Asporin _ ASPN Antibody
- Known as:
- Asporin _ ASPN Antibody
- Catalog number:
- AF1120a
- Product Quantity:
- 0.1mg
- Category:
- -
- Supplier:
- Abgen
- Gene target:
- Asporin _ ASPN Antibody
Related genes to: Asporin _ ASPN Antibody
- Gene:
- ASPN NIH gene
- Name:
- asporin
- Previous symbol:
- -
- Synonyms:
- FLJ20129, SLRR1C, PLAP-1
- Chromosome:
- 9q22.31
- Locus Type:
- gene with protein product
- Date approved:
- 2001-03-21
- Date modifiied:
- 2017-07-14
Related products to: Asporin _ ASPN Antibody
Related articles to: Asporin _ ASPN Antibody
- Lanthipeptides represent the largest group of ribosomally synthesized and post-translationally modified peptides (RiPPs). Lanthipeptides offer promising avenues for discovering new antibacterial and antifungal agents. Here, we identify and structurally analyze the product of the BGC, which encodes a class II lanthipeptide in the thermophilic bacterium sp. DSM 45891. Heterologous co-expression of the lanthipeptide synthetase TlaM resulted in modification of the two precursor peptides TlaA1 and TlaA2, which share 58% identity. TlaA1 was dehydrated seven times and TlaA2 six times. In both peptides, four thioether rings were formed with two overlapping DL-(methyl)lanthionine rings at the C-terminus. Both peptides also contain two central and N-terminal non-overlapping DL-methyllanthionines. These findings demonstrate that these peptides deviate from the general rule of stereoselective LL-(methyl)lanthionine formation from a DhxDhxXxxXxxCys motif (Dhx = dehydroalanine or dehydrobutyrine). AspN-cleaved TlaM-modified TlaA1 displayed anti-microbial activity against a subset of bacteria including Gram-negative ESKAPE pathogens. We named the lantibiotic thermolanthin. - Source: PubMed
Publication date: 2026/04/04
Weir EnleyonaZhu Lingyangvan der Donk Wilfred A - The evolution of Spinal Cord Stimulation (SCS) from simple bipolar programming to sophisticated physiologic closed-loop technology has introduced significant complexity into programming and associated reimbursement coding and billing. To address these challenges, the American Society for Pain and Neuroscience (ASPN) developed this evidence-based consensus document to establish best practices for integrating advanced SCS programming into clinical workflows. - Source: PubMed
Publication date: 2026/01/18
Deer Timothy RNairizi AliHunter Corey WKalia HemantPope Jason ECornidez Eric GSayed DawoodSmith Gregory LGoree Johnathan HAntony Ajay BStaats Peter SGilligan ChristopherKarcz MarcinTrainor DrewBroachwala Mustafa YReynolds DustinBloomfield AndrewVu Chau MLad Shivanand PTrainer RobertMonacelli CarlaDevers JolaynePetersen Erika A - Intrinsically disordered proteins and proteins containing intrinsically disordered regions often harbor sequences that are difficult to digest with conventional proteases, such as trypsin, Asp-N, or pepsin. In particular, proline-rich regions (PRRs) resist efficient proteolysis and limit sequence coverage in proteomic workflows. Nepenthesins originate from pitcher plants, combining high catalytic activity and stability under acidic conditions with a broad substrate specificity. We describe a workflow for the extraction and purification of native nepenthesin (NEP-NAT) from greenhouse-cultivated Nepenthes species, followed by the enzyme's covalent immobilization on POROS-AL chromatographic material. The performance of the NEP-NAT reactor was evaluated in an online digestion liquid chromatography/tandem mass spectrometry setup for accelerated proteolysis, showing a high proteolytic activity for myoglobin, α-synuclein, and insulin-like growth factor 2 mRNA-binding protein 1. While commercial nepenthesin columns yielded broad coverage for structured proteins, the NEP-NAT reactor generated the largest number of peptides for the intrinsically disordered protein α-synuclein. Cleavages at Pro residues showed enhanced digestion in the PRR of the tumor suppressor protein p53, where conventional proteases show limited activity. These results confirm NEP-NAT as a potent protease in proteomics workflows, offering enhanced access to Pro-rich and disordered domains that are largely inaccessible to common proteases. - Source: PubMed
Wall ChristianHause FrankGrimm WiebkeOtto Florian WSiefke ErikKipping MarcSinz Andrea - Despite advances in oral cancer treatment, therapeutic resistance remains a major challenge. Cancer-associated fibroblasts (CAFs) play a pivotal role in shaping the tumor microenvironment. Building on our previous findings on immune responses in gingival fibroblasts, we investigated the immune characteristics of CAFs. Myofibroblast CAF-like cells (myCAF-like) were established using a co-culture system and compared with gingival fibroblast-derived myofibroblasts. MyCAF-like cells exhibited markedly reduced expression of TLR3 and TLR4, whereas RIG-I, COX-2, IL-1β, IL-6, and IL-8 were significantly upregulated. Activation of p38 MAPK signaling contributed to the increased expression of COX-2 and pro-inflammatory cytokines, and TGF-β was involved in the phenotypic transformation of gingival fibroblasts into myCAF-like cells. Microarray analysis revealed upregulation of IL-1α, IL-1β, CXCL8, PTGS2, and CXCL5, alongside downregulation of OMD, COL15A1, and ASPN in myCAF-like cells. Collectively, these findings demonstrate that CAFs acquire a distinct inflammatory signature that differs from gingival fibroblasts and promotes tumor invasion and progression. Targeting CAF-associated inflammatory and signaling pathways may represent a promising strategy to overcome tumor infiltration and treatment resistance in oral cancer. - Source: PubMed
Kubota KoseiFurudate KenMatsumiya TomohNarita NorihikoTamura YoshihiroIkami EijiKobayashi Wataru - Periodontal disease is a chronic inflammatory condition that destroys tooth-supporting tissues, particularly the alveolar bone and the periodontal ligament, and effective regenerative therapies remain limited. While the role of metabolic-epigenomic crosstalk in determining cell fate is well established, the specific mechanism by which a tricarboxylic acid (TCA) cycle metabolite can modulate chromatin regulation to promote periodontal regeneration remains to be elucidated. The impact of one TCA cycle metabolite, alpha-ketoglutarate (α-KG), was examined in human periodontal ligament fibroblasts cultured under osteogenic induction and profiled by ALP assays, RT-qPCR, analyses of multiple histone modifications, ATAC-seq, and RNA-seq. α-KG increased ALP activity and upregulated genes associated with osteogenesis and the extracellular matrix (ECM). ATAC-seq revealed minimal genome-wide accessibility changes, whereas histone analyses showed reduced H3K27me3, consistent with an epigenetic mechanism that does not require extensive chromatin opening. The RNA-seq identified 14 upregulated α-KG-induced genes, including multiple components of the --/- loci, supporting an osteogenic/ECM transcriptional program. In a mouse periodontal regeneration model, oral administration of α-KG enhanced alveolar bone regeneration and reduced H3K27me3 signals and collagen-rich tissue organization within the periodontal ligament space. These findings identify α-KG as a metabolite-driven epigenetic modulator that alleviates H3K27me3-mediated repression and supports periodontal regeneration. - Source: PubMed
Publication date: 2026/02/24
Hasegawa RyuSuzuki ShigekiFahreza Rahmad RifqiTsai Shin-HoDaidouji YoshinoOmori MasatoKajikawa TetsuhiroYamada Satoru