Micromod

micromod Partikeltechnologie GmbH is a German biotechnology company specializing in the development and production of monodisperse micro- and nanoparticles and their coatings. With over 30 years of experience, micromod serves as a reliable supplier of system components for in-vitro diagnostics, high-throughput screening, magnetic bioseparation, cell labeling, and research and development of novel diagnostic and therapeutic methods.

Key Products:

Magnetic Particles: Utilized in applications such as Magnetic Particle Imaging (MPI), Magnetic Resonance Therapy (MRT), hyperthermia, biosensors, lab-on-chip designs, cell separation, and cell tracking. Available in sizes ranging from 30 nm to 100 nm with various coatings like COOH, dextran, and starch.
Fluorescent Particles: Designed for applications requiring fluorescence detection, these particles come in various sizes and fluorescence properties.
Fluorescent Magnetic Particles: Combining magnetic and fluorescent properties, these particles are suitable for applications requiring both magnetic manipulation and fluorescence detection.
White Particles: Available in sizes from 10 nm to 100 µm, these particles are made from materials like silica (sicastar®) and polystyrene/polymethacrylate (micromer®), suitable for various applications.

Services Offered:

Custom Particles: micromod manufactures particles tailored to specific requirements, including custom coatings and functionalizations.
Custom Production: The company offers production services for particles in bulk quantities, catering to diverse application needs.
Particle Processing & Treatment: Services include surface modifications, functionalization, and other treatments to enhance particle performance.
Particle Analysis: micromod provides comprehensive analysis services to characterize particle size, distribution, surface properties, and more.
Coupling Service for Molecules: The company offers services to couple various molecules to particles, facilitating applications like immunoassays and targeted delivery.

