Synonym |
Acetyl-tetradecapeptide renin substrate (human) |
Species |
Human |
Protein Accession |
P00797 |
Purity |
Greater than 95% as determined by SDS-PAGE |
Endotoxin Level |
Less than 1 EU/μg |
Biological Activity |
Not available |
Expression System |
E. coli |
Fusion Tag |
None |
Predicted Molecular Mass |
1.6 kDa |
Formulation |
Lyophilized from a 0.2 μm filtered solution in PBS |
Reconstitution |
It is recommended to reconstitute the lyophilized product with sterile water at a concentration
of 0.1 mg/ml, which can be further diluted into other aqueous solutions |
Storage & Stability |
Store at -20°C. For long-term storage, store at -80°C. Once reconstituted, store at 4°C for
short-term use and -20°C for long-term storage |
FAQ
What is Acetyl-Tetradecapeptide Renin Substrate (human), and what makes it
unique?
Acetyl-Tetradecapeptide Renin Substrate (human) is a synthetic peptide based on the human
renin substrate sequence. Renin is an enzyme that plays a critical role in the regulation of blood
pressure, electrolyte balance, and fluid homeostasis, making this particular substrate highly
significant in both physiological and research contexts. This peptide is uniquely designed to mimic the
natural substrate of the renin enzyme, allowing researchers to study the enzyme's activity and its role
in the renin-angiotensin system (RAS) effectively.
What sets Acetyl-Tetradecapeptide Renin
Substrate apart is its precise replication of the natural substrate’s characteristics, including the
structural and sequence fidelity that allow for the accurate modeling of substrate-enzyme interactions.
This specificity is crucial for studies aiming to elucidate the biochemical pathways concerning
hypertension and other cardiovascular diseases. Furthermore, its synthetic nature provides the stability
and purity needed for consistent results in laboratory settings. Unlike natural peptides that might
degrade more quickly or be less homogenous, the synthesized version ensures that researchers are working
with a consistent and reliable material, crucial for reproducible and valid experimental
outcomes.
Additionally, this substrate is particularly valuable for drug development research. By
providing a stable and predictable interaction model, researchers and pharmacologists can better design
and test potential inhibitors of renin, a strategy that holds promise for the development of therapies
for hypertension and related cardiovascular conditions. Using Acetyl-Tetradecapeptide Renin Substrate,
drugs can be screened for their efficiency in inhibiting the renin enzyme, and potential side effects
can be studied in a controlled and timely manner.
Moreover, the careful synthesis and quality
control ensure that the Acetyl-Tetradecapeptide Renin Substrate does not include impurities or
variations that might otherwise skew results or interpretations. This aspect makes it an indispensable
tool for laboratories looking to conduct in-depth research into RAS and its implications in human
health. By providing a reliable model substrate, researchers can also explore the genetic variations in
the human population that might affect the interactions between renin and its natural substrates,
leading to personalized medicine approaches for treating hypertension.
How does the
Acetyl-Tetradecapeptide Renin Substrate (human) contribute to cardiovascular research?
The
Acetyl-Tetradecapeptide Renin Substrate (human) significantly advances cardiovascular research in
numerous ways, chiefly by acting as a specialized tool for investigating the renin-angiotensin system
(RAS), which is directly implicated in the regulation of cardiovascular function. Given its role as a
precisely engineered mimic of the natural renin substrate, this peptide allows researchers to delineate
the function and regulation of renin, an enzyme centrally involved in blood pressure regulation,
electrolyte balance, and overall fluid homeostasis. Understanding how renin interacts with its
substrates and its inhibitors is pivotal for unravelling the complex physiology underpinning
hypertension and other cardiovascular diseases.
By using this substrate in cardiovascular
studies, scientists can probe into the functional mechanisms of the renin enzyme, observing how it
cleaves its substrate to influence downstream effects on the RAS. Since this substrate is engineered to
reflect the human sequence, the peptide provides a relevant physiological model to assess how variations
in this system can contribute to disease. This is particularly significant for identifying genetic
predispositions or environmental factors that may affect an individual's RAS activity, offering
potential avenues for predicting cardiovascular risk.
In the realm of therapeutic development,
the Acetyl-Tetradecapeptide Renin Substrate facilitates the testing of potential pharmacological agents
aimed at inhibiting renin activity. Renin inhibitors have been recognized as potential treatment options
for managing hypertension more effectively than current methods, and the substrate supplies a stable,
consistent means to evaluate these drugs' efficacy and mechanisms of action. By using this peptide in
high-throughput screening assays, pharmaceutical researchers can expedite the identification and
refinement of new therapeutic candidates, potentially leading to breakthroughs in hypertension
treatment.
