Synonym |
ET-1 (19-37) |
Species |
Human |
Protein Accession |
P63104 |
Purity |
Greater than 98% as determined by HPLC and SDS-PAGE |
Endotoxin Level |
Less than 1 EU/μg as determined by LAL method |
Biological Activity |
Fully biologically active when compared to standard |
Expression System |
E. coli |
Fusion Tag |
None |
Predicted Molecular Mass |
2471.8 Da |
Formulation |
Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA |
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 at -20°C upon receipt. Do not freeze. Once reconstituted, store at 4°C for up to 2 weeks
|
FAQ
What is (Phe22)-Big Endothelin-1 fragment (19-37) (human) and how does it function in the body?
The
(Phe22)-Big Endothelin-1 fragment (19-37) (human) is a peptide fragment derived from the larger
endothelin protein, which plays a pivotal role in the regulation of vascular tone and blood pressure.
This particular fragment is synthesized to study its specific functionalities and how it interacts with
various physiological pathways. Endothelins are a group of peptides produced by endothelial cells and
are known to be potent vasoconstrictors; they contribute significantly to the regulation of
cardiovascular functions. Endothelin-1, in particular, is the best-characterized member of this family
and is involved in numerous physiological and pathological processes, including hypertension, heart
failure, and other cardiovascular diseases.
The (Phe22)-Big Endothelin-1 fragment (19-37) is
specifically engineered to mimic a certain section of the endothelin protein, allowing researchers to
investigate its intricate mechanisms of action without the confounding effects of the full-length
peptide. This fragment allows scientists to isolate and study the impact of this particular segment on
the endothelin receptor pathway. When introduced into research settings, this fragment can be used to
evaluate the binding affinity and specificity to endothelin receptors, the ET_A and ET_B receptors,
which are instrumental in mediating the biological effects of endothelin proteins.
Studies utilizing
this fragment contribute to our understanding of how selective receptor activation or inhibition can
modulate vascular tone and impact blood pressure regulation. As scientists decipher the physiological
roles of endothelin fragments, the (Phe22)-Big Endothelin-1 fragment (19-37) offers insights into
potential therapeutic applications for disorders associated with endothelin dysregulation. The
understanding gained from studying this fragment could lead to the development of new peptide-based
therapies aimed at managing or mitigating cardiovascular conditions arising from aberrant endothelin
activity.
What are the potential research applications for (Phe22)-Big Endothelin-1 fragment
(19-37) (human)?
The (Phe22)-Big Endothelin-1 fragment (19-37) (human) holds significant promise for
a multitude of research applications that extend across various areas of human health, particularly
those concerned with cardiovascular studies. This peptide fragment is used as a research tool to
investigate the complex pathways of endothelin biology and its implication in hypertension and other
cardiovascular disorders. By simplifying the complexity of studying full-length endothelins, researchers
can focus on specific biochemical interactions and mechanisms provoked by this fragment.
One primary
application is in the study of vascular physiology and pathophysiology. Researchers can utilize the
fragment to explore its role in modulating blood vessel constriction and dilation. Understanding these
pathways is fundamental for uncovering how increases or disruptions in endothelin signaling may lead to
hypertension and subsequent cardiovascular complications. Moreover, this fragment helps in analyzing
receptor-ligand interactions fundamental in receptor pharmacology. Investigating how this fragment
interacts with endothelin receptors can elucidate the process of receptor binding, activation, and
signaling pathway engagement, leading to new avenues for therapeutic targeting.
Further research
employing this fragment also delves into elucidating the role of endothelin fragments in heart disease.
By investigating how this fragment affects cardiac myocyte function, contractility, and cardiac output,
researchers may identify potential intervention strategies to address heart dysfunction and failure.
Additionally, understanding how endothelin signaling regulates cardiac hypertrophy and remodeling could
provide insights into combating heart disease.
Besides cardiovascular implications, the fragment
serves as a research axis for exploring the complex role of endothelin signaling in other organ systems,
including the kidneys and central nervous system. Potentially, this fragment could be employed to
investigate the interplay between endothelin signaling and renal function, as it pertains to fluid
balance and blood pressure homeostasis, or the implication of endothelin activity in neural conditions
and neurovascular anomalies.
How does the (Phe22)-Big Endothelin-1 fragment (19-37) (human)
contribute to understanding cardiovascular diseases?
In understanding cardiovascular diseases, the
(Phe22)-Big Endothelin-1 fragment (19-37) (human) offers a crucial resource for investigating the
molecular mechanisms that underpin these conditions. Cardiovascular diseases often arise from complex
interactions within biochemical pathways that govern vascular function, cardiac performance, and
systemic blood pressure regulation. As a segment of the larger endothelin-1 peptide, this fragment
presents a unique avenue for dissecting the specific roles that endothelin-derived peptides play in
these processes.
Researchers can utilize the fragment to examine how specific endothelin pathways
contribute to vascular dysfunction and its consequent diseases. Vascular anomalies, such as endothelial
dysfunction and altered vasomotor tone, are central features of many cardiovascular conditions,
including hypertension, atherosclerosis, and heart failure. By examining the effects of this fragment on
endothelin receptors, researchers can determine how it influences vasoconstriction and vasodilation,
leading to changes in blood pressure and vascular resistance. Understanding these interactions is
crucial for developing therapeutic interventions that target specific pathways implicated in vascular
disease.
