Taiy Chemical
ACTH (4-11) C75H106N20O19S 22006-64-0
Synonym Corticotropin (4-11)
Species Human
Protein Accession P03950
Purity > 95%
Endotoxin Level < 1 EU/μg
Biological Activity Fully biologically active when compared to standard.
Expression System E. coli
Fusion Tag None
Predicted Molecular Mass 2483.2 Da
Formulation Lyophilized from a concentrated (5 mg/ml) solution in water containing 0.2% TFA
Reconstitution Centrifuge vial before opening. Reconstitute in sterile water 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 ACTH (4-11), and what are its primary applications in the scientific and medical fields?

ACTH (4-11), identified with the chemical structure C75H106N20O19S and CAS number 22006-64-0, is a peptide fragment derived from the adrenocorticotropic hormone (ACTH). This segment specifically encompasses amino acids 4 to 11. This peptide is significant because it continues to retain certain biological activities of the full-length ACTH hormone. Full-length ACTH is involved in the regulation of the adrenal cortex, influencing the secretion of glucocorticoids, and is crucial in the body's response to stress. Researchers have shown interest in ACTH (4-11) for its potential roles and effects separate from those of full-length ACTH, particularly in neuroendocrinological and behavioral contexts.

The peptide has been primarily used in laboratory settings to investigate its partial sequence and how such sequences contribute to the activity of full-length ACTH. Researchers often utilize it to better understand how specific segments of the ACTH molecule interact with receptors and influence biochemical pathways. Further, ACTH (4-11) can serve as a tool for exploring the complex processes of peptide hormone actions, such as binding affinity and specificity.

Moreover, this peptide fragment may serve as a significant component in studying neurotransmission processes. ACTH (4-11) has emerged in some studies that seek to delineate its influence on neurological functions, possibly affecting memory, learning, and mood regulation. These attributes make the peptide an intriguing subject for brain research, particularly in the context of psychiatric disorder research, where altered hormonal responses could be insightful.

In medical research, ACTH (4-11) might be used to explore potential therapeutic applications, understanding its role in disorders linked with stress and hormonal imbalances. Although it does not fully emulate the effects of ACTH, its study may help develop new pharmacological strategies targeting hormonal disorders or stress-related pathologies.

Given its importance, this peptide is utilized in a wide variety of experimental setups, allowing scientists to systematically explore its properties and effects under controlled conditions. This helps to refine the understanding of peptide functionality in relation to human physiology and potential disruptions. In conclusion, ACTH (4-11) is a versatile component in biochemical and neuroendocrinological research, contributing valuable insights into the complex interactions of peptides and their roles in human health and disease.

How does ACTH (4-11) differ from the full-length ACTH in terms of structure and function?

ACTH (4-11) differs significantly from the full-length ACTH both structurally and functionally. Structurally, full-length ACTH is a peptide comprising 39 amino acids, responsible for its complete range of biological activities. In contrast, ACTH (4-11) is a shorter sequence, consisting of only 8 amino acids that represent a segment within the broader structure of full-length ACTH. This peptide fragment retains a specific sequence segment from ACTH that may carry partial biological activity but lacks the full spectrum of functionality attributed to the complete hormone.

Functionally, ACTH is a critical component of the hypothalamic-pituitary-adrenal (HPA) axis, stimulating the adrenal glands to produce and release cortisol, a crucial hormone in stress response, metabolism, and immune function regulation. Full-length ACTH binds to melanocortin receptors on the adrenals, activating signaling pathways that lead to cortisol production. This process involves precise conformational changes and receptor interactions that are unique to the full 39-amino acid structure of ACTH, which ACTH (4-11) cannot replicate due to its truncated form.

Moreover, ACTH (4-11), due to its limited sequence, may interact differently with receptor sites or exhibit entirely distinct patterns of interaction at a molecular level. The shortened structure might mean that while it has some receptor binding capacity, it probably has reduced or altered activity compared to full-length ACTH. Researchers often use peptide fragments like ACTH (4-11) to investigate specific segments' roles in receptor interaction. These studies help decipher how structure affects function across complex peptide molecules.

