ALG2 (Human) Recombinant Protein (P01)
- Known as:
- ALG2 (Human) Recombinant Protein (P01)
- Catalog number:
- H00085365-P01-10
- Product Quantity:
- 10 ug
- Category:
- -
- Supplier:
- Abno
- Gene target:
- ALG2 (Human) Recombinant Protein (P01)
Related genes to: ALG2 (Human) Recombinant Protein (P01)
- 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:
- BZW2 NIH gene
- Name:
- basic leucine zipper and W2 domains 2
- Previous symbol:
- -
- Synonyms:
- HSPC028, MST017, MSTP017
- Chromosome:
- 7p21.1
- Locus Type:
- gene with protein product
- Date approved:
- 2002-08-05
- Date modifiied:
- 2016-10-05
- Gene:
- C2CD3 NIH gene
- Name:
- C2 calcium dependent domain containing 3
- Previous symbol:
- -
- Synonyms:
- DKFZP586P0123
- Chromosome:
- 11q13.4
- Locus Type:
- gene with protein product
- Date approved:
- 2007-10-17
- Date modifiied:
- 2016-06-08
- Gene:
- MBTD1 NIH gene
- Name:
- mbt domain containing 1
- Previous symbol:
- -
- Synonyms:
- SA49P01, FLJ20055
- Chromosome:
- 17q21.33
- Locus Type:
- gene with protein product
- Date approved:
- 2003-01-15
- Date modifiied:
- 2015-04-21
- Gene:
- TMEM63C NIH gene
- Name:
- transmembrane protein 63C
- Previous symbol:
- C14orf171
- Synonyms:
- DKFZp434P0111, CSC1, hsCSC1
- Chromosome:
- 14q24.3
- Locus Type:
- gene with protein product
- Date approved:
- 2003-12-10
- Date modifiied:
- 2017-10-17
Related products to: ALG2 (Human) Recombinant Protein (P01)
Related articles to: ALG2 (Human) Recombinant Protein (P01)
- Tumor cells are constantly confronted with nutrient deprivation; however, the effect of serum starvation on the remodeling of endosomal compartments and extracellular vesicles (EVs) in tumor cells remains unclear. Here, we found that serum starvation pronouncedly promotes multivesicular body (MVB) biogenesis, EV formation, and cargo selection. Specifically, by generating a constitutively active Rab5Q79L mutant to induce the enlargement of MVB, we revealed for the first time to our knowledge that ANXA3 is sorted into intraluminal vesicles (ILVs) of MVB. Mechanistically, we confirmed that serum starvation regulates the endosomal sorting complex required for transport-associated (ESCRT-associated) protein ALG-2 interacting protein X (ALIX), which recruits ESCRT-III to MVB and binds to annexin A3 (ANXA3) to mediate its sorting into ILVs of MVB. Our study highlights that serum starvation promotes an ALIX-dependent ESCRT-III recruitment pathway, which loads protumor ANXA3 cargo to exert a profound effect on tumor progression. - Source: PubMed
Publication date: 2026/06/08
Peng XueqiangLiu JiaxingZeng GuolongXiao YafeiHao ZhixiongHe GuangpengJin HongyuanGao YuTang ShileiWei ShiboLi YanYu YifanYang LiangLi Hangyu - (Turcz.) Baill. (Schisandraceae) is a medicinal plant widely distributed in East Asia and has long been used in traditional herbal medicine. Phytochemical studies have identified lignans as the major bioactive constituents of , among which Schisandrin B (Sch B) is one of the most abundant and pharmacologically active compounds. Previous studies have demonstrated that Sch B exhibits a variety of biological activities, including antioxidant, anti-inflammatory, hepatoprotective, and cytoprotective effects. As a natural lignan compound derived from , Sch B has attracted increasing attention for its potential protective effects against environmental and inflammatory insults. This study aimed to investigate the protective effects of Sch B against PM-induced inflammatory injury in THP-1 cells and to elucidate the underlying molecular mechanisms. An in vitro PM-induced THP-1 cell injury model was established by stimulating THP-1 cells with PM. Subsequently, Sch B was applied to the model, and inflammation-related indicators and pathways were detected using methods such as ELISA, PCR, and Western Blot (WB). The results showed that Sch B significantly inhibited interleukin-1β (IL-1β) secretion and attenuated PM-induced pyroptosis in THP-1 cells. Mechanistically, Sch B alleviated cell membrane damage and inflammatory factor release by suppressing Caspase-1 activation and inhibiting the cleavage of gasdermin D (GSDMD) into its active N-terminal fragment (N-GSDMD). Furthermore, Sch B treatment was associated with the up-regulation of ALG-2, ALIX, and TSG101, suggesting the potential involvement of ESCRT-III-associated membrane repair mechanisms. In conclusion, Sch B, a natural lignan compound derived from , exhibits protective effects against PM-induced THP-1 cell pyroptosis by reducing cell membrane damage and inflammatory cytokine release. These effects are associated with the inhibition of Caspase-1 activity and GSDMD cleavage, as well as the activation of ESCRT-III-associated membrane repair responses. Collectively, these findings highlight the potential of Sch B as a natural cytoprotective compound against particulate matter-induced inflammatory injury. - Source: PubMed
Publication date: 2026/05/09
Deng LeLiao Lian-YingLing XiaoLi LiHe You-JieGuo Miao-Miao - N-glycosylation in eukaryotes begins with the assembly of a lipid-linked oligosaccharide on the endoplasmic reticulum membrane. As a pivotal post-translational protein modification, it is conserved across all three domains of life. However, the evolutionary origins of the Nglycosylation pathway remain a subject of ongoing debate in evolutionary biology, largely due to the limited availability of robust data regarding the evolutionary trajectories of the glycosyltransferases involved in this process. Here, we present phylogenetic analyses of the eukaryotic ALG1 and ALG2 mannosyltransferases (MTases), which are crucial for constructing the core trimannosyl Man3GlcNAc2 structure conserved in eukaryotic N-glycans. Our comprehensive phylogenetic study, combined with functional and structural analyses, suggests that the ALG2 MTase likely originated from a bacterial ancestor. This inference is further supported by the identification of sequential and functional ALG1 homologs exclusively within bacterial lineages, rather than in Asgard archaea or other archaeal groups. Our findings challenge the prevailing hypothesis that the eukaryotic N-glycosylation pathway primarily evolved from archaeal ancestors, instead suggesting a chimeric origin involving contributions from both bacterial and archaeal lineages. - Source: PubMed
Xu SiChen ShuaiGu Yu-HeHuang Yi-FanNakanishi HidekiGao Xiao-Dong - 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 to maintain cell integrity, including sites of dynamic polarized growth, septum formation, and fungicide-induced membrane disruption. - Source: PubMed
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