Aurion

Aurion Biotech is a clinical-stage biotechnology company committed to developing innovative regenerative therapies aimed at restoring vision for patients suffering from ocular diseases. Headquartered in Seattle, Washington, with additional operations in Boston and Tokyo, the company's mission is to address significant unmet needs in ophthalmology through advanced cell therapy solutions.

Key Product – AURN001: Aurion Biotech's lead product candidate, AURN001, is an allogeneic cell therapy designed to treat corneal edema secondary to corneal endothelial disease. This condition can lead to significant vision impairment and currently lacks sufficient treatment options. AURN001 utilizes healthy donor corneal endothelial cells, expanded through a proprietary process, allowing a single donor to treat multiple patients—a significant advancement given the global shortage of donor corneas.

Browse Aurion Products

AURION BSA-c™ (10%)

SKU: 900.022|Size: 100 mL

AURION Enhancement Conditioning Solution (10x)

SKU: 500.055|Size: 100 mL

AURION R-Gent SE-EM

SKU: 500.044|Size: 90 mL

AURION R-Gent SE-Intense

SKU: 500.077|Size: 500 mL

AURION R-Gent SE-LM, replaced see 500.066

SKU: 500.011|Size: 60 mL

AURION R-Gent SE-LM, replaced see 500.077

SKU: 500.022|Size: 500 mL

AURION Ready-to-Use Incubation buffer (BSA-c and Tween)

SKU: 900.099-PBST|Size: 1000 mL

AURION Ready-to-Use Incubation buffer (BSA-c)

SKU: 900.099-PBS|Size: 1000 mL

AURION Ultra Small

SKU: 300.011|Size: 20 mL

Anionic tracer Conventional 10-nm gold

SKU: 210.022|Size: 10 mL

Anionic tracer Conventional 15-nm gold

SKU: 215.022|Size: 10 mL

Anionic tracer Conventional 25-nm gold

SKU: 225.022|Size: 10 mL

Anionic tracer Conventional 6-nm gold

SKU: 206.022|Size: 10 mL

Anionic tracer Ultra Small gold

SKU: 200.022|Size: 10 mL

BSA tracer Conventional 10-nm gold

SKU: 210.033|Size: 10 mL

BSA tracer Conventional 15-nm gold

SKU: 215.033|Size: 10 mL

BSA tracer Conventional 25-nm gold

SKU: 225.033|Size: 10 mL

BSA tracer Conventional 6-nm gold

SKU: 206.033|Size: 10 mL

BSA tracer Ultra Small gold

SKU: 200.133|Size: 5 mL

BSA, Fraction V

SKU: 900.011|Size: 25 mL

Basic Blocking solution (for e.g. protein A and G)

SKU: 905.001|Size: 30 mL

Biotinylated albumin 10nm gold

SKU: 810.122|Size: 1 mL

Biotinylated albumin Ultra Small gold

SKU: 100.122|Size: 1.5 mL

Blocking solution for donkey gold conjugates

SKU: 905.005|Size: 30 mL

Blocking solution for goat gold conjugates

SKU: 905.002|Size: 30 mL

Blocking solution for rabbit gold conjugates

SKU: 905.003|Size: 30 mL

Blocking solution for sheep gold conjugates - DISCONTINUED

SKU: 905.004|Size: 30 mL

CFWS Gelatin

SKU: 900.033-100|Size: 100 mL

COL-AURION protein stain

SKU: 600.011|Size: 500 mL

Conventional Kit Donkey-anti-Goat IgG (H&L) 10 nm gold

SKU: 710.333|Size: 1 Kit

Conventional Kit Donkey-anti-Goat IgG (H&L) 15 nm gold

SKU: 715.333|Size: 1 Kit

Conventional Kit Donkey-anti-Goat IgG (H&L) 25 nm gold

SKU: 725.333|Size: 1 Kit

Conventional Kit Donkey-anti-Goat IgG (H&L) 6 nm gold

SKU: 706.333|Size: 1 Kit

Conventional Kit Donkey-anti-Mouse IgG (H&L) 10 nm gold

SKU: 710.322|Size: 1 Kit

Conventional Kit Donkey-anti-Mouse IgG (H&L) 15 nm gold

SKU: 715.322|Size: 1 Kit

Conventional Kit Donkey-anti-Mouse IgG (H&L) 25 nm gold

SKU: 725.322|Size: 1 Kit

Conventional Kit Donkey-anti-Mouse IgG (H&L) 6 nm gold

SKU: 706.322|Size: 1 Kit

Conventional Kit Donkey-anti-Rabbit IgG (H&L) 10 nm gold

SKU: 710.311|Size: 1 Kit

Conventional Kit Donkey-anti-Rabbit IgG (H&L) 15 nm gold

SKU: 715.311|Size: 1 Kit

Conventional Kit Donkey-anti-Rabbit IgG (H&L) 25 nm gold

SKU: 725.311|Size: 1 Kit

Conventional Kit Donkey-anti-Rabbit IgG (H&L) 6 nm gold

SKU: 706.311|Size: 1 Kit

Conventional Kit Donkey-anti-Sheep IgG (H&L) 10 nm gold

SKU: 710.344|Size: 1 Kit

Conventional Kit Donkey-anti-Sheep IgG (H&L) 15 nm gold

SKU: 715.344|Size: 1 Kit

Conventional Kit Donkey-anti-Sheep IgG (H&L) 25 nm gold

SKU: 725.344|Size: 1 Kit

Conventional Kit Donkey-anti-Sheep IgG (H&L) 6 nm gold

SKU: 706.344|Size: 1 Kit

Conventional Kit F (ab') 2 Goat-anti-Mouse IgG + IgM 10 nm gold

SKU: 710.188|Size: 1 Kit

Conventional Kit F (ab') 2 Goat-anti-Mouse IgG + IgM 15 nm gold

SKU: 715.188|Size: 1 Kit

Conventional Kit F (ab') 2 Goat-anti-Mouse IgG + IgM 25 nm gold

SKU: 725.188|Size: 1 Kit

Conventional Kit F (ab') 2 Goat-anti-Mouse IgG + IgM 6 nm gold

SKU: 706.188|Size: 1 Kit

Conventional Kit F (ab') 2 fragment of Goat-anti-Mouse IgG (H&L) 10 nm gold

SKU: 710.177|Size: 1 Kit

Conventional Kit F (ab') 2 fragment of Goat-anti-Mouse IgG (H&L) 15 nm gold

SKU: 715.177|Size: 1 Kit

Conventional Kit F (ab') 2 fragment of Goat-anti-Mouse IgG (H&L) 25 nm gold

SKU: 725.177|Size: 1 Kit

Conventional Kit F (ab') 2 fragment of Goat-anti-Mouse IgG (H&L) 6 nm gold

SKU: 706.177|Size: 1 Kit

Conventional Kit F (ab') 2 fragment of Goat-anti-Rabbit IgG (H&L) 10 nm gold

SKU: 710.166|Size: 1 Kit

Conventional Kit F (ab') 2 fragment of Goat-anti-Rabbit IgG (H&L) 15 nm gold

SKU: 715.166|Size: 1 Kit

Conventional Kit F (ab') 2 fragment of Goat-anti-Rabbit IgG (H&L) 25 nm gold

SKU: 725.166|Size: 1 Kit

Conventional Kit F (ab') 2 fragment of Goat-anti-Rabbit IgG (H&L) 6 nm gold

SKU: 706.166|Size: 1 Kit

Conventional Kit F (ab') fragment of Sheep-anti-Digoxigenin 10 nm gold

SKU: 710.211|Size: 1 Kit

