Taiy Chemical
ACTH (1-16) C75H106N20O19S 22006-64-0
Synonym ACTH (1-16)
Species Human
Protein Accession P01189
Purity Greater than 95% as determined by SEC-HPLC
Endotoxin Level Less than 1 EU/μg
Biological Activity The ED50, calculated by the dose-dependant stimulation of cAMP production in mouse Y1 cells, is less than 1 ng/ml
Expression System E. coli
Fusion Tag None
Predicted Molecular Mass 2855.4 Da
Formulation Lyophilized from a 0.2 μm filtered solution in PBS
Reconstitution Centrifuge vial before opening. When reconstituting the product, gently pipet and wash down the sides of the vial to ensure full recovery of the protein into solution.
Storage & Stability Store at -20°C. After reconstitution, store at 4°C for up to one week. For long term storage, aliquot and store at -20°C or -80°C. Avoid repeated freeze-thaw cycles.
FAQ
What is ACTH (1-16) C75H106N20O19S 22006-64-0 used for in research applications?

ACTH (1-16), or Adrenocorticotropic Hormone fragment 1-16, with the molecular formula C75H106N20O19S and CAS number 22006-64-0, is a peptide primarily utilized in scientific research focusing on endocrinology and metabolic disorders. Researchers are particularly interested in this fragment because it represents a specific portion of the full ACTH hormone, which is involved in stimulating the adrenal glands to produce cortisol, a vital hormone for stress response. By studying ACTH (1-16), scientists can gain insights into its role in the biological pathway of hormone regulation. Research using ACTH (1-16) is crucial for understanding the sequential structure-function relationship of ACTH and for exploring potential therapeutic agents that might mimic or inhibit its action. This fragment allows researchers to isolate particular effects of ACTH, excluding the full hormone’s other potential interactions in the body. Moreover, studies can focus on the peptide’s involvement in stress-related biological responses, including its neurological and psychological impacts. Researchers might use ACTH (1-16) to analyze receptor binding affinity and specificity or to develop assays for detecting ACTH levels in biological samples. Such insights are important for developing treatments for diseases such as Cushing's disease, Addison's disease, and other disorders of the hypothalamic-pituitary-adrenal (HPA) axis. Moreover, since this peptide can serve as a model systems tool in physiological and pathophysiological situations, it is extensively used to understand how certain conditions affect its function and regulation. Consequently, ACTH (1-16) plays a pivotal role in pharmacological research which aims to modulate ACTH pathways for therapeutic benefit. These research avenues can ultimately lead to significant advancements in medical science, particularly for diseases linked to dysregulation of the HPA axis. Additionally, ACTH (1-16) may be used in comparative studies against other fragments of ACTH to assess its unique effects and mechanisms.

How does ACTH (1-16) C75H106N20O19S 22006-64-0 differ from the full-length ACTH peptide?

ACTH (1-16) is a fragment of the adrenocorticotropic hormone consisting of the first 16 amino acids of the full-length peptide. The full-length ACTH comprises 39 amino acids, with each part of the molecule contributing to its overall biological function and receptor interactions. The significance of utilizing ACTH (1-16) in research stems from the need to understand which parts of the ACTH molecule are responsible for specific biological activities. While the full-length ACTH is essential for triggering cortisol production in the adrenal cortex, its various regions, including ACTH (1-16), may exert distinct activities. The fragment itself retains a portion of the biological activity but is often employed to elucidate its exact role in the receptor binding process and subsequent intracellular signaling pathways. By focusing specifically on ACTH (1-16), researchers can discern which functions are attributed to this part of the molecule without interference from the remaining amino acids in ACTH 1-39 which might have additional roles or effects. Importantly, while the full-length hormone is known to activate the MC2R (melanocortin 2 receptor) to stimulate steroid synthesis, ACTH (1-16) may have specific receptor binding characteristics that differ from the entire peptide. It can provide insights into binding interactions, efficacy, and potency within adrenal receptor environments. Studies may further reveal if ACTH (1-16) can modulate other melanocortin receptors, thus broadening its linkage to other physiological effects beyond cortisol secretion. Therefore, ACTH (1-16) offers an invaluable investigative framework to explore the pharmacological potential and mechanistic pathways of ACTH fragments, furthering the development of selective peptide-based therapies that could offer more targeted approaches with potentially fewer side effects compared to full-length hormone utilization.

What are the mechanistic insights into ACTH (1-16) effects on cellular processes?