Furthermore, ACTH (4-11) may partake in interactions beyond the scope of the adrenal cortex, potentially influencing neurological pathways. Some findings suggest a connection between this fragment and behavioral and mood influences, unlike the broader systemic roles of complete ACTH. This exploration holds significance in neuroendocrinology, where distinct peptide fragments provide insights into peptide function in the central nervous system, potentially leading to innovative therapeutic approaches for mood and anxiety disorders and cognitive function modulation.

In summary, while ACTH (4-11) retains a fraction of the structural features of full-length ACTH, its function and applications diverge significantly due to its shorter sequence. These differences make the peptide both limited and valuable, presenting opportunities for specialized research applications that contribute uniquely to scientific understanding in endocrinology and neuroscience.

What are the potential research applications and therapeutic implications of ACTH (4-11)?

The research applications and potential therapeutic implications of ACTH (4-11) are broad and multifaceted, primarily due to its role as a peptide fragment with distinct biological properties compared to the full-length ACTH hormone. One of the primary research applications is in the field of endocrinology, where scientists utilize this fragment to study specific hormone signaling pathways. Since ACTH (4-11) is a segment of the complete ACTH sequence, researchers can employ it to hone in on particular biochemical interactions and receptor engagements that occur within the broader context of hormonal regulation by full ACTH.

Moreover, ACTH (4-11) is valuable in neuroscientific research as scientists explore its effects on brain function and behavior. Preliminary studies indicate that this peptide may influence processes related to memory, mood, and behavior, making it a significant point of interest in researching psychiatric disorders and cognitive health. Understanding how this peptide fragment interacts with receptors and contributes to neurological signaling can provide insight into potential treatment avenues for mood disorders, anxiety, and neurodegenerative diseases.

Therapeutically, while ACTH (4-11) is not presently used as a direct treatment, its exploration could lead to the development of new pharmacological agents targeting specific conditions. For instance, if the influence of ACTH (4-11) on mood and behavior can be confirmed and more clearly understood, it could inspire the creation of novel therapies for stress-related disorders or cognitive impairments. Additionally, by examining how this peptide affects cellular signaling pathways, researchers might identify new therapeutic targets that address hormonal imbalances or enhance cognitive resilience against stress.

In the context of drug development, ACTH (4-11) could serve as a lead compound or model structure for designing analogs with enhanced stability or specificity for therapeutic applications. Its unique interactions with biological systems provide an insightful basis for novel drug design paradigms that could optimize desired effects while minimizing side effects.

Furthermore, ACTH (4-11) offers applications in translational medicine, where understanding its mechanisms could aid in bridging laboratory findings with clinical applications. By identifying how certain peptide sequences mediate physiological responses, precision therapies tailored to individual hormonal or neurological profiles may be developed. Such personalized medical strategies could revolutionize treatment options for chronic conditions influenced by hormonal activity and neurological function.

Lastly, in the field of molecular biology, ACTH (4-11) can be employed to study peptide-receptor interactions at a detailed molecular level, providing foundational knowledge that can underpin various biotechnological innovations. These might include diagnostic advancements or novel therapeutic delivery mechanisms that capitalize on the specificity and targeted action of peptide-based substrates.

Collectively, the research and therapeutic potential of ACTH (4-11) spans several domains, offering a promising platform for advancing both scientific understanding and clinical applications.

What methodologies are most frequently used to study ACTH (4-11) and its effects on biological systems?

Studying ACTH (4-11) and its effects on biological systems requires a diverse array of methodologies, reflecting the peptide’s complex role within the human body. One primary methodology is the use of in vitro assays, which allow researchers to investigate the molecular interactions of ACTH (4-11) under highly controlled laboratory conditions. These assays can include receptor binding studies where scientists assess how the peptide interacts with specific protein targets on cell surfaces. By understanding these interactions, researchers can deduce how ACTH (4-11) might influence cellular pathways, including those crucial for hormonal or neurological responses.

Another common methodological approach is the application of in vivo animal models, providing an opportunity to observe the systemic effects of ACTH (4-11) in a complete physiological context. In such experiments, researchers inject the peptide into model organisms, such as rodents, to monitor changes in behavior, hormonal regulation, or neurological responses. These studies provide valuable insights into the peptide's potential effects on stress response, cognitive function, and overall homeostasis, contributing significantly to the translational aspect of biomedical research.