Conventional Kit Goat-anti-Biotin 10 nm gold

SKU: 710.088|Size: 1 Kit

Conventional Kit Goat-anti-Biotin 15 nm gold

SKU: 715.088|Size: 1 Kit

Conventional Kit Goat-anti-Biotin 25 nm gold

SKU: 725.088|Size: 1 Kit

Conventional Kit Goat-anti-Biotin 6 nm gold

SKU: 706.088|Size: 1 Kit

Conventional Kit Goat-anti-Chicken IgG (H&L) 10 nm gold

SKU: 710.244|Size: 1 Kit

Conventional Kit Goat-anti-Chicken IgG (H&L) 15 nm gold

SKU: 715.244|Size: 1 Kit

Conventional Kit Goat-anti-Chicken IgG (H&L) 25 nm gold

SKU: 725.244|Size: 1 Kit

Conventional Kit Goat-anti-Chicken IgG (H&L) 6 nm gold

SKU: 706.244|Size: 1 Kit

Conventional Kit Goat-anti-Guinea Pig IgG (H&L) 10 nm gold

SKU: 710.144|Size: 1 Kit

Conventional Kit Goat-anti-Guinea Pig IgG (H&L) 15 nm gold

SKU: 715.144|Size: 1 Kit

Conventional Kit Goat-anti-Guinea Pig IgG (H&L) 25 nm gold

SKU: 725.144|Size: 1 Kit

Conventional Kit Goat-anti-Guinea Pig IgG (H&L) 6 nm gold

SKU: 706.144|Size: 1 Kit

Conventional Kit Goat-anti-Human IgG (H&L) 10 nm gold

SKU: 710.066|Size: 1 Kit

Conventional Kit Goat-anti-Human IgG (H&L) 15 nm gold

SKU: 715.066|Size: 1 Kit

Conventional Kit Goat-anti-Human IgG (H&L) 25 nm gold

SKU: 725.066|Size: 1 Kit

Conventional Kit Goat-anti-Human IgG (H&L) 6 nm gold

SKU: 706.066|Size: 1 Kit

Conventional Kit Goat-anti-Mouse IgG (H&L) 10 nm gold

SKU: 710.022|Size: 1 Kit

Conventional Kit Goat-anti-Mouse IgG (H&L) 15 nm gold

SKU: 715.022|Size: 1 Kit

Conventional Kit Goat-anti-Mouse IgG (H&L) 25 nm gold

SKU: 725.022|Size: 1 Kit

Conventional Kit Goat-anti-Mouse IgG (H&L) 6 nm gold

SKU: 706.022|Size: 1 Kit

Conventional Kit Goat-anti-Mouse IgG (H+L) xRat 10nm

SKU: 710.422|Size: 1 Kit

Conventional Kit Goat-anti-Mouse IgG + IgM 10 nm gold

SKU: 710.044|Size: 1 Kit

Conventional Kit Goat-anti-Mouse IgG + IgM 15 nm gold

SKU: 715.044|Size: 1 Kit

Conventional Kit Goat-anti-Mouse IgG + IgM 25 nm gold

SKU: 725.044|Size: 1 Kit

Conventional Kit Goat-anti-Mouse IgG + IgM 6 nm gold

SKU: 706.044|Size: 1 Kit

Conventional Kit Goat-anti-Mouse IgM (µ-chain) 10 nm gold

SKU: 710.033|Size: 1 Kit

Conventional Kit Goat-anti-Mouse IgM (µ-chain) 15 nm gold

SKU: 715.033|Size: 1 Kit

Conventional Kit Goat-anti-Mouse IgM (µ-chain) 25 nm gold

SKU: 725.033|Size: 1 Kit

Conventional Kit Goat-anti-Mouse IgM (µ-chain) 6 nm gold

SKU: 706.033|Size: 1 Kit

Conventional Kit Goat-anti-Rabbit IgG (H&L) 10 nm gold

SKU: 710.011|Size: 1 Kit

Conventional Kit Goat-anti-Rabbit IgG (H&L) 15 nm gold

SKU: 715.011|Size: 1 Kit

Conventional Kit Goat-anti-Rabbit IgG (H&L) 25 nm gold

SKU: 725.011|Size: 1 Kit

Conventional Kit Goat-anti-Rabbit IgG (H&L) 6 nm gold

SKU: 706.011|Size: 1 Kit

Conventional Kit Goat-anti-Rat IgG (H&L) 10 nm gold

SKU: 710.055|Size: 1 Kit

Conventional Kit Goat-anti-Rat IgG (H&L) 15 nm gold

SKU: 715.055|Size: 1 Kit

Conventional Kit Goat-anti-Rat IgG (H&L) 25 nm gold

SKU: 725.055|Size: 1 Kit

Conventional Kit Goat-anti-Rat IgG (H&L) 6 nm gold

SKU: 706.055|Size: 1 Kit

Conventional Kit Goat-anti-Rat IgG (H+L) xMouse 10nm

SKU: 710.455|Size: 1 Kit

Conventional Kit Mouse-anti-FITC 10 nm gold

SKU: 710.233|Size: 1 Kit

Conventional Kit Protein A 10 nm gold

SKU: 710.111|Size: 1 Kit

