Description

Product Description

Elranatamab is a high-purity bispecific monoclonal antibody designed exclusively for in vitro mechanistic research. Its unique bispecificity enables simultaneous binding to two molecular targets, providing researchers with a precise experimental tool to study receptor-ligand interactions, protein-protein interactions, and intracellular signaling pathways in controlled laboratory settings. By using Elranatamab, scientists can dissect complex molecular mechanisms with high specificity and reproducibility, making it an invaluable reagent for molecular biology, biochemistry, and cellular signaling research.

This lyophilized antibody maintains excellent structural integrity and binding functionality after reconstitution, ensuring that experimental observations are consistent and reliable. Researchers can leverage Elranatamab to investigate mechanistic aspects of target engagement, receptor clustering, and downstream molecular events in cell-free systems or controlled in vitro models. Its high purity (≥98%) minimizes the risk of interference from impurities, supporting accurate mechanistic conclusions and high-confidence data interpretation.

Elranatamab is particularly suitable for studies of dual target engagement dynamics, allowing researchers to explore how simultaneous binding influences signaling cascade initiation, molecular complex formation, and pathway modulation. The bispecific nature of Elranatamab offers a versatile platform for evaluating target interactions, molecular synergy, and mechanistic perturbations under defined experimental conditions.

In addition to mechanistic studies, Elranatamab is compatible with multi-omic approaches, including proteomics and computational modeling. Experimental data generated using Elranatamab can be integrated with in silico simulations to predict binding kinetics, molecular interactions, and pathway outcomes. This capability makes it a valuable reagent for laboratories combining experimental and computational mechanistic research.

Elranatamab is supplied by factory-direct manufacturing, ensuring consistent quality, traceability, and availability for both small-scale and high-throughput mechanistic assays. Certificates of Analysis (COA) are provided for each batch to document purity, identity, and functional verification, supporting reproducible experimental workflows.

Designed exclusively for research use in molecular mechanism studies, Elranatamab is not intended for human, animal, or clinical applications. Its lyophilized form allows long-term storage, and careful handling ensures sustained activity for repeated experiments. Researchers can use Elranatamab to explore a broad spectrum of mechanistic questions, including target specificity, signaling cross-talk, and protein complex formation, providing critical insights into fundamental molecular biology processes.

By incorporating Elranatamab into in vitro experimental systems, laboratories gain a reliable, high-purity, and versatile tool for advancing understanding of molecular interactions and signaling mechanisms. Its combination of high structural integrity, dual target specificity, and compatibility with advanced analytical techniques makes Elranatamab a cornerstone reagent for mechanistic research in molecular biology and biochemistry laboratories worldwide.

Product Specifications

Mechanism of Action

Elranatamab is a bispecific monoclonal antibody that can simultaneously bind two distinct molecular targets, providing a controlled experimental tool for dissecting molecular interactions in vitro. In laboratory research, this dual-target engagement enables precise analysis of receptor-ligand interactions, protein clustering, and initiation of downstream molecular signaling under defined conditions.

The bispecific nature of Elranatamab allows for receptor cross-linking and spatial coordination, which can be monitored in cell-free systems, recombinant protein assays, or in vitro signaling models. By engaging two targets concurrently, researchers can study how molecular proximity affects signal transduction, complex formation, and mechanistic outcomes. This capability is particularly useful for probing the dynamics of protein-protein interactions and elucidating pathway-specific mechanistic relationships.

In controlled experiments, Elranatamab provides a quantifiable platform for evaluating the influence of dual target binding on downstream molecular events. Researchers can measure biochemical readouts, structural changes, or interaction kinetics in response to bispecific engagement, supporting mechanistic interpretation and validation of theoretical models. Its predictable and reproducible binding properties facilitate comparative studies across multiple experimental conditions.

Furthermore, Elranatamab is compatible with computational and multi-omic integration, enabling modeling of molecular interactions and pathway simulations. Experimental binding data can be used to refine in silico predictions of target clustering, interaction dynamics, and mechanistic signaling networks. This combined approach enhances mechanistic insight and supports robust hypothesis generation for laboratory studies.

