GJA3 antibody
- Known as:
- GJA3 (anti-)
- Catalog number:
- orb107162
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Biorbyt biorb
- Gene target:
- GJA3 antibody
Related genes to: GJA3 antibody
- Gene:
- GJA3 NIH gene
- Name:
- gap junction protein alpha 3
- Previous symbol:
- CZP3
- Synonyms:
- CX46
- Chromosome:
- 13q12.11
- Locus Type:
- gene with protein product
- Date approved:
- 1990-02-12
- Date modifiied:
- 2015-11-09
Related products to: GJA3 antibody
Related articles to: GJA3 antibody
- Posterior polar cataract (PPC), a rare congenital cataract, is characterized by subcapsular opacities in the lens affecting vision and posing surgical challenges. Genetic heterogeneity exists, though several genes are implicated in its pathogenesis. This study reports on the genetic profile of late-onset PPC cases and identifies variations specific to posterior capsular rupture (PCR) during surgery. - Source: PubMed
Publication date: 2026/02/11
Sharma AnshulSharma NamrataAgarwal TusharSharma ArundhatiVajpayee Rasik B - Congenital cataract (CC), defined as lens opacity present at birth or in early infancy, is a major cause of reversible childhood blindness and shows marked genetic heterogeneity. This study aimed to investigate the genetic basis of CC in a multigenerational Chinese family. - Source: PubMed
Publication date: 2026/01/13
Zhou ChenchenLi KunkeZhou ZhenxingJian ShuhuiJin LingWang ChenghuZhang Xiaoqian - Gap junctions, formed by connexin proteins, establish direct electrical and metabolic coupling between cells, enabling coordinated tissue responses. These channels universally respond to intracellular pH changes, closing under acidic conditions to limit the spread of cytotoxic signals during cellular stress, such as ischemia. Using cryo-electron microscopy (cryo-EM), we uncover insights into the structural mechanism of pH-gating in native lens connexin-46/50 (Cx46/50) gap junctions. Mild acidification drives lipid infiltration into the channel pore, displacing the N-terminal (NT) domain and stabilizing pore closure. Lipid involvement is shown to be both essential and fully reversible. Structural transitions involve an ensemble of gated states formed through non-cooperative NT domain movement as well as minor populations of a distinct destabilized open-state. These findings provide molecular insights into pH-gating dynamics, illustrating how structural changes may regulate gap junction function under cellular stress and linking Cx46/50 dysregulation to age-related cataract formation. - Source: PubMed
Publication date: 2026/01/12
Jarodsky Joshua MMyers Janette BReichow Steve L - Drought and water scarcity, exacerbated by global warming, are enormous threats to global food sustainability and security. Poultry, in particular, are highly impacted by adverse environmental stressors. As nutrient absorption and intestinal integrity are critical for growth and performance, understanding the impact on the broiler gastrointestinal tract is highly relevant. Here, we examined the effect of chronic cyclic heat stress (HS) on the jejunal expression profile of tight-junction, gap-junction, adherens, and desmosome genes in the 4th generation of broiler lines divergently selected for low (LWE)- and high-water efficiency (HWE). Male HWE and LWE broilers (n = 240/line) were allotted to 12 environmental chambers (2 floor pens/chamber, 6 chambers/line, 20 birds/pen) and were exposed to cyclic HS (36°C for 9h/day from 9:00 am to 6:00 pm) or thermoneutral conditions (25°C) from day 29 to 49 of age in a 2 × 2 factorial design. Growth performance and mortality were recorded. At day 49, jejunal tissues were collected for molecular analyses using real-time quantitative PCR and immunoblot. Jejunal gene expression of multiple gut integrity factors were higher (P < 0.05) in the HWE as compared to the LWE lines, including claudin 22 (CLDN22), -34, occluding (OCDN), zona-occludin-2 (ZO-2), gap junction alpha1 (GJA1), GJA3, GJC1, and cadherin 1 (CDH1). CLDN8, -20, -25, -4, GJC2, and GJD2 were also greater (P < 0.05) in HWE, but were additionally downregulated (P < 0.05) during HS. Conversely PALS1-associated tight junction protein (PATJ) and desmocollin 1 (DSC1) mRNAs were significantly downregulated in the HWE as compared to the LWE broilers. Significant interactions between the line and environment were seen in CLDN1, where the expression was decreased in the LWE but increased in the HWE in HS. Additionally, CLDN15 and -16 genes were greatest in the HWE under TN conditions, while catenin alpha 2 (CTNNA2) was highest in the HWE during HS. Overall, the jejunal expression profile of key genes associated with intestinal barrier integrity likely contributes to the water efficiency phenotype and the response of these birds to HS. - Source: PubMed
Publication date: 2025/12/16
Greene Elizabeth SOrlowski SaraDridi Sami - Gap junction GJB2 (connexin 26, Cx26) gene mutations are responsible for >50 % of nonsyndromic hearing loss. The pathological changes mainly locate in the cochlea. However, little is known about genetic changes in the cochlea after Cx26 deficiency. In this study, we employed bulk Poly(A) RNA-Seq technique and found that Cx26 deficiency could cause many genes up- and down-regulated in the cochlea. One of the unexpected findings is significant upregulation of a gap junctional gene GJA3 (Cx46), which normally expresses in the eye rather than the ear. Quantitative PCR and digital droplet PCR further confirmed the promotion of Cx46 expression in the cochlea after Cx26 deficiency. Immunofluorescent staining showed that the promoted Cx46 was expressed at the same location as Cx26 expression in the cochlea and integrated into the same gap junctional plaques. This promotion is Cx26-specific; there was no promotion of Cx46 expression in the cochlea after knockout (KO) of Cx30 (GJB6), which is another predominant connexin co-expressed in the cochlea. Gene Set Enrichment Analysis (GSEA) revealed that Cx26 deficiency but not Cx30 KO upregulated a phototransduction pathway to promote the eye-specific gene Cx46 expression in the cochlea. This may present a natural compensation to the loss of Cx26 function, since both Cx26 and Cx46 have similar channel properties. Our findings also provide a new cue for developing a genetic approach to treat this common hereditary deafness. - Source: PubMed
Publication date: 2025/10/16
Zhai Tian-YingChen JinKong YongLiang ChunZhao Hong-Bo