Fracture toughness showed a statistically significant improvement only for PI2 (up to 93%). Changes in PI1, PI3, PI4, and PI5 fell within the experimental scatter and were interpreted as non-significant trends. In air, abrasive wear dominated in unreinforced PI, while graphite/PI composites exhibited adhesive wear and improved transfer film formation, reducing wear rates by up to 26%. In vacuum, the wear rate of aged graphite/PI increased by up to two orders of magnitude. - Source: PubMed
Publication date: 2026/07/02
Nikonovich MaksimRamalho AmilcarEmami Nazanin - Genome integrity relies on DNA mismatch repair (MMR) to correct replication errors, yet whether non-protein cofactors regulate this pathway remains unexplored. Here, we identify nuclear phosphatidylinositol-3-phosphate (PI3P) as a lipid regulator of MMR. Using biosensors, lipid pulldown, and proximity ligation assays, we show that PI3P forms discrete nuclear puncta in close proximity to the MutSα (MSH2:MSH6) and MutSβ (MSH2:MSH3) MMR recognition complexes. Pharmacological or genetic depletion of the class III PI3-kinase Vps34 impaired MutSα and MutSβ heterodimer assembly without altering MMR protein nuclear abundance, compromised DNA substrate association of MMR components in nuclear extracts, and elevated microsatellite instability at mononucleotide repeats. Exogenous PI3P enhanced MMR recognition complex assembly and DNA association in PI3P-deficient nuclear extracts, supporting a role for PI3P in promoting MMR. We further show that a nuclear Beclin-1/Vps34 complex produces this PI3P pool through an autophagy-independent mechanism. Functionally, loss of nuclear PI3P blunts MMR-dependent DNA damage signaling and confers 6-thioguanine resistance in cultured cells and in Beclin-1-deficient zebrafish in vivo. These findings reveal an autophagy-independent nuclear function for the Beclin-1/Vps34 complex in genome maintenance and identify PI3P as a lipid mediator of MMR, thereby expanding the functional repertoire of nuclear phosphoinositide signaling. - Source: PubMed
Li XinyiVicinanza MariellaLopez AnaFesta Beatrice PaolaSchlotawa LarsBarbosa Antonio DanielTakla MichaelBalmus GabrielFleming AngeleenRubinsztein David C - Gasdermin D (GSDMD) executes pyroptosis by forming membrane pores, yet how these structures assemble and are regulated in cells has remained technically inaccessible. We introduce polymer-supported plasma membranes (PSPMs), which preserve native PM properties while providing cytosolic access for nanoscopic imaging. Combining PSPMs with DNA-PAINT super-resolution microscopy, we visualize human and mouse GSDMD nanostructures directly at the PM of pyroptotic cells and uncover species-specific differences in pore size. Quantitative analyses reveal that GSDMD assembles into heterogeneous macromolecular architectures, including ring-shaped structures, which correlate with PM permeabilization. The palmitoylation-deficient C191A mutant retains minor membrane association but fails to form complete rings, indicating that ring assembly, more than membrane binding, determines pore activity. Last, we identify PI(3,4,5)P as a key regulator of pore stabilization. Its early increase during pyroptosis promotes growth of large rings, and mutations in PI(3,4,5)P-interacting residues undermine assembly. These findings define the native architecture of GSDMD pores and reveal lipid-dependent stabilization as a central mechanism regulating pyroptotic membrane permeabilization. - Source: PubMed
Publication date: 2026/07/10
Kappelhoff ShirinHoltmannspötter MichaelSchaefer Stefan LMargheritis Eleonora GAsik Özgün DogaGehle NadineVeit HannahDanial John S HFranzkoch RicoStrauss SebastianAlvelid JonatanKoerfer AgnesEggeling ChristianPsathaki Olympia EJungmann RalfKurre RainerHummer GerhardPiehler JacobCosentino Katia - Hypoglycemia remains a major cause of neurological morbidity. However, effective targeted therapies for affected brain regions remain lacking. Although excitotoxicity and energy failure have long been implicated, emerging evidence has identified dysregulated zinc signaling as a central mediator of neuronal vulnerability and recovery. During acute glucose deprivation, synapse-released zinc accumulates intracellularly, impairing mitochondrial function, activating nicotinamide adenine dinucleotide phosphate oxidase, amplifying oxidative stress, and triggering poly (ADP-ribose) polymerase-dependent cell death pathways. Notably, neuronal injury is markedly exacerbated during glucose reperfusion, when zinc-reactive oxygen species coupling drives metabolic collapse. During the recovery phase, zinc contributes to neurogenesis, synaptic remodeling, and circuit repair, underscoring its phase-dependent duality. Here, we synthesize mechanistic and translational evidence supporting zinc as a dynamic regulator of neuronal fate in hypoglycemia-induced brain injury. We propose that zinc functions as a metabolic switch linking acute oxidative injury to subsequent regenerative processes. Importantly, this framework suggests a precision-timed therapeutic strategy involving acute zinc chelation or inhibition of zinc-coupled oxidative pathways during injury, followed by controlled restoration of zinc-dependent signaling during recovery. By redefining hypoglycemic brain injury through phase-specific zinc modulation, we identify new therapeutic opportunities relevant not only to hypoglycemia but also to broader metabolic and ischemic brain disorders. - Source: PubMed
Publication date: 2026/07/09
Ko Dong GyunYang Hyun WookJeong Hyun HoPark Min KyuChoi Bo YoungWon Seok JoonSwanson Raymond ASuh Sang Won