Overall, Elranatamab functions as a versatile mechanistic probe for in vitro research, offering dual-target engagement, reproducible binding, and compatibility with advanced analytical techniques. It provides researchers with a powerful tool to study molecular recognition, complex formation, and signaling pathways in controlled experimental systems.

Structure :

Applications

Elranatamab is applied as a research-grade bispecific antibody for a wide range of in vitro mechanistic studies. Its dual-target binding properties enable detailed investigation of receptor-ligand interactions, protein-protein interactions, and downstream molecular signaling pathways under controlled experimental conditions. Researchers can use Elranatamab to probe the dynamic effects of dual target engagement on molecular complex formation and pathway modulation.

One primary application is in cell-free protein interaction studies, where Elranatamab facilitates mechanistic exploration of bispecific engagement and structural coordination between molecular targets. These experiments allow precise measurement of binding affinity, complex stoichiometry, and the impact of simultaneous target interactions on molecular signaling outcomes.

Elranatamab is also utilized in in vitro signaling assays, providing a controlled platform for examining how dual receptor engagement influences signal transduction, molecular activation, and mechanistic pathway integration. Such studies are critical for dissecting the relationship between target proximity, clustering, and downstream signaling events at the molecular level.

Additionally, Elranatamab supports biochemical assay development, including enzyme-linked detection methods and binding kinetics experiments. Its high purity and reproducible binding ensure consistent experimental results when studying protein network dynamics and molecular cross-talk. Researchers can integrate these findings into mechanistic models to better understand complex molecular systems.

Elranatamab can further be incorporated into multi-omic and computational research frameworks. Experimental data from in vitro bispecific engagement studies can be combined with proteomic, transcriptomic, and molecular modeling analyses to elucidate the effects of target co-binding on cellular pathways and mechanistic networks. This integrative approach enhances experimental design, supports hypothesis testing, and expands the scope of mechanistic research.

Overall, Elranatamab provides a versatile, reproducible, and high-purity platform for laboratories conducting in vitro mechanistic studies. Its applications span protein-protein interaction analysis, signaling pathway investigation, complex formation studies, and integrated multi-omic research, making it an essential tool for molecular biology and biochemical research.

Research Models

Elranatamab can be employed in a variety of in vitro research models designed to investigate dual-target engagement, protein-protein interactions, and downstream signaling mechanisms. These models enable precise mechanistic studies in controlled laboratory environments, allowing reproducible evaluation of molecular interactions.

One commonly used model is the cell-free protein interaction system, in which purified recombinant proteins are exposed to Elranatamab. This setup allows detailed analysis of bispecific binding, complex formation, and mechanistic cooperativity between two molecular targets. Researchers can quantify binding kinetics, affinity, and stoichiometry without interference from cellular components.

Another valuable model involves reconstituted in vitro signaling systems, where Elranatamab is applied to synthetic molecular assemblies or isolated receptor complexes. These systems enable the study of mechanistic outcomes of receptor cross-linking, pathway activation, and downstream molecular responses, providing insights into the dynamics of dual-target engagement.

Elranatamab is also integrated into biochemical assay models, such as enzyme-linked detection methods, fluorescence-based interaction assays, and surface plasmon resonance studies. These approaches allow researchers to probe binding specificity, temporal signaling responses, and structural-functional relationships under highly controlled conditions.

In addition, Elranatamab can be combined with computational and multi-omic modeling. Data obtained from in vitro binding and signaling experiments can be used to simulate molecular dynamics, interaction networks, and mechanistic pathway behavior, enabling predictive analysis and hypothesis testing. Integration of experimental and computational models supports robust mechanistic interpretation and reproducibility.

Overall, Elranatamab-based research models provide flexible, scalable, and reproducible platforms for laboratories investigating molecular mechanisms. They are suitable for protein-protein interaction studies, bispecific engagement analysis, signaling pathway mapping, and multi-omic integration, making Elranatamab a versatile tool for mechanistic research in vitro.

Experimental Design Considerations

When using Elranatamab in in vitro mechanistic studies, careful experimental design is essential to ensure reproducibility, accuracy, and interpretability. Its bispecific nature requires attention to concentration control, timing, and assay selection to accurately capture dual-target engagement and downstream molecular responses.

Stock solutions should be prepared in PBS or other compatible neutral buffers immediately prior to experiments to maintain antibody stability and binding activity. Lyophilized powder should be carefully weighed using calibrated instruments to minimize variability. Working concentrations must be optimized through preliminary titration to achieve specific dual-target binding without nonspecific interactions.

Temporal parameters are critical for mechanistic studies. Researchers should define precise exposure durations and sampling intervals, particularly when monitoring complex formation, signaling activation, or protein-protein interaction kinetics. Time-course experiments can elucidate dynamic molecular behaviors and provide insights into mechanistic causality.

Control experiments are highly recommended. Single-target controls, isotype controls, and vehicle-only controls help distinguish bispecific binding effects from background signals. Inclusion of these controls supports accurate data interpretation and ensures that observed effects are attributable to Elranatamab-mediated engagement.

Assay selection should match the mechanistic question. Cell-free protein interaction systems, reconstituted signaling complexes, and biochemical detection assays provide different levels of mechanistic insight. Combining multiple models can enhance reliability, validate findings across platforms, and support robust hypothesis testing.

Finally, detailed record-keeping is crucial. Documenting batch numbers, preparation dates, storage conditions, and experimental parameters ensures traceability and reproducibility. Proper planning of experimental variables maximizes the value of data generated using Elranatamab in dual-target mechanistic research.

Laboratory Safety & Handling Guidelines

Elranatamab should be handled exclusively within controlled laboratory environments by trained personnel familiar with antibody handling and chemical safety protocols. As a research-grade bispecific monoclonal antibody, proper handling ensures experimental integrity, reproducibility, and safety during in vitro mechanistic studies.

All manipulations should be conducted in a ventilated laboratory setting, such as a certified chemical fume hood or biosafety cabinet, to prevent contamination and minimize exposure to aerosols or dust. Standard laboratory personal protective equipment (PPE), including gloves, lab coat, and safety glasses, should be worn at all times during weighing, reconstitution, and experimental use.

Lyophilized Elranatamab should be reconstituted in compatible buffers immediately prior to use. Avoid exposure to extreme temperatures, direct sunlight, or prolonged moisture, as these factors may compromise structural integrity and binding activity. Only use clean, dry instruments to prevent contamination or degradation during solution preparation.

Proper storage is essential to maintain antibody stability. Elranatamab should be kept at –20°C in a dry, light-protected environment. Avoid repeated freeze-thaw cycles to preserve functional activity. Containers should be tightly sealed when not in use to maintain quality over time.

Waste handling should comply with institutional chemical safety and biosafety policies. Any unused material, contaminated consumables, or residual solutions must be collected in designated waste containers. Label all containers clearly to prevent accidental exposure or misuse. Maintaining comprehensive documentation of batch numbers, preparation dates, and storage conditions is strongly recommended to support traceability and reproducibility.

By following these laboratory safety and handling guidelines, researchers can ensure reliable performance of Elranatamab in in vitro mechanistic studies, minimize the risk of experimental variability, and uphold laboratory safety standards.

Integration with Multi-Omic & Computational Studies

Elranatamab can be effectively incorporated into multi-omic and computational research frameworks to provide a comprehensive understanding of dual-target engagement and downstream molecular mechanisms. Its predictable bispecific binding enables precise perturbation in controlled in vitro systems, which is essential for integrating experimental results across multiple analytical platforms.

In proteomics studies, Elranatamab allows researchers to observe changes in protein interaction networks, complex formation, and signaling pathway dynamics. By introducing a defined bispecific interaction, researchers can quantify protein abundance shifts, post-translational modifications, and molecular interactions under controlled conditions.

For transcriptomic analysis, data from Elranatamab-treated in vitro systems can be used to map gene expression changes associated with dual target engagement. These datasets help elucidate the mechanistic impact of receptor cross-linking and binding dynamics on molecular signaling and regulatory networks.

Elranatamab is also compatible with epigenomic and structural analyses, enabling study of protein-DNA or protein-protein complex organization in response to bispecific binding. Controlled laboratory models allow researchers to evaluate how dual engagement affects macromolecular assembly and mechanistic pathways.

From a computational perspective, experimental data generated using Elranatamab can be integrated into molecular modeling, reaction kinetics simulations, and network analysis. Simulations can predict binding site occupancy, interaction dynamics, and mechanistic outcomes, which can then be validated experimentally. Combining multi-omic datasets with computational models provides a holistic view of molecular mechanisms and enhances predictive understanding in mechanistic research.

Overall, Elranatamab serves as a versatile tool for integrative mechanistic studies, bridging experimental in vitro findings with computational and multi-omic analyses. This integration supports robust hypothesis generation, pathway mapping, and comprehensive investigation of molecular signaling networks under controlled laboratory conditions.

Things to Note

Elranatamab is intended exclusively for in vitro laboratory research and should only be used in controlled mechanistic studies. It is not suitable for clinical, human, or animal applications. Researchers should ensure that all experimental protocols clearly define its role as a bispecific reagent for mechanistic and molecular interaction studies.

Due to its highly specific binding and structural sensitivity, Elranatamab should be handled with care during reconstitution, solution preparation, and storage. Exposure to moisture, light, or repeated freeze-thaw cycles may reduce its functional activity and compromise experimental reproducibility. It is recommended to prepare working solutions immediately before use and minimize unnecessary handling.

Accurate concentration control is essential for reliable dual-target engagement. Variations in solution preparation, assay timing, or storage conditions can affect binding kinetics and mechanistic outcomes. Detailed documentation of batch number, preparation date, buffer composition, and experimental conditions is strongly advised to maintain traceability and reproducibility.

Elranatamab should not be mixed indiscriminately with reactive or incompatible reagents without prior compatibility testing. Such interactions may alter binding properties and confound mechanistic interpretations. Finally, laboratories should follow proper chemical waste disposal and decontamination procedures in accordance with institutional safety guidelines to ensure responsible and safe handling.

By observing these considerations, researchers can maximize the reliability and reproducibility of Elranatamab in in vitro mechanistic studies while maintaining laboratory safety standards.

Keywords

Elranatamab, bispecific antibody, laboratory reagent, high purity, in vitro research, molecular mechanism, dual target binding, Tumor (compound) Research, protein-protein interactions, factory direct supply, wholesale.

Shipping Guarantee

Elranatamab is packaged using laboratory-grade, tamper-evident materials to preserve compound integrity during transit. Temperature-controlled logistics maintain stability and functional activity. Global delivery with tracking ensures secure and reliable shipment to research laboratories worldwide.

Trade Assurance

Factory-direct supply guarantees consistent batch quality, analytical verification, and full traceability for every shipment. Bulk and wholesale procurement options support high-throughput mechanistic studies. Certificates of Analysis (COA) are provided to document purity, identity, and functional verification for reproducibility.

Payment Support

Flexible payment options include Credit Card (Visa, MasterCard, AMEX), Telegraphic Transfer (T/T), and Cryptocurrency (BTC, ETH, and supported digital assets). Secure, encrypted payment channels ensure smooth processing for international laboratory orders.

Disclaimer

Elranatamab is for laboratory research use only and is not intended for human, veterinary, or clinical applications. All experiments should be conducted under controlled in vitro conditions with proper laboratory safety protocols. Researchers are responsible for safe handling, storage, and disposal in accordance with institutional guidelines.

References

1. PubChem — Monoclonal Antibodies Overview

2. DrugBank — Bi-specific Antibodies

3. Selleck Chemicals — Antibody Reagents

4. MedChemExpress — Monoclonal Antibodies for Research

5. Wikipedia — Bispecific Antibodies