ALG2 antibody Ab host: Rabbit
- Known as:
- ALG2 (anti-) Antibody production species: Rabbit
- Catalog number:
- 'AP43589PU-N
- Product Quantity:
- 0.1 mg
- Category:
- -
- Supplier:
- ACR
- Gene target:
- ALG2 antibody host: Rabbit
Related genes to: ALG2 antibody Ab host: Rabbit
- Gene:
- ALG2 NIH gene
- Name:
- ALG2 alpha-1,3/1,6-mannosyltransferase
- Previous symbol:
- -
- Synonyms:
- CDGIi, FLJ14511, hALPG2, NET38, CDG1I
- Chromosome:
- 9q22.33
- Locus Type:
- gene with protein product
- Date approved:
- 2003-10-15
- Date modifiied:
- 2019-01-18
- Gene:
- PPP1R18 NIH gene
- Name:
- protein phosphatase 1 regulatory subunit 18
- Previous symbol:
- KIAA1949
- Synonyms:
- phostensin
- Chromosome:
- 6p21.33
- Locus Type:
- gene with protein product
- Date approved:
- 2004-03-02
- Date modifiied:
- 2016-10-05
Related products to: ALG2 antibody Ab host: Rabbit
Related articles to: ALG2 antibody Ab host: Rabbit
- The fungal plasma membrane is the target of fungicidal compounds, such as polyenes and saponins, that directly interact with fungus-specific ergosterol to cause deleterious membrane disruption. To counter membrane attack, diverse eukaryotic cells employ Ca2+-binding penta-EF (PEF)-hand proteins, including the human ortholog, ALG-2, to maintain membrane integrity. Candida albicans is a major fungal pathogen in humans, where increasing resistance to current antifungal drugs that target the plasma membrane is of serious concern. Combinatorial treatments that additionally compromise the plasma membrane offer a way forward, but our mechanistic understanding of how fungi respond to direct membrane disruption remains limited. Here, we investigated the PEF-hand ortholog, Pef1, in this polymorphic species. GFP-tagged Pef1 localized at sites of polarized growth in yeast and hyphal cells of C. albicans. On treatment of hyphae with the polyene drug, amphotericin B, or the saponin tomatine, GFP-Pef1 became distributed as punctate spots at the membrane. In a similar manner, loss of calcineurin A (Cna1), but not of its transcription factor, Crz1, caused this punctate localization pattern of GFP-Pef1. While deletion of PEF1 slightly impaired yeast cell growth rate, filamentation was not affected. Strikingly, pef1Δ hyphae could not maintain plasma membrane integrity in serum, as also seen in the cna1Δ mutant, and exhibited attenuated virulence in an insect larvae infection model. Together, these observations suggest that Pef1 localizes to sites of membrane perturbation in order to maintain cell integrity, including sites of dynamic polarized growth, septum formation, and fungicide-induced membrane disruption. - Source: PubMed
Publication date: 2026/04/01
Weichert MartinSchumann Marcel RenéBrandt UlrikeBedford CameronBrand Alexandra CFleißner André - Endoplasmic reticulum (ER) exit sites (ERES) serve as essential hubs for the packaging and export of secretory proteins into the COPII vesicular pathway. Previous studies have shown that ERES are dynamic and capable of adapting to stress, but the molecular details controlling their degradation under nutrient-stress conditions were largely unknown. A recent study by Liao et al. introduces a new mechanism in which ERES are degraded through lysosome-dependent microautophagy in response to nutrient stress. This process is uniquely facilitated by COPII components, the calcium-binding adaptor ALG2, and the ESCRT machinery. The authors demonstrate that inhibiting MTOR triggers calcium release from lysosomes, which then recruits ALG2, leading to SEC31 ubiquitination and subsequently promoting PDCD6IP/ALIX-ESCRT-dependent lysosomal engulfment of ERES. This research reveals an unexplored pathway for the quality control and recycling of secretory machinery, thereby improving our understanding of ER turnover and establishing a mechanistic link between nutrient sensing, autophagy, and remodeling of the secretory pathway. - Source: PubMed
Publication date: 2026/02/23
Bhattacharyya DibyenduKlionsky Daniel J - Congenital disorders of glycosylation (CDG) are a complex and heterogeneous family of rare metabolic diseases that affect protein and lipid glycosylation and glycosylphosphatidylinositol synthesis. These disorders can affect multiple organs, leading to a broad spectrum of symptoms that vary among different CDG subtypes and between individuals with same type of CDG. This study aimed to investigate the genetic variants, molecular etiologies, and clinical features of 20 Chinese patients diagnosed with CDG. - Source: PubMed
Publication date: 2025/12/23
Zhao PeiweiTan LiMeng QingjieZhang LeiHuang YufengZhang XiankaiHu YanqiuZhou ShiqiongHe Xuelian - Glycosylation defects are a recognized cause of congenital myasthenic syndrome (CMS), affecting the stability and functions of the neuromuscular junction proteins. Mutations in five genes (GFPT1, DPAGT1, GMPPB, ALG2, and ALG14) are currently associated with glycosylation-related CMS. This cohort describes Iranian patients with CMS and variants in these genes. - Source: PubMed
Publication date: 2025/11/28
Ramezani MahtabOkhovat Ali AsgharNilipour YaldaGhasemi AidaAshtiani Bahram HaghiSarraf PayamKariminejad ArianaNafissi Shahriar - Congenital Disorders of Glycosylation (CDG) are severe disruptions in the synthesis of glycoconjugates, resulting in inherited metabolic conditions. These multisystem diseases, typically inherited in an autosomal recessive manner, have an occurrence rate of approximately 1 in 20,000 to 1 in 50,000 live births. The clinical presentation of CDG is highly varied and complex, with neurological symptoms being predominant, affecting multiple organ systems. The process of glycosylation, a critical post-translational modification, is tightly controlled by proteins encoded by over 250 genes, and mutations in any of these genes are known to cause CDG. The discovery of new associated genes over recent years has accelerated; comprehensively characterizing these, especially rare ones, will aid in identifying novel therapeutic targets, improving prognostic evaluations, and developing effective treatments. In vitro models (such as cell lines or patient-derived "clinical-grade" cells) are essential for advancing CDG research. Notably, 60% of defects affecting N- or O-glycosylation impact the eyes, leading to photoreceptor degeneration and cell death. The 661W cell line, derived from immortalized mouse retinal cells and expressing specific ocular markers, serves as a valuable experimental model to study the ocular involvement in CDG. - Source: PubMed
Publication date: 2025/10/21
Cubilla Marisa AngelicaSclausero Ana ClaraBisbal MarianoAsteggiano Carla Gabriela