CX36 antibody - middle region (ARP36685_T100)
- Known as:
- CX36 (anti-) - middle region (ARP36685_T100)
- Catalog number:
- arp36685_t100
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- CX36 antibody - middle region (ARP36685_T100)
Related genes to: CX36 antibody - middle region (ARP36685_T100)
- Gene:
- GJD2 NIH gene
- Name:
- gap junction protein delta 2
- Previous symbol:
- GJA9
- Synonyms:
- CX36
- Chromosome:
- 15q14
- Locus Type:
- gene with protein product
- Date approved:
- 2007-01-16
- Date modifiied:
- 2016-10-05
Related products to: CX36 antibody - middle region (ARP36685_T100)
Related articles to: CX36 antibody - middle region (ARP36685_T100)
- In-feed beta-mannanase supplementation has been used for decades to improve gut health and growth performances in poultry, yet its underlying molecular mechanisms are not completely defined. The aim of the present study was to determine the effect and potential mode of action of a new endo-1,4-β-D-mannanase (Natupulse® TS, NPU) on gut integrity and growth performances of turkeys. A total of 640 one-day-old male Hybrid Converter poults were randomly assigned to two dietary treatments without (control, CON) or with Natupulse® TS (NPU, 800 TMU/kg feed) for a 49 day-trial, each treatment having 16 replicate pens of 20 birds each. Body weight (BW), BW gain (BWG), feed intake (FI), and feed conversion ratio (FCR) and intestinal permeability using fluorescein isothiocyanate-dextran (FITC-d) were measured on days 21 and 49. Jejunal samples (16 birds/treatment) were analyzed for markers of stress, inflammation, and gut barrier integrity using real-time quantitative PCR and immunoblot. Dietary NPU supplementation significantly reduced serum FITC-D levels in turkey at day 49 and increased BWG at both day 21 and day 49 compared to the CON group. Molecular analyses showed that dietary NPU supplementation significantly increased jejunal protein levels of HSP60/70/90 on day 21. On day 49, HSP60 remained unchanged, HSP70 was high and HSP90 protein levels were significantly decreased compared to the CON diet. In-feed NPU administration significantly downregulated the jejunal expression of IL8, IL18, Crp and Tnfsf4 genes on day 21, and only IL8 gene on day 49. In addition, NPU supplementation decreased jejunal protein levels of claudins (CLDN1/4/5) on day 21 and CLDN5 on day 49. The expression of genes coding for gap junction proteins was also affected by NPU supplementation, with a significant downregulation of Gja1, Gjb1, Gjc1, and Gjd2 on day 21, and Gjc1 and Gjd2 on day 49. Dietary supplantation of NPU significantly downregulated the jejunal expression of the adherens junction protein afadin (afdn1) gene on day 49 compared to the CON group. In summary, dietary NPU supplementation improved growth performance and jejunal barrier integrity potentially through modulation of the expression of HSPs, pro-inflammatory cytokines, tight junction, gap junction, and adherens junction proteins. - Source: PubMed
Publication date: 2026/05/07
Sokale Adebayo OAderibigbe Ayodeji SMoore Danvon Heimendahl ElkeStringfellow KendreDridi Sami - Electrical synapses containing Connexin 36 (Cx36) represent the main means for direct electrical communication among neurons in the mammalian nervous system. However, little is known about the protein complexes that constitute these synapses. In the present study, we applied different BioID strategies to screen the interactomes of Connexin 36 and its zebrafish orthologue Cx35.1 in retinal neurons. For in vivo proximity labeling in mice, we took advantage of the Cx36-EGFP strain and expressed a GFP-nanobody-TurboID fusion construct selectively in AII amacrine cells. For in vivo BioID in zebrafish, we generated a transgenic line expressing a Cx35.1-TurboID fusion under control of the promoter. Both strategies allowed us to capture a plethora of molecules that were associated with electrical synapses and showed a high degree of evolutionary conservation in the proteomes of both species. Besides known interactors of Cx36 such as ZO-1 and ZO-2, we have identified more than 50 new proteins, such as scaffold proteins, adhesion molecules, and regulators of the cytoskeleton. Moreover, we determined the subcellular localization of these proteins in mouse retina and tested potential binding interactions with Cx36. Among these new interactors, we identified signal-induced proliferation associated 1 like 3 (Sipa1l3), a protein that has been implicated in cell junction formation and cell polarity, as a new scaffold of electrical synapses. Interestingly, Sipa1l3 was able to interact with ZO-1, ZO-2, and Cx36, suggesting a pivotal role in electrical synapse function. In summary, our study provides the first detailed view of the electrical synapse proteome in retinal neurons, which is likely to apply to electrical synapses elsewhere. - Source: PubMed
Publication date: 2026/05/20
