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.