CRYBB2 Antibody
- Known as:
- CRYBB2 Antibody
- Catalog number:
- abx000083
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Abbexa
- Gene target:
- CRYBB2 Antibody
Related genes to: CRYBB2 Antibody
- Gene:
- CRYBB2 NIH gene
- Name:
- crystallin beta B2
- Previous symbol:
- CCA2, CRYB2A, CRYB2
- Synonyms:
- -
- Chromosome:
- 22q11.23
- Locus Type:
- gene with protein product
- Date approved:
- 1991-06-28
- Date modifiied:
- 2015-11-12
Related products to: CRYBB2 Antibody
Related articles to: CRYBB2 Antibody
- We identify the genetic cause of autosomal dominant congenital cataract in a large family and define how a CRYBB2 splice-site variant perturbs lens development and associated ocular phenotypes. - Source: PubMed
Wei XingWang JingWang YanyunZhou CongChen ZhaoyiLiu ShanlingSun HuaqinZhou BinZhang Lin - Congenital cataract is a major cause of blindness and severe visual impairment in children. It may occur as an isolated ocular abnormality or in combination with microcornea, microphthalmia, aniridia, or glaucoma. It can also be part of syndromic conditions. Whole-exome sequencing (WES) is now recognized as an appropriate first-line approach for genetic testing in patients with congenital cataract. In this study, we use WES to characterize the genotype spectrum in a pediatric cataract cohort from southern China. - Source: PubMed
Publication date: 2026/02/26
Huang TengSun Hai-SenLiu Ya-NanXie Qiu-LingLiu YangMiao Xue-ChuanWu WenhuiLi Jin - Imidacloprid (IMI) poses risks to aquatic ecosystems and exhibits visual toxicity to nontarget organisms. However, the underlying mechanism of its visual toxicity has not been fully elucidated. After exposure to IMI at the concentrations 10, 100, and 1000 µg/L for 4 or 21 days, the visual behavior of zebrafish larvae was first suppressed, followed by enhanced locomotor and visual activities as exposure prolonged. The eye development in zebrafish larvae was significantly disrupted. Structurally, the lens area of zebrafish larvae was reduced from 15.63 % to 50.21 % (4 days) and from 37.00 % to 47.22 % (21 days), and the retina exhibited a thickening of the OPL and IPL, along with thinning of the RPE. Genes related to lens structure (e.g., CRYBA4 and CRYBB2) were significantly down-regulated at 4 days (100 and 1000 µg/L) and then up-regulated (10 and 100 µg/L) at 21 days at the mRNA and protein levels (P < 0.05). Furthermore, IMI exposure disrupted the phototransduction and retinol metabolism cascade in zebrafish larvae, which involves the generation of visual signals across three critical stages, namely, light input, photopigment activation, and photoelectric conversion. Generally, the key genes and metabolites associated with these processes (e.g., Rhodopsin, OPN1SW1, GNGT1, REP65A, 11-cis-retinal) were significantly decreased in zebrafish exposed to IMI for 4 days and increased in those exposed for 21 days (P < 0.05). Therefore, the abnormal color perception was observed in exposed zebrafish larvae. This study elucidates the mechanism underlying IMI-induced visual toxicity in zebrafish and provides crucial theoretical insights for assessing the visual toxicity of agrochemicals. - Source: PubMed
Publication date: 2025/12/02
Fu RuiqiangZheng HanfeiGao HanMao LiangangWu ChiZhu LizhenLiu XingangZhang Lan - Resolving spatial protein dynamics in native human epithelial tissues presents a significant technical challenge, particularly in inherently curved or unevenly mounted specimens. Here, we introduce an image processing pipeline for high-resolution, compartment-based analysis of protein localization, using the native three-dimensional architecture of the human anterior lens epithelium and capsule complex as a robust ex vivo proof-of-principle platform for precise cell segmentation and quantitative analysis. This platform integrates whole-mount immunostaining, 3D confocal imaging, computational tissue flattening, digital segmentation, and spatial regression to quantitatively map subcellular protein distributions at the tissue scale. To demonstrate the utility of this approach, we examined the spatial distribution of αB-crystallin (CRYAB), a stress-associated small heat shock protein, and βB2-crystallin (CRYBB2), a predominantly structural lens protein, in specimens obtained during cataract surgery. We observed a marked accumulation of CRYAB in epithelial cells at the capsule edge following both laser and manual capsulorhexis, indicating a localized stress response to surgical intervention. In contrast, CRYBB2 distribution remained unaffected. Furthermore, both proteins exhibited consistent cytoplasmic localization, while only CRYBB2 occasionally showed exclusive nuclear accumulation. This pipeline offers a scalable framework for quantitatively resolving protein localization in native epithelial architectures, using CRYAB and CRYBB2 as examples of how stress-associated changes can be spatially mapped in situ within the human lens. - Source: PubMed
Publication date: 2025/10/03
Cristoforetti AlessandroBaldessari GiorgioChychko LizavetaChust Ignacio BabiloniSartori SamueleSchickhardt SonjaRavelli FlaviaBertoluzza SilviaCarl MatthiasSel SaadettinAuffarth Gerd UPoggi Lucia - To identify novel candidates for cataract and evaluate the contribution of protein-coding variants to cataract susceptibility. - Source: PubMed
Chaar Dima LJiang ChenCoomson Sarah YDuot MatthieuSangani PoorabHoffmann Thomas JJorgenson EricHufnagel Robert BHysi PirroLachke Salil AChoquet Hélène