Conventional Kit Protein A 15 nm gold

SKU: 715.111|Size: 1 Kit

Conventional Kit Protein A 25 nm gold

SKU: 725.111|Size: 1 Kit

Recent Breakthroughs

Design, synthesis, and antidiabetic activity of new furan-clubbed 1,2,3-triazole derivatives as <i>α</i>-glucosidase inhibitors.

Devi P, Maity S, Singh A, Mehan S, Singh G, Asati V.

Future Med Chem

PMID:41994872

Free PMC article

Aim The study aims to design, synthesize, and evaluate novel furan-clubbed 1,2,3-triazole derivatives as potential α-glucosidase inhibitors for the management of diabetes mellitus. Materials and methods Ten furan-clubbed-1,2,3-triazole derivatives PD(1-10) were synthesized and characterized through sophisticated instrumentation techniques, including FT-IR, 1 H NMR, 13 C NMR, and LC-MS. The compounds were assessed in vitro for their ability to inhibit the α-glucosidase enzyme. The in vivo antidiabetic effect of the best molecules was evaluated using STZ-nicotinamide induced diabetic mouse model. The observed results were further supported by molecular docking against α-glucosidase (PDB ID: 3L4U) and histopathological examinations. Results The results of in vitro studies showed that the test compound PD-10 exhibited the strongest α-glucosidase inhibition (IC 5 0 = 13.82 μM), outperforming acarbose (IC 5 0 = 32.03 μM), followed by PD-1 and PD-6 . Further, the in vivo antidiabetic evaluation of the best compounds adjudged compound PD-10 as the best molecule among the series. Docking analyses indicated a significant binding affinity of PD-10 (-4.34 kcal/mol). Conclusions The research highlights PD-10 as a promising α-glucosidase inhibitor with strong in vitro and in vivo antidiabetic effects, supported by favorable molecular docking interactions, and emphasizes its potential for development as an antidiabetic lead for further studies and evaluations.

Mechanistic perspectives on antimalarial agents: from FDA-approved drugs to next-generation candidates.

Monika, Sharma B, Awasthi SK.

RSC Adv

PMID:42006802

Free PMC article

Malaria is a major global health challenge, demanding continued innovation in drug discovery and development. This review gives a comprehensive overview of FDA-approved antimalarial drugs and emerging clinical candidates, focusing their chemical structures, mechanisms of action, and molecular targets such as PfATP4, DHFR, DHODH, and PfCRT. The discussion showcases structure-activity relationships, mechanisms underlying drug resistance, and recent advances in structure-guided design of next-generation antimalarials. The review also summarizes the year of approval, mechanistic class, and synthetic origin of key therapeutic agents. Moreover, novel molecules currently in preclinical and clinical trials are discussed in the context of their mode of action, efficacy, and potential for overcoming resistance. Collectively, this article bridges medicinal chemistry insights with biological mechanisms, outlining future directions in the rational design of potent, resistance-resilient antimalarial drugs.

Total chemical synthesis of pentameric cholera toxin subunit B.

Spaltenstein P, Scherer SR, Jones TE, Giesler RJ, Kay MS.

