Taiy Chemical
(Phe22)-Big Endothelin-1 Fragment (19-37) (human
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.
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