The fragment also lends insight into the endothelin system's contribution to cardiac
hypertrophy, remodeling, and heart failure. Cardiac hypertrophy, for instance, is a maladaptive response
to increased workload and is a significant risk factor for heart failure. Research into how the
(Phe22)-Big Endothelin-1 fragment (19-37) affects myocardial cells, collagen deposition, and tissue
fibrosis is invaluable in identifying potential intervention points for treatment. By exploring how this
fragment interacts at the molecular level within cardiac cells, researchers can advance the
understanding of disease-modifying therapies that can alter the course of heart disease
progression.
Additionally, the fragment provides a model for studying the pathophysiology of
hypertension, as endothelin signaling significantly impacts systemic vascular resistance and fluid
balance. Investigating how this fragment affects renal function, through its influence on endothelin
receptor signaling in the kidneys, could help clarify the role of endothelin in blood pressure
regulation and lead to novel approaches for managing hypertension. Hence, the (Phe22)-Big Endothelin-1
fragment is an integral tool in cardiovascular research, fostering new insights and therapeutic angles
in the field.
Can the (Phe22)-Big Endothelin-1 fragment (19-37) (human) have therapeutic
potential?
The (Phe22)-Big Endothelin-1 fragment (19-37) (human) is primarily utilized in research
to deepen understanding of endothelin pathways and their role in various biological processes. While the
fragment itself is not currently used as a direct therapeutic agent in clinical settings, its study is
instrumental in paving the way for therapeutic potentials that target endothelin-related pathways in
diseases.
One avenue of potential therapeutic interest lies in the cardiovascular realm. The
endothelin system plays a crucial role in modulating blood vessel tone and kidney function, and its
dysregulation is implicated in conditions such as pulmonary arterial hypertension, systemic
hypertension, and heart failure. By studying this fragment, researchers gather insights into the
specificities of receptor-ligand interactions and signal transduction pathways involved in endothelin
signal mediation. With this knowledge, peptide-based therapies or small molecules could be designed to
target endothelin receptors selectively, thereby modulating abnormal vascular constriction or cardiac
responses linked to disease.
Furthermore, the fragment's implications in cardiac pathologies open
possibilities for therapeutic interventions aimed at heart disease. As research elucidates how
endothelin fragments influence cardiac hypertrophy and myocardial remodeling, there is a potential for
developing therapies that mitigate these changes, thereby preserving heart function in patients with
heart failure or post-myocardial infarction.
Beyond cardiovascular applications, endothelin pathways
are implicated in renal diseases and certain neurovascular disorders, suggesting that therapies emerging
from studies of this fragment could extend beyond traditional cardiovascular targets. For instance,
potential therapies could also aim to modulate endothelin activity in fibrotic diseases or conditions
characterized by endothelial dysfunction.
While the (Phe22)-Big Endothelin-1 fragment itself is not a
direct therapeutic entity, its role as a research instrument allows scientists to uncover vital insights
into disease mechanisms and potential intervention strategies. This research is pivotal in informing the
design of novel therapeutics aimed at endothelin-related pathways, with the hope of alleviating or
curing diseases associated with endothelin dysregulation. As science evolves, the findings derived from
studying this fragment could offer significant contributions to developing targeted, effective medical
treatments.
What are the challenges researchers face when studying (Phe22)-Big Endothelin-1
fragment (19-37) (human)?
Studying the (Phe22)-Big Endothelin-1 fragment (19-37) (human) presents
several challenges, which researchers often have to navigate during experiments and data interpretation.
First, the primary complexity arises from the inherent nature of biological systems, which are highly
intricate and include myriad pathways that can interact or influence the result of studies focused on
specific peptide fragments. The challenge is to isolate the specific effects of this fragment to
understand its precise role within the larger context of the endothelin pathway and its physiological
implications.
Another significant challenge is related to receptor specificity and variability in
biological responses. Endothelin receptors, namely ET_A and ET_B, show differential expression and
functional outcomes across tissues. Therefore, research using this fragment must carefully consider the
variable expression profiles and receptor subtype distribution within different tissues, as these
factors substantially impact the observed outcomes. This variability necessitates the use of precise
experimental designs and conditions to accurately characterize the fragment's influence on receptor
behavior and downstream signaling pathways.
Furthermore, technical challenges, such as issues with
peptide stability and precise quantification, can impact experimental reliability. The stability of
peptide fragments in biological assays is crucial for ensuring that the observed effects can be
unequivocally attributed to the fragment itself rather than to degradation products or nonspecific
interactions. Additionally, quantifying the precise concentrations of the peptide and monitoring its
interaction with receptors in real-time remain a technical hurdle that requires advanced analytical
techniques and instrumentation.
Ethical and logistical considerations also pose challenges; for
instance, translating findings from in vitro or animal models to human pathophysiology can sometimes
lead to unexpected complexities, as the precise replication of human physiological conditions in
experimental settings remains imperfect. Researchers must thus exercise caution in extrapolating their
findings, acknowledging the translational gap that exists until further validated by clinical
contexts.
Despite these challenges, advances in technology and methodology continuously enhance the
ability to study such peptide fragments with increasing accuracy and detail. Overcoming these challenges
requires a multifaceted approach, combining rigorous experimental design with cutting-edge analytical
techniques and comprehensive understanding of biological systems. Nonetheless, the effort invested in
overcoming these hurdles is essential as the insights gained from studying the (Phe22)-Big Endothelin-1
fragment (19-37) have the potential to drive significant progress in understanding and eventually
treating diseases associated with the endothelin pathway.