The mechanistic insights into ACTH (1-16) involve its ability to interact with specific cellular receptors to elicit biological responses, critical in the understanding of hormone regulation and therapeutic modulation. ACTH, a product of the proopiomelanocortin (POMC) gene, is central to stress response by promoting glucocorticoid release from the adrenal glands. ACTH (1-16), as a fragment, engages primarily with the melanocortin 2 receptor (MC2R), a G protein-coupled receptor (GPCR) located in the adrenal cortex. Upon binding, ACTH (1-16) triggers a conformational change in the receptor that activates intracellular G-proteins, which subsequently elevate cAMP production through adenylyl cyclase activation. Increased cAMP acts as a secondary messenger that promotes protein kinase A (PKA) activity, leading to downstream phosphorylation of target proteins integral to cortisol synthesis and secretion. While the primary role of the full-length hormone is to manage cortisol levels and stress response, the studies focusing on ACTH (1-16) provide evidence that specific signaling cascades can be dissected and targeted for focused therapies. Moreover, research may indicate that ACTH (1-16) influences gene transcription pathways that correlate with cellular growth, ion channel regulation, and even immune modulation. Each mechanistic step offers a potential target for pharmaceutical interventions, highlighting the importance of receptor and downstream signaling specificity. Experimental studies have been instrumental in determining the changes in cyclic AMP levels and protein kinase activity in response to ACTH (1-16), helping delineate its functional domains within cellular processes. Research delving deeper into these mechanistic pathways opens the door for new pharmacological tools that utilize synthetic ACTH (1-16) analogs, which can selectively mimic or inhibit its action in adrenal and extra-adrenal tissues, potentially leading to groundbreaking treatments for disorders such as adrenal insufficiency or ACTH receptor dysregulation. Additionally, exploring the potential immunomodulatory roles of ACTH (1-16) may further refine its application in immune-related disorders.

Can ACTH (1-16) C75H106N20O19S 22006-64-0 impact other physiological systems outside adrenal functions?

Yes, ACTH (1-16) has the potential to impact physiological systems beyond traditional adrenal cortex functions. While its predominant role is encapsulated within the endocrine system's regulation of cortisol production, ACTH (1-16) can also modulate several other physiological responses, owing to its interactions with melanocortin receptors expressed in various tissues. Melanocortins, the substrate class to which ACTH belongs, interact with five distinct melanocortin receptors (MC1R through MC5R), each contributing to a variety of biological processes ranging from pigmentation, energy homeostasis, to immune regulation. ACTH (1-16) primarily interacts with MC2R to regulate adrenal steroidogenesis, yet it binds with varying affinity to other melanocortin receptors expressed in tissues such as the skin, brain, and immune cells, indicating broader physiological roles. For instance, ACTH (1-16) may play a part in influencing immune responses through MC1R or MC5R, which have implications in anti-inflammatory pathways, as these receptors mediate effects on cytokine production and modulate immune cell activity. Its interaction with MC4R in the central nervous system implicates potential roles in appetite regulation and energy balance, providing a basis for research into metabolic disorders. Although the exact physiological implications of ACTH (1-16) on non-adrenal systems require further elucidation, studies suggest that synthetic analogs of this peptide could be explored for benefits that extend outside traditional cortisol-related therapies. Furthermore, the fragment's activity in promoting skin pigmentation through MC1R in melanocytes points to potential cosmetic or dermatological applications, offering melanotropic effects that might be leveraged in treating conditions like vitiligo or other pigmentation disorders. These overlaps in physiological influence signify that ACTH (1-16) is not solely an adrenal modulator but a versatile peptide with a promising therapeutic potential across diverse biological systems, making it a focal point of interest within multidisciplinary research areas.

What are the potential therapeutic applications of ACTH (1-16) in medical science?

ACTH (1-16) holds considerable promise within therapeutic contexts, primarily due to its role in modulating the adrenocortical system and potential influences over other physiological domains. In medical science, the therapeutic applications of ACTH (1-16) span several areas, including endocrine, neurological, immunological, and dermatological fields. One of the primary applications of ACTH (1-16) lies in treating adrenal insufficiency conditions, such as Addison's disease, where this peptide fragment might serve as a precursor signal to stimulate insufficient adrenal activity with greater specificity than full-length ACTH. Its targeted interaction with melanocortin receptors provides a scaffold for developing analogs that can act as agonists or antagonists, enhancing or inhibiting specific signaling pathways. Moreover, ACTH (1-16) is being explored for its implications in neurodegenerative diseases, implicating its potential neuroprotective effects. By modulating stress responses through its central nervous system receptors, it may contribute to therapeutic strategies that alleviate the adverse impacts of chronic stress and inflammation on neurological health. In conjunction with standard treatments, ACTH (1-16) could improve quality of life by managing symptoms related to stress-induced neurochemical dysregulation. Furthermore, emerging research supports possibