Native proteins are a cornerstone of scientific research, providing essential resources for exploring biological processes and advancing various applications. Our comprehensive catalog of native proteins ensures a wide selection to address diverse experimental demands. These proteins, validated across numerous techniques such as functional studies, ELISA, western blot, and flow cytometry, empower scientists to delve deep into cellular functions, protein interactions, and molecular mechanisms with precision.
We offer various forms of native proteins, including biologically active and inactive variants. This range ensures that researchers can select the optimal protein for their specific applications, whether studying enzymatic activity or simply requiring structural control. Unlike recombinant proteins, the native proteins in our catalog are entirely free from tags or artificial modifications and are derived from endogenous sources. This preserves their natural form, making them highly reliable for applications where native protein behavior is critical.
Native proteins from our catalog of different peptides and proteins play a pivotal role in key areas such as functional studies, enabling researchers to investigate cellular functions, signaling pathways, and protein-protein interactions. In addition, native proteins are suitable for a broad spectrum of other research needs. They serve as valuable tools in structural biology, drug development, and biomarker discovery, offering unparalleled insights into biological systems. Their unaltered nature makes them an ideal choice for studying protein folding, conformational changes, and other intricate biochemical phenomena.
Leveraging the native state of proteins offers researchers the benefit of enhanced reliability and flexibility, ensuring robust and reproducible results in their experiments. The availability of proteins from multiple species further expands the scope of research possibilities, enabling comparative studies and cross-species analyses. Our range of native protein molecules stands as a valuable resource for driving innovation in modern bioscience.
FEATURES
- Wide species selection: Native proteins are derived from over 10 species, including humans, mice, and rats, offering a diverse range of options to meet various research requirements.
- Extensive validation: These proteins are validated for use in multiple applications, such as functional studies, ELISA, western blot, and flow cytometry, ensuring reliability and accuracy.
- Biological versatility: Both biologically active and non-active native proteins are available, providing flexibility for studying different biological processes and experimental needs.
- Endogenous nature: Native proteins are completely free from tags or artificial modifications, preserving their natural state and integrity for authentic research outcomes.
APPLICATIONS
- Functional studies: Assist in investigating cellular mechanisms, signaling pathways, and protein interactions.
- ELISA: Native proteins are employed as controls or standards for reliable assay results.
- Western blot: These facilitate accurate detection and analysis of target proteins.
- Flow Cytometry: Help analyze cell populations and protein expression with precision.
- Additional applications: Can be utilized in structural biology research, pre-clinical drug discovery, and other advanced research fields.
FAQs
What are native proteins?
Native proteins are naturally occurring proteins extracted from various species, including humans, mice, and rats. These proteins play a crucial role in scientific research by offering an authentic model to study biological processes in their natural state. Their unmodified nature ensures an accurate representation of protein behavior in experiments.
How are native proteins utilized in research?
Native proteins are indispensable in functional studies, ELISA, western blot, and flow cytometry, where they help investigate cellular functions, interactions, and signaling pathways. These proteins serve as reliable standards or controls, enabling precise detection and analysis in a wide range of experimental techniques. Their versatility makes them valuable across multiple research domains.
Are all native proteins biologically active?
Not all native proteins are biologically active. Some are chosen for their structural properties rather than activity. This diversity ensures researchers have access to proteins tailored to their specific needs, whether studying enzymatic activity or utilizing non-active proteins as benchmarks in experimental setups.
Do native proteins come with tags or modifications?
Native proteins in our catalog are free from tags or artificial modifications, preserving their original and natural state. This ensures compatibility for studies requiring unaltered proteins and allows for authentic exploration of biochemical processes.
How do native protein workflows differ from recombinant protein workflows?
Native protein workflows differ significantly from recombinant protein workflows due to the source, preparation, and applications of the proteins.
Native proteins are directly isolated from natural sources, such as tissues, cells, or organisms, and they retain their natural form and modifications. The workflow for native proteins typically involves extraction, purification, and validation steps to ensure that the proteins remain unaltered. These workflows prioritize maintaining biological authenticity, making native proteins ideal for studying processes in their natural state.
Recombinant protein workflows, on the other hand, rely on the expression of proteins in host systems like E. coli, yeast, or mammalian cells through genetic engineering. The workflow involves gene cloning, vector construction, expression optimization, and purification, often with added tags for easier handling. Recombinant proteins are customizable, allowing researchers to modify them for specific experiments or applications, such as adding tags to enhance purification or detection.
How can native proteins be stabilized for long-term storage and research?
Native proteins can be stabilized for long-term storage by using protective agents like glycerol or ethylene glycol to prevent aggregation and degradation. Freezing proteins at ultra-low temperatures, such as -20°C or -80°C, or lyophilizing them helps maintain their structural integrity. Buffering solutions with optimal pH and excipients like surfactants further ensures that proteins remain stable and functional over extended periods.