Taiy Chemical
Dnp-RNATAV-NH2
Synonym Dynorphin-A (1-7), Human, Radetide, Dynorphin A (1-7), Dnp-Dynorphin-1-7
Species Human
Protein Accession P01201
Purity Greater than 98% as determined by HPLC and SDS-PAGE analysis
Endotoxin Level Less than 1 EU/μg
Biological Activity Not determined
Expression System E. coli
Fusion Tag None
Predicted Molecular Mass 870.99 Da
Formulation Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA
Reconstitution It is recommended to reconstitute the lyophilized Dnp-Dynorphin A in sterile 18MΩ-cm H2O not less than 100 μg/ml, which can then be further diluted to other aqueous solutions.
Storage & Stability Store lyophilized protein at -20°C to -80°C. Lyophilized protein is stable for up to 6 months from date of receipt at -20°C to -80°C. Upon reconstitution, this product can be stored in working aliquots at 2°C - 8°C for one month, or at -20°C to -80°C in a manual defrost freezer for six months without detectable loss of activity.
FAQ
What is Dnp-RNATAV-NH2, and how does it work?
Dnp-RNATAV-NH2 is a synthetic peptide designed for research purposes, particularly in the field of biochemistry and molecular biology. This particular compound is engineered to assist researchers in studying protein interactions, cellular signaling pathways, or enzyme activity due to its unique sequence and structure. Peptides like Dnp-RNATAV-NH2 are often utilized in research because they can mimic portions of proteins or interact uniquely with cellular components, providing insights into their biological functions. The "Dnp" prefix often signifies a functional group addition, which may influence the stability, solubility, or reactivity of the peptide. "NH2" at the end typically represents an amidated C-terminus, which can affect the peptide's stability and resistance to enzymatic degradation. Understanding how Dnp-RNATAV-NH2 works requires basic knowledge of peptide chemistry. Peptides are short chains of amino acids linked by peptide bonds. Their function is determined by the sequence of amino acids, which form the primary structure. In more advanced applications, the peptide's secondary and tertiary structures—how it folds and forms stable shapes—also contribute to its role in biological processes.

Researchers interested in protein-protein interactions might use Dnp-RNATAV-NH2 to probe how proteins communicate or bind in a cellular context. By observing the changes in cellular behavior or protein activity upon introducing the peptide, it becomes possible to infer the peptide's role or influence. Moreover, synthetic peptides are advantageous in research because they can be designed with high specificity, targeting a particular protein structure or function. This specificity makes them powerful tools for dissecting complex biological processes. Overall, Dnp-RNATAV-NH2 is a versatile research tool that can provide significant insights into diverse areas of biological research. By elucidating the roles and interactions of biological molecules, it helps in advancing our understanding of molecular biology's fundamental processes.

How does Dnp-RNATAV-NH2 compare to other peptides in its category?
Dnp-RNATAV-NH2 stands out in its category due to its tailored structural features and functional properties that enable specific applications in biochemical research. While many peptides are available for scientific study, each peptide's effectiveness is determined by its amino acid sequence, length, and attached functional groups, which dictate its binding affinity, stability, and target specificity. Comparing Dnp-RNATAV-NH2 to other peptides requires an understanding of these variables and how they align with the research objectives. One distinguishing factor of Dnp-RNATAV-NH2 is the presence of the Dnp group, which may affect the hydrophobicity or electronic properties of the peptide. This modification could impart unique characteristics that are not present in unmodified counterparts, potentially influencing how the peptide interacts with biological membranes or proteins. Such specificity can make Dnp-RNATAV-NH2 suitable for more precise biochemical assays or as a probe for investigating particular pathways.

When evaluating peptides for research, factors such as peptide stability, ease of synthesis, and solubility are essential. Dnp-RNATAV-NH2 may offer high stability due to its amidated NH2 C-terminus, reducing degradation by enzymes that often target peptide bonds at the ends of amino acid chains. Stability is particularly advantageous for studies involving prolonged incubation periods or in vivo applications, where peptides face challenges from cellular proteases. Moreover, when compared with other peptides, Dnp-RNATAV-NH2 might offer improved solubility, an essential property for achieving consistent results in aqueous environments typical of biological systems. Optimal solubility ensures the peptide remains in a form that is biologically relevant and readily available to interact with its intended targets.

Ultimately, the choice between Dnp-RNATAV-NH2 and other peptides depends on the specifics of the research application. Researchers should consider the peptide's biological target, desired duration of action, and any specific structural considerations crucial to their study. Dnp-RNATAV-NH2's unique chemical properties allow it to be a compelling option for many research scenarios, providing a platform for innovative discovery in the life sciences.

What are the potential applications of Dnp-RNATAV-NH2 in scientific research?
Dnp-RNATAV-NH2 exhibits potential utility across a broad spectrum of scientific research areas, primarily due to its unique chemical structure and customizable nature. As a synthetic peptide, it is especially useful in molecular biology, cell biology, and biochemistry to investigate protein-protein interactions, signaling pathways, and enzyme activity. One potential application of Dnp-RNATAV-NH2 is in elucidating protein interaction networks. Proteins often operate within complex networks, and understanding these interactions is crucial for deciphering cellular functions. Dnp-RNATAV-NH2, equipped with its specific sequence and modifications such as Dnp and amidated NH2, can be used as a probe to map interaction sites on proteins, helping researchers identify critical interfaces for binding and signal transduction. Such studies can unravel the mysteries of cell communication and open the door to developing targeted therapeutics.

Moreover, Dnp-RNATAV-NH2 is valuable in studying protein modifications and their effect on activity. Post-translational modifications often alter protein functions and interactions, and by providing a model system mimicking such modifications or binding partners, Dnp-RNATAV-NH2 can help explore these processes in detail. It can be used in assays designed to test enzyme activities, substrate specificity, or inhibition, leading to insights into metabolic pathways and potential drug targets. Furthermore, this peptide could be instrumental in structural biology research, serving as a ligand or structural complement to target proteins. Through approaches like X-ray crystallography or nuclear magnetic resonance (NMR), Dnp-RNATAV-NH2 can assist in determining the three-dimensional structures of macromolecular complexes. Understanding these structures is vital for designing small molecules or biologics that can modulate biochemical pathways in disease contexts.

In summary, the applications of Dnp-RNATAV-NH2 in scientific research are diverse and significant. Its engineered properties allow for a wide range of experimental investigations into the fundamental processes of life, offering insights that can be translated into new therapeutic strategies and biotechnological advancements. As research tools continue to evolve, the strategic application of synthetic peptides like Dnp-RNATAV-NH2 remains essential for advancing our understanding of biological systems.

How can Dnp-RNATAV-NH2 aid in the study of cellular signaling pathways?
Dnp-RNATAV-NH2 can significantly aid in studying cellular signaling pathways by serving as a tool to dissect the intricate networks of communication that occur within and between cells. These pathways involve a cascade of signaling events, often initiated by external stimuli leading to specific cellular responses. Understanding these pathways is crucial for uncovering how cells make decisions, maintain homeostasis, and respond to environmental changes. The structured nature of peptides like Dnp-RNATAV-NH2 makes them well-suited for interacting with specific proteins involved in signaling pathways. These interactions can either mimic, inhibit, or otherwise modify the pathway's natural course, allowing researchers to observe changes in signaling dynamics and infer the role of particular components within the network.

One approach is using Dnp-RNATAV-NH2 as a competitive inhibitor or a molecular mimic of endogenous signaling molecules. By binding to key proteins or receptors within the pathway, it can block or alter normal signaling events, aiding in identifying crucial points of control and the effects of their modulation. This can provide valuable information on targets for drug development, especially in diseases where signaling pathways are dysregulated, such as cancer or autoimmune disorders. Moreover, Dnp-RNATAV-NH2 could be employed in various assay formats to monitor real-time signaling changes, leveraging techniques like fluorescence resonance energy transfer (FRET) or surface plasmon resonance (SPR). These assays help visualize how signaling components interact and the dynamics of these interactions in living cells or cell-free systems.

Additionally, incorporating Dnp-RNATAV-NH2 in signaling studies may provide insights into the temporal aspects of pathway activation. Signaling pathways are dynamic, and understanding when specific signaling events occur is as important as knowing their order. By using peptides that interact selectively with different pathway components, researchers can chart activation timelines and elucidate the sequence of biochemical events following a stimulus. In conclusion, Dnp-RNATAV-NH2 serves as a powerful tool in the researcher's arsenal to unravel the complexities of cellular signaling pathways. By offering specificity, modifiability, and compatibility with various analytical techniques, it enhances our ability to comprehend cellular signaling mechanisms and their broader implications for health and disease.

What are the benefits of using synthetic peptides like Dnp-RNATAV-NH2 in laboratory research?
The use of synthetic peptides such as Dnp-RNATAV-NH2 in laboratory research offers numerous benefits that help push the boundaries of biological and biochemical inquiry. One of the primary advantages is the high degree of specificity and versatility they offer. This specificity is foundational in designing peptides to interact with precise molecular targets, enabling detailed study of cellular components, pathways, and interactions. Researchers can tailor these peptides to meet specific requirements, whether it's to serve as enzyme substrates, competitive inhibitors, or structural probes. This adaptability ensures that synthetic peptides can be crafted to meet a wide range of experimental demands, from fundamental biology to complex drug discovery efforts.

Synthetic peptides like Dnp-RNATAV-NH2 also offer the benefit of reproducibility and consistency, critical factors in scientific research. Unlike biological samples, which can vary due to factors such as genetic differences or environmental conditions, synthetic peptides are manufactured using controlled processes. This production consistency ensures that peptide properties are uniform across batches, leading to highly reproducible experiments. Such consistency is invaluable for assays requiring precise quantification and comparison, directly impacting the reliability of research findings. Another significant benefit is the ability to incorporate unnatural amino acids and chemical modifications, expanding the functionality of these peptides beyond what is available in nature. This flexibility allows for the incorporation of elements such as fluorescent tags or biotinylation, facilitating tracking in cellular environments or enhancing detection capabilities.

Moreover, synthetic peptides like Dnp-RNATAV-NH2 often have improved stability compared to their natural counterparts. Peptides can be engineered for enhanced resistance to enzymatic degradation, an essential quality for experiments involving prolonged incubation times or studies requiring in vivo application. This stability ensures that the peptide will remain intact and functionally active throughout the experimental duration, a critical factor in obtaining meaningful and accurate results. Lastly, the ease of synthesis and modification makes synthetic peptides cost-effective and time-efficient tools for research laboratories. Advances in peptide synthesis technologies have made it possible to produce complex peptides quickly and at lower costs, democratizing access to these crucial research tools across various research settings.

In sum, synthetic peptides like Dnp-RNATAV-NH2 provide a flexible, reproducible, and customizable approach to exploring biological questions, leading to more thorough and insightful scientific investigations. They are central to advancing research across numerous life science disciplines, contributing directly to the development of new therapeutic and diagnostic applications.
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