Mass spectrometry is also frequently used to characterize the peptide and study its interaction with other proteins or peptides, which allows for the precise identification of structural and compositional nuances that may impact ACTH (4-11) activity. Structural elucidation insights garnered from techniques like nuclear magnetic resonance (NMR) or X-ray crystallography might further clarify how specific structural elements of the peptide align with their functional roles, potentially informing the design of analogs for therapeutic purposes.

Cell culture systems provide another methodological avenue, offering a simplified yet functional model of cellular environments where the effects of ACTH (4-11) can be meticulously examined. These systems enable the examination of peptide effects on cell signaling, gene expression, and functional responses in a controlled setting. For instance, studying how ACTH (4-11) influences glucocorticoid production in adrenal cell lines could illuminate its potential as a modulator of hormonal activity.

Electrophysiological techniques may also be employed to assess the peptide’s action on neuronal activity. Investigating how ACTH (4-11) alters synaptic transmission or neuronal excitability can reveal its influence on brain function and behavior. This approach is particularly valuable in discerning potential applications in mental health and neurology, where precise modulation of neuronal pathways is critical.

Finally, computational modeling and simulations provide a modern methodology to predict the interactions and potential pathways influenced by ACTH (4-11). Such in silico approaches can offer predictive insights that guide experimental design and hypothesis formulation, helping to streamline research efforts by highlighting likely molecular targets or interactions.

Collectively, these methodologies not only advance the understanding of ACTH (4-11) in biological systems but also pave the way for innovative therapeutic applications and scientific discoveries.

What safety considerations should be taken into account when handling ACTH (4-11) in a research setting?

When handling ACTH (4-11) in a research setting, a range of safety considerations must be taken into account to ensure both researcher safety and experimental integrity. Firstly, understanding and adhering to established protocols for peptide handling is essential. Detailed knowledge of the chemical and physical properties of ACTH (4-11) should be reviewed before commencing any laboratory work to incorporate specific safety measures appropriately.

Researchers must employ appropriate personal protective equipment (PPE) such as lab coats, gloves, and safety goggles to minimize exposure risks. Given that ACTH (4-11) is a biologically active peptide, unintended substance contact can lead to unforeseen biological effects, making physical barriers critical for protection. In addition, working in a well-ventilated laboratory space or using appropriate fume hoods can further mitigate potential inhalation exposure to peptide aerosols or powdered forms.

Correct storage of ACTH (4-11) is paramount in maintaining its stability and efficacy while ensuring laboratory safety. The peptide should be stored in tightly sealed vials, typically at low temperatures, to prevent degradation and maintain potency. Researchers should also be cautious of peptide lyophilization processes, where handling should be conducted under reduced temperatures and conditions minimizing peptide loss or exposure to humidity.

Proper training in peptide-related laboratory procedures is another critical safety consideration. This includes the correct usage of laboratory instruments and familiarity with data sheets describing the properties, hazards, and first aid measures related to ACTH (4-11). Training ensures that laboratory personnel can effectively manage these substances and respond accurately and effectively to any accidental exposure or spillage incidents.

Documentation and labeling are fundamental for ensuring safety and traceability in laboratory environments. All tubes and containers with ACTH (4-11) should be clearly labeled with the peptide's identity, concentration, preparation date, and relevant handling instructions. This precaution aids in preventing accidental misuse or cross-contamination and facilitates accurate experimental replication.

Additionally, researchers should implement stringent waste disposal protocols for materials that have come into contact with ACTH (4-11). Decontamination and disposal should comply with institutional and regulatory guidelines to prevent environmental contamination or unauthorized exposure beyond the laboratory setting.

Lastly, comprehensive risk assessments should be performed before initiating experiments involving ACTH (4-11). These evaluations help identify potential hazards associated with peptide handling and inform decision-making processes around control measures required to maintain a safe working environment.

By rigorously applying these safety considerations, researchers can effectively manage the risks associated with handling ACTH (4-11) while fostering a secure and efficient research space.
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