Chem Commun (Camb)

PMID:41891529

Free PMC article

Vibrio cholerae annually infects millions worldwide, causing intense and life-threatening diarrheal disease. The pentameric cholera toxin subunit B (CtxB) binds to the ganglioside GM1 on epithelial cells, initiating endocytosis and downstream toxicity. We present the total chemical protein synthesis of L-CtxB and mirror-image D-CtxB using a three-segment N-to-C native chemical ligation approach. Oxidative folding produced the desired 62 kDa pentameric proteins, with L-CtxB capable of binding native GM1 ligand. Synthetic D-CtxB is now ready to serve as a target in mirror-image phage display, representing a significant milestone for the discovery of toxin-neutralizing D-peptides to treat and prevent cholera.

Can amoxicillin be detected in the aquatic environment? A critical assessment.

Hernández F, Botero-Coy AM, Bijlsma L, Fabregat-Safont D.

Environ Int

PMID:42001666

Free PMC article

Amoxicillin is a broad-spectrum β-lactam antibiotic widely used in both human and veterinary medicine. Following administration, approximately 60-80% of the dose is excreted, largely unmetabolized, via urine within a few hours. Consequently, environmental contamination with amoxicillin, especially in aquatic systems, is a significant concern. Due to its potential ecological risks and the current scarcity of data required for a full assessment, it was included in two consecutive European Union Watch Lists (2018, 2020) of substances for comprehensive monitoring to inform water policy. However, data on amoxicillin levels in aquatic environments are contradictory, ranging from high concentrations in some studies to non-detection in others. The presence of intact amoxicillin in aquatic environments is inherently transient, and the risk of substantial analytical errors in its detection, identification, and quantification is considerable unless stringent methodological precautions are applied. Driven by the need for reliable environmental data, inconsistencies in the existing literature and our own extensive analytical experience, we comprehensively investigated amoxicillin degradation in surface water, influent and effluent wastewater under various conditions. Experiments were conducted under both dark and sunlight conditions using water samples spiked with amoxicillin at 5 μg/L and 50 μg/L. The parent compound was quantified by liquid chromatography-tandem mass spectrometry, whereas transformation products were identified by high-resolution mass spectrometry. By critically assessing the factors that influence the analysis and environmental occurrence of amoxicillin, this study resolves discrepancies in prior reports and clarifies the realistic prospects for its detection. We demonstrate that the parent antibiotic should be rarely found in water samples due to its rapid degradation. Therefore, future monitoring efforts should be focused on its primary degradation product, amoxicillin penicilloic acid, as more reliable indicator of contamination in aquatic environments.

Characterising the urinary metabolome in HIV/TB coinfection and the impact of antiretroviral treatment.

Allen B, Wood R, Luies L.

BMC Infect Dis

PMID:41992151

Free PMC article

Background HIV/TB coinfection poses significant challenges due to complex interactions between both pathogens and the metabolic disruptions they induce. Although antiretroviral treatment (ART) has transformed disease management, its impact on metabolism is not fully understood. Metabolomics offers an in-depth approach to explore the metabolic changes in this coinfected population, providing information into disease mechanisms and the effects of ART. Methods This exploratory study used untargeted urine gas chromatography mass spectrometry metabolomics to profile metabolic alterations in treatment-naïve HIV/TB coinfected patients and those on ART. Healthy controls were included for comparison. Metabolite changes were analysed using univariate statistical methods, including Kruskal-Wallis tests and pairwise comparisons, to identify key metabolites associated with coinfection and ART. Results Findings revealed significant disruptions in several metabolic pathways. Mitochondrial dysfunction was evident, contributing to altered lipid metabolism, impaired energy production, and increased cardiovascular risk. Disruptions in glucose metabolism, including compromised insulin secretion, were observed, alongside evidence of gut dysbiosis linked to inflammation and microbial imbalance. These metabolic disturbances were also associated with increased oxidative stress, reflected in changes to protein metabolism and the development of cachexia. Although ART partially alleviated some metabolic alterations, disruptions remained evident in treated patients. Conclusion This study provides a comprehensive view of the metabolic disturbances in HIV/TB coinfection and the impact of ART. Our findings suggest that persistent mitochondrial dysfunction, altered lipid metabolism, and gut dysbiosis contribute to ongoing metabolic imbalances, underscoring the need for targeted therapeutic strategies to address these challenges.