Synonym |
Human Renin Substrate |
Species |
Human |
Protein Accession |
NA |
Purity |
≥ 95% |
Endotoxin Level |
< 1 EU/μg |
Biological Activity |
NA |
Expression System |
Chemical Synthesis |
Fusion Tag |
NA |
Predicted Molecular Mass |
1620.9 Da |
Formulation |
Supplied as a lyophilized powder |
Reconstitution |
Centrifuge vial before opening. Reconstitute in sterile distilled water or aqueous buffer
containing 0.1% BSA to a concentration of 0.1-1.0 mg/ml. |
Storage & Stability |
Store lyophilized protein at -20°C. Aliquot reconstituted protein and store at -20°C to -80°C.
Avoid repeated freeze-thaw cycles. |
FAQ
What is Tetradecapeptide Renin Substrate (human)?
Tetradecapeptide Renin Substrate (human) is a
synthetic peptide designed to mimic a specific portion of the naturally occurring human angiotensinogen,
the substrate for the enzyme renin. The interaction between renin and angiotensinogen is crucial for the
regulation of blood pressure and electrolyte balance via the renin-angiotensin system (RAS), a hormone
system within the body. This synthetic peptide acts as a model to study the physiological and
biochemical processes involved in the regulation of this system. It can provide insights into the
mechanisms of hypertension and kidney diseases, as the peptide represents the substrate that renin acts
upon to produce angiotensin I, a precursor to the vasoconstrictor angiotensin II. In laboratories,
Tetradecapeptide Renin Substrate (human) is utilized to evaluate renin activity and study various
aspects of its inhibition or stimulation, which can be integral in developing treatments for conditions
related to blood pressure regulation. This research is vital as it assists in understanding how
interruptions or malfunctions in the RAS can lead to pathophysiological conditions, including
cardiovascular diseases. Thus, the study of this substrate helps researchers delve deeper into potential
therapeutic avenues and the genesis of various hypertension-related conditions. Deeper exploration at
the molecular level of this renin substrate can lead to novel approaches in the treatment and management
of diseases caused by RAS dysfunction.
How does Tetradecapeptide Renin Substrate (human) function
in the study of the renin-angiotensin system?
Tetradecapeptide Renin Substrate (human) functions
primarily as a tool in biochemical and physiological research to elucidate the complex workings of the
renin-angiotensin system (RAS). The RAS is a multi-enzyme cascade responsible for regulating blood
volume, systolic pressure, and electrolyte balance in the body. The system is activated when renin, an
enzyme secreted by the kidneys, cleaves angiotensinogen to form angiotensin I. The Tetradecapeptide
Renin Substrate serves to imitate this natural substrate, enabling researchers to probe the efficiency
and kinetics of the renin-angiotensinogen interaction. In experimental setups, this synthetic substrate
is instrumental in gauging renin activity under various conditions, which is invaluable when assessing
how different factors may influence the RAS. For instance, understanding how specific inhibitors or
genetic mutations affect the catalytic efficiency of renin can be determined using this substrate.
Furthermore, it becomes a basis for investigating how environmental factors like diet, stress, and
exercise engage with the RAS in living organisms. By using this model substrate, the enzymatic cleavage
can be quantitatively monitored, providing key insights into enzyme-substrate specificity and subsequent
regulatory mechanisms within the RAS. Hence, it plays a crucial role in broadening the scientific
community’s comprehension of normal renal and cardiovascular functionality, as well as in understanding
what goes awry in disease scenarios such as hypertension, heart failure, and chronic kidney
disease.
What are potential applications of studying Tetradecapeptide Renin Substrate
(human)?
The study of Tetradecapeptide Renin Substrate (human) opens various doors for
applications spanning medical research and pharmacology aimed at tackling cardiovascular diseases and
hypertension. By using the substrate as a model system, researchers can deepen their understanding of
how the RAS functions at a molecular level. One primary application is the investigation of renin
activity, which is central to the regulation of blood pressure. Understanding this enzyme's role
facilitates the development of novel pharmaceuticals that can either inhibit or modulate its activity,
providing breakthroughs in anti-hypertensive therapies. Moreover, since renin activity is pivotal in the
pathophysiology of several conditions, from congestive heart failure to renal disorders, insights
gleaned from studying the Tetradecapeptide Renin Substrate can inform targeted therapeutic interventions
and personalized medicine approaches. Another critical area of application is in drug development and
testing. Pharmaceutical companies can employ this substrate to screen potential renin inhibitors, a
pivotal step in drug discovery and optimization. The assays developed around the Tetradecapeptide Renin
Substrate can be pivotal in assisting pharmacologists in selecting compounds with the desired efficacy
and safety profile, speeding up the development process of effective interventions. In research focused
on genetic predispositions and mutations that affect the RAS, this substrate provides a controlled
environment to explore how these genetic factors may alter enzyme dynamics and impact vascular and renal
health. Additionally, the substrate can serve in educational and training settings, offering medical and
scientific students a practical perspective on how enzymes, substrates, and inhibitors interplay within
critical physiological systems. These diverse applications underscore the substrate’s utility not just
as a research tool but as a cornerstone for innovative healthcare solutions and academic
enlightenment.
How does understanding Tetradecapeptide Renin Substrate (human) contribute to
hypertension research?
Understanding Tetradecapeptide Renin Substrate (human) significantly
contributes to hypertension research by offering insights into the biochemical pathways and regulatory
mechanisms of the renin-angiotensin system (RAS). Hypertension, or high blood pressure, is often
associated with heightened renin activity, which leads to increased production of angiotensin II — a
potent vasoconstrictor contributing to elevated blood pressure levels. By utilizing the Tetradecapeptide
Renin Substrate as an analytical tool, researchers can quantify renin activity and observe how it
correlates with blood pressure regulation. This substrate-based approach provides a clear understanding
of how renin catalyzes the conversion of angiotensinogen to angiotensin I under varying physiological
and pathological conditions. The substrate’s role in hypertension research extends to exploring the
molecular interactions between renin and its inhibitors. Understanding these interactions helps in the
design of specific and effective renin inhibitors, offering a strategic approach to managing
hypertensive patients. Furthermore, the substrate aids in discerning how different factors such as
genetics, diet, or medications can alter renin efficiency and thus impact blood pressure. This
understanding is invaluable in identifying subgroups within the hypertensive population who may benefit
from tailored therapeutic strategies. It also contributes to discovering biomarkers for early detection
and stratification of risk in hypertensive patients, which is crucial for implementing preventative
measures. Additionally, research using this substrate can reveal the broader impacts of
renin-angiotensin system modulation, such as its role in inflammation and cardiovascular remodeling
associated with sustained high blood pressure. Thus, the incorporation of Tetradecapeptide Renin
Substrate into hypertension research can drive innovations in treatment and prevention strategies,
improving patient outcomes and contributing to a broader understanding of hypertension’s underlying
causes.
Can Tetradecapeptide Renin Substrate (human) be used in pharmaceutical
development?
Yes, Tetradecapeptide Renin Substrate (human) holds significant potential for use in
pharmaceutical development, particularly in the context of designing and testing medications that target
the renin-angiotensin system (RAS). This is because the synthetic substrate mimics angiotensinogen, the
natural substrate for renin, thus allowing researchers and pharmaceutical developers to replicate and
study the enzyme-substrate interactions that are crucial for blood pressure regulation. By utilizing
this substrate, pharmaceutical companies can undertake preclinical testing of drug candidates that aim
to inhibit or modulate renin activity. This is especially relevant for developing drugs that can manage
hypertension or cardiovascular diseases exacerbated by overactive RAS. The substrate provides a
controlled and reproducible means to measure the efficacy of potential renin inhibitors, thus guiding
the iterative process of drug optimization. Furthermore, the substrate aids in the elucidation of
mechanistic insights, shedding light on how novel drug candidates impact the enzymatic action of renin.
In addition to inhibitor development, the substrate is pivotal in evaluating the potential side effects
and safety profiles of compounds, thereby advancing the preclinical phase of drug development. Utilizing
the Tetradecapeptide Renin Substrate also allows for the exploration of new therapeutic targets within
the RAS pathway, potentially identifying alternative intervention points that could lead to novel
treatment methods. Beyond therapeutic uses, the substrate can be essential in the development of
diagnostic tests, such as those aimed at measuring renin activity in clinical settings, thus
contributing to diagnostic advancements. The combination of these factors underscores the substrate’s
role as an invaluable asset in pharmaceutical development aimed at mitigating the clinical and economic
burdens of hypertension and related disorders, steering the path toward more effective and tailored
therapeutic solutions.