Furthermore, the substrate’s role extends beyond drug testing, providing a controlled
experimental condition for exploring the implications of RAS modifications in various physiological and
pathophysiological states. Researchers can simulate different states of the heart and vasculature by
manipulating the substrate and enzyme interactions, thereby gaining insights into how chronic
hypertension might develop or how acute episodes of high blood pressure manifest. Through these
controlled laboratory models, deeper insights into the molecular underpinnings of cardiovascular
diseases can emerge, driving the development of novel interventions and personalized medicine approaches
that cater to the specific needs of individual patients.
Have there been any notable research
findings using the Acetyl-Tetradecapeptide Renin Substrate (human)?
Yes, there have certainly
been notable research findings wherein the Acetyl-Tetradecapeptide Renin Substrate (human) played a
pivotal role. This substrate has been instrumental in a variety of studies aiming to deepen our
understanding of the renin-angiotensin system (RAS) and its relevance in cardiovascular health and
disease. Several key findings have emerged from these studies, shedding light on the intricate dynamics
of blood pressure regulation and offering pathways for innovative therapeutic approaches.
One
significant research area has been the role of the renin enzyme within the RAS and its effect on
hypertension. Studies utilizing this precise synthetic substrate have allowed scientists to observe and
measure the catalytic efficiency and specificity of renin, leading to a better understanding of how this
enzyme is regulated in the body. Such research has highlighted differences in renin activity across
individuals and populations, pointing towards genetic or environmental factors that may influence the
prevalence and severity of hypertension.
Furthermore, through the use of Acetyl-Tetradecapeptide
Renin Substrate in controlled laboratory settings, researchers have developed a clearer picture of how
certain renin inhibitors—potential hypertensive drug candidates—interact at the molecular level with the
active site of renin. This reduces drug development times significantly, as it facilitates the rapid
screening and optimization of inhibitor compounds. It provides foundational data pivotal for advancing
these agents through clinical trials. This progress means the potential release of new classes of
hypertension drugs with improved specificity and fewer side effects than traditional
therapies.
Researchers have also used this substrate to investigate the effects of biochemical
feedback on the RAS, particularly how it influences cardiac and renal pathology. By closely examining
these interactions, scientists have started to unlock how chronic conditions, such as heart failure or
kidney disease, can be linked to dysregulation within the RAS. This substrate has, therefore, provided
insight into preventive measures or early interventions that could mitigate the progression of these
chronic conditions.
The authenticity and consistency of this substrate have enabled large,
collaborative studies looking into population-level health issues. These studies assess how lifestyle
changes, including diet and exercise, might modulate RAS activity and, in turn, impact cardiovascular
health. By offering a reliable model for studying these interactions, the Acetyl-Tetradecapeptide Renin
Substrate has become a cornerstone for research initiatives aiming to curb the global burden of
cardiovascular diseases through both clinical and lifestyle modifications.
Overall, the research
findings leveraging the Acetyl-Tetradecapeptide Renin Substrate have paved the way for a deeper
molecular understanding of hypertension, innovative treatment strategies, and customized patient care
pathways. They continue to contribute significantly to the global effort to effectively manage
cardiovascular diseases.
How is the Acetyl-Tetradecapeptide Renin Substrate (human) used in
laboratory settings, and what are the practical considerations?
The use of
Acetyl-Tetradecapeptide Renin Substrate (human) in laboratory settings is integral to biochemical and
pharmacological research, especially concerning studies of the renin-angiotensin system (RAS) and
cardiovascular health. In practical terms, this synthetic peptide serves as a crucial tool for assays
aimed at analyzing the activity of renin, providing a consistent and scientifically valid model for
understanding this enzyme’s function under various conditions and within different experimental
frameworks.
In a laboratory setting, researchers often employ this substrate in enzyme kinetic
studies to determine the efficiency and specificity of renin. These studies involve quantifying how
renin interacts with its substrate, detailing aspects such as the Michaelis-Menten constants or
inhibitor effects. By optimizing these assays, researchers can generate invaluable data on how renin’s
activity might vary based on genetic or environmental influences, contributing to a broader
understanding of cardiovascular physiology and pathology.
Moreover, the substrate is widely
employed in screening assays for novel renin inhibitors. Researchers use high-throughput screening
methodologies that allow them to test numerous compounds against the standard activity of this
substrate. Such processes are fundamental for the drug discovery pipeline, providing early-stage
insights into how potential drugs might inhibit renin activity more effectively or with fewer side
effects than existing treatments. These studies rely on the substrate's stability and purity, ensuring
that the results are attributable to the test compounds, not extraneous variables or experimental
inconsistencies.
Practical considerations when using the Acetyl-Tetradecapeptide Renin Substrate
in laboratories include the need for meticulous handling to maintain its integrity and activity.
Laboratories must store the substrate under recommended conditions, often at low temperatures, to
prevent degradation. Additionally, researchers may need to account for the peptide’s concentration and
purity when designing experiments, ensuring that these parameters align with standardized protocols for
enzyme assays or drug screening.
Another critical aspect is ensuring compatibility with the
analytical methods used to quantify enzyme-substrate interactions. This may involve using
chromatography, mass spectrometry, or fluorescence-based techniques, each with specific requirements for
sample preparation and data analysis. Researchers must select the appropriate methods that align with
these requirements to maximize the accuracy and reliability of their data.
The substrate’s
potential to model human physiological conditions closely also necessitates an awareness of the broader
experimental design, including the selection of appropriate cellular or in vivo models if more complex
system interactions are under investigation. This holistic approach ensures that outcomes not only
reflect enzyme dynamics but also inform real-world physiological contexts.
Ultimately, the
integration of the Acetyl-Tetradecapeptide Renin Substrate into laboratory research embodies a
commitment to precision and innovation. Its appropriate use facilitates cutting-edge research that
advances scientific understanding and drives the development of therapeutic strategies aimed at
improving human health.
What are the broader implications of using the Acetyl-Tetradecapeptide
Renin Substrate (human) in biomedical research?
The broader implications of using
Acetyl-Tetradecapeptide Renin Substrate (human) in biomedical research are extensive, spanning from
improved understanding of fundamental biological processes to innovative approaches in drug development
and personalized medicine. Given the critical role of the renin-angiotensin system (RAS) in regulating
blood pressure and fluid balance, insights gained through research using this substrate have
far-reaching impacts on how cardiovascular and related diseases are understood, treated, and managed
globally.
One significant implication is the potential for personalized medicine approaches in
treating hypertension and cardiovascular diseases. As researchers deepen their understanding of how the
renin enzyme interacts with its substrate, considering individual genetic and environmental variations,
they can develop more tailored treatments. Personalized therapies that are based on a precise knowledge
of an individual’s unique RAS characteristics could revolutionize hypertension management, reducing the
risk of side effects and improving patient outcomes. The Acetyl-Tetradecapeptide Renin Substrate
facilitates these personalized approaches by providing a model that reflects human physiological
conditions accurately.
Moreover, the substrate empowers the development of new pharmacological
agents. By understanding its interactions with potential inhibitors, researchers can devise more
specific drugs aimed at curbing renin activity, providing alternatives to existing antihypertensive
medications. This is vital not only in addressing drug efficacy issues but also in overcoming side
effects associated with broad-spectrum approaches. As the substrate undergoes modifications to test
various drug interactions or resistances, it aids researchers in optimizing these therapies to offer
greater selectivity and efficacy.
In the realm of disease prevention, the insights gained through
studies with this substrate could also lead to the identification of biomarkers for early diagnosis.
Early identification of dysregulation within the RAS could prompt preventive measures long before the
clinical onset of disease symptoms, minimizing both healthcare costs and patient
distress.
Furthermore, the substrate's use extends beyond cardiovascular research into broader
systemic effects involving the kidneys, adrenal glands, and central nervous system, among others. The
RAS is interlinked with numerous physiological pathways; hence, through the improved comprehension of
this system enabled by research with Acetyl-Tetradecapeptide Renin Substrate, we can expect advancements
in treating related conditions like chronic kidney disease, heart failure, and even diabetic
complications.
Collaboratively, the pursuit of such research fosters technological and
methodological advancements. The need for precise analytical techniques to assess substrate interactions
pushes forward developments in biotechnology and analytical chemistry. These advancements contribute to
a better equipped and more knowledgeable scientific community prepared to tackle a range of biomedical
challenges.
Given these expansive implications, Acetyl-Tetradecapeptide Renin Substrate remains a
vital component in the toolkit of modern biomedical research. Its applications and the resulting
insights foster a deeper understanding of human health and disease, ultimately driving progress towards
more effective, accessible, and individualized healthcare solutions.