Tetenborg StephanShihabeddin EyadKumar Elizebeth Olive Akansha ManojSigulinsky Crystal LDedek KarinLin Ya-PingEcheverry Fabio AHoff HannahPereda Alberto EJones Bryan WRibelayga Christophe PEbnet KlausMatsuura KenO'Brien John - Refractive errors are the leading cause of visual impairment and blindness globally. High myopia (HM) poses significant risks of severe ocular complications and blindness. 12 SNPs, including rs580839, have been associated with refractive errors in European and Asian populations, but their roles in Chinese cohorts remain unexplored. Their genetic association with HM is investigated in this study. - Source: PubMed
Publication date: 2026/05/13
Liu JianxinLiao WeijiangXie ChunbaoWang XinyuGong YukaiYang ChunchunHao FangYang YinZou LiangShi YiMeng JiayuJiang Lingxi - Within the islets of Langerhans, gap junction coupling is important for synchronizing oscillatory free-calcium activity ([Ca2+]) and regulating pulsatile insulin release. In islets from multiple models of diabetes, gap junction coupling is disrupted, and [Ca2+] synchronization and pulsatile insulin is lost. Functional subpopulations have been identified within the islet that are linked to driving synchronized [Ca2+] and insulin release. These subpopulations can be disrupted under conditions associated with diabetes, such as glucolipotoxicity and inflammatory environments, and their loss may drive islet dysfunction. Here we investigated how loss of gap junction coupling influences functional subpopulations under diabetogenic environments. We treated islets with a cocktail of pro-inflammatory cytokines and protected gap junction coupling via co-treatment with a Cx36 peptide S293 that was previously shown to specifically prevent a decline in gap junction permeability and synchronized [Ca2+] dynamics. We performed calcium imaging and ChR2 stimulation and analyzed islet [Ca2+] dynamics and the presence of functional subpopulations, including hubs and first-responders. 1- or 24-h cytokine treatment disrupted gap junction coupling, which was fully prevented by S293 peptide co-treatment. Treatment with pro-inflammatory cytokines decreased the recruitment of [Ca2+] upon ChR2 stimulation, increased the time between first and last responding cells upon glucose stimulation, and reduced the number and consistency of hub cells. When preserving gap junction coupling by S293 during cytokine treatment, the presence and consistency of these subpopulations were only marginally improved. We therefore concluded that while gap junction coupling is important for functional subpopulations to exert their influence on islet function, the restoration of gap junctions alone is not sufficient to recover functional subpopulations under diabetogenic conditions. Thus, preventing a disruption to intrinsic β-cell properties that define functional subpopulations is likely important for preserving these subpopulations during diabetes. - Source: PubMed
Publication date: 2026/03/31
Levitt Claire HIsaacs DominicHansen Maria SKravets ViraBriggs Jennifer KBenninger Richard K P - Connexin36 (Cx36) is highly expressed in inhibitory and excitatory neurons as well as pancreatic β-cells, where it forms gap junction channels that coordinate metabolic and electrical responses. In addition, Cx36 forms hemichannels in pancreatic β-cells, where it may play a critical role in endocrine cell signaling. Despite this, the regulatory mechanisms and biophysical properties of Cx36 HCs remain poorly understood. Using HeLa cells lacking endogenous expression of large-pore channels and transfected with mouse Cx36-EGFP, we evaluated hemichannel activity through dye uptake assays and membrane current recordings. We found that Cx36 hemichannel activity is strongly inhibited by extracellular Mg, rather than Ca, in contrast to hemichannels formed by other connexins. Under reduced extracellular Mg, or under alkaline extracellular pH conditions, Cx36 hemichannels exhibited increased activity and allowed Ca influx, as detected by ratiometric dye FURA-2. Under low extracellular Mg conditions, Cx36 hemichannels exhibited increased permeability to small molecules and were blocked by La and quinine, but not by high glucose concentration. In-silico studies revealed interactions between Mg and two amino acid residues within a pore constriction (D47-E49), which alter the electrostatic potential of the hemichannel pore. Consistent with these observations, mutation of either amino acid residue to alanine (D47A or E49A) markedly reduced the inhibitory effect of extracellular Mg. Together, these findings offer critical insights into the regulation of Cx36 hemichannels and suggest that alterations in Mg homeostasis may have significant consequences for Cx36-mediated signaling. - Source: PubMed
Publication date: 2026/03/16
García AníbalMárquez-Miranda ValeriaBravo-Acuña NicolásAraya-Duran IngridRojas MaximilianoPalacios-Prado NicolásO'Brien JohnGonzález-Nilo Fernando DSáez Juan C