Browse Micromod Products

BNF-Dextran COOH

SKU: 84-02-102|Size: 5 mL

BNF-Dextran NH2

SKU: 84-01-102|Size: 5 mL

BNF-Dextran PEG-COOH

SKU: 84-56-102|Size: 5 mL

BNF-Dextran PEG-NH2

SKU: 84-55-801|Size: 5 mL

BNF-Dextran plain

SKU: 84-00-801|Size: 10 mL

BNF-Dextran protein A

SKU: 84-20-102|Size: 1 mL

BNF-Dextran streptavidin

SKU: 84-19-102|Size: 1 mL

BNF-Dextran-far redF NH2

SKU: 194-01-102|Size: 5 mL

BNF-Dextran-far redF plain

SKU: 194-00-102|Size: 5 mL

BNF-Dextran-far redF streptavidin

SKU: 194-19-102|Size: 1 mL

BNF-Dextran-redF NH2

SKU: 94-01-102|Size: 5 mL

BNF-Dextran-redF plain

SKU: 94-00-102|Size: 5 mL

BNF-Dextran-redF streptavidin

SKU: 94-19-102|Size: 1 mL

BNF-Starch COOH

SKU: 10-02-102|Size: 5 mL

BNF-Starch NH2

SKU: 10-01-102|Size: 5 mL

BNF-Starch PEG-COOH

SKU: 10-56-801|Size: 5 mL

BNF-Starch PEG-NH2

SKU: 10-55-102|Size: 5 mL

BNF-Starch plain

SKU: 10-00-102|Size: 10 mL

BNF-Starch protein A

SKU: 10-20-102|Size: 1 mL

BNF-Starch streptavidin

SKU: 10-19-102|Size: 1 mL

BNF-Starch-far redF NH2

SKU: 164-01-102|Size: 5 mL

BNF-Starch-far redF plain

SKU: 164-00-102|Size: 5 mL

BNF-Starch-far redF streptavidin

SKU: 164-19-102|Size: 1 mL

BNF-Starch-redF NH2

SKU: 64-01-102|Size: 5 mL

BNF-Starch-redF plain

SKU: 64-00-102|Size: 5 mL

BNF-Starch-redF streptavidin

SKU: 64-19-102|Size: 1 mL

Iron oxide particles Au-labeled

SKU: 45-42-252|Size: 10 mL

Iron oxide particles plain

SKU: 45-00-252|Size: 10 mL

Iron oxide particlesCOOH

SKU: 45-02-501|Size: 50nm

Iron oxide particlesphospholipid

SKU: 45-111-701|Size: 70nm

Micromer® C18

SKU: 01-51-703|Size: 0.5 mL

Micromer® COOH

SKU: 01-02-154|Size: 10 mL

Micromer® DBCO

SKU: 01-115-204|Size: 5 mL

Micromer® NH2

SKU: 01-01-304|Size: 10 mL

Micromer® NR3+

SKU: 01-05-703|Size: 10 mL

Micromer® NTA

SKU: 01-11-303|Size: 10 mL

Micromer® Ni-NTA

SKU: 01-48-303|Size: 10 mL

Micromer® PEG 300

SKU: 01-54-803|Size: 10 mL

Micromer® avidin

SKU: 01-18-803|Size: 2 mL

Micromer® collagen

SKU: 01-25-603|Size: 5 mL

Micromer® plain

SKU: 01-00-503|Size: 10 mL

Micromer® protein A

SKU: 01-20-104|Size: 1 mL

Micromer® streptavidin

SKU: 01-19-803|Size: 1 mL

Micromer®-M COOH

SKU: 08-02-403|Size: 10 mL

Micromer®-M NH2

SKU: 08-01-403|Size: 10 mL

Micromer®-M PEG-COOH

SKU: 08-56-603|Size: 10 mL

Micromer®-M PEG-NH2

SKU: 08-55-603|Size: 10 mL

Micromer®-M avidin

SKU: 08-18-503|Size: 2 mL

Micromer®-M protein A

SKU: 08-20-703|Size: 1 mL

Micromer®-M streptavidin

SKU: 08-19-104|Size: 1 mL

Micromer®-greenF COOH

SKU: 29-02-251|Size: 5 mL

Micromer®-greenF NH2

SKU: 29-01-251|Size: 5 mL

Micromer®-greenF plain

SKU: 29-00-252|Size: 10 mL

Micromer®-redF COOH

SKU: 30-02-303|Size: 10 mL

Micromer®-redF NH2

SKU: 30-01-252|Size: 5 mL

Micromer®-redF plain

SKU: 30-00-251|Size: 10 mL

Micromer®-redF streptavidin

SKU: 30-19-303|Size: 1 mL

Nanomag®-CLD COOH

SKU: 05-02-302|Size: 10 mL

Nanomag®-CLD NH2

SKU: 05-01-302|Size: 10 mL

Nanomag®-CLD PEG-COOH

SKU: 05-56-502|Size: 10 mL

Nanomag®-CLD streptavidin

SKU: 05-19-502|Size: 1 mL

Nanomag®-CLD-redF plain

SKU: 23-00-502|Size: 5 mL

Nanomag®-D COOH

SKU: 09-02-252|Size: 10 mL

Nanomag®-D NH2

SKU: 09-01-502|Size: 10 mL

Nanomag®-D NTA

SKU: 09-11-502|Size: 10 mL

Nanomag®-D Ni-NTA

SKU: 09-48-252|Size: 10 mL

Nanomag®-D PEG 2000

SKU: 09-82-182|Size: 10 mL

Nanomag®-D PEG 300

SKU: 09-54-132|Size: 10 mL

Nanomag®-D PEG-COOH

SKU: 09-56-132|Size: 10 mL

Nanomag®-D PEG-NH2

SKU: 09-55-252|Size: 10 mL

Nanomag®-D avidin

SKU: 09-18-132|Size: 2 mL

Nanomag®-D biotin

SKU: 09-26-502|Size: 2 mL

Nanomag®-D plain

SKU: 09-00-132|Size: 10 mL

Nanomag®-D protein A

SKU: 09-20-502|Size: 1 mL

Nanomag®-D streptavidin

SKU: 09-19-502|Size: 1 mL

Nanomag®-silica COOH

SKU: 13-02-252|Size: 10 mL

Nanomag®-silica NH2

SKU: 13-01-252|Size: 10 mL

Nanomag®-silica plain

SKU: 13-00-252|Size: 10 mL

PLA particles COOH

SKU: 11-02-105|Size: 10 mL

PLA particles plain

SKU: 11-00-502|Size: 10 mL

PLA-M COOH

SKU: 12-02-504|Size: 10 mL

PLA-M plain

SKU: 12-00-304|Size: 10 mL

PLA-greenF COOH

SKU: 51-02-105|Size: 5 mL

PLA-greenF plain

SKU: 51-00-502|Size: 5 mL

PLA-redF COOH

SKU: 52-02-304|Size: 5 mL

PLA-redF plain

SKU: 52-00-252|Size: 5 mL

Perimag® COOH

SKU: 102-02-132|Size: 10 mL

Perimag® NH2

SKU: 102-01-132|Size: 5 mL

Perimag® plain

SKU: 102-00-132|Size: 10 mL

Sicastar® C18

SKU: 43-51-302|Size: 0.5 mL

Sicastar® COOH

SKU: 43-02-303|Size: 10 mL

Sicastar® NH2

SKU: 43-01-502|Size: 10 mL

Sicastar® NTA

SKU: 43-11-502|Size: 10 mL

Sicastar® Ni-NTA

SKU: 43-48-302|Size: 10 mL

Sicastar® plain

SKU: 43-00-402|Size: 10 mL

Sicastar® protein A

SKU: 43-20-153|Size: 1 mL

Sicastar® streptavidin

SKU: 43-19-153|Size: 1 mL

Sicastar®-M C18

SKU: 39-51-153|Size: 0.5 mL

Sicastar®-M COOH

SKU: 39-02-153|Size: 10 mL

Sicastar®-M NH2

SKU: 39-01-153|Size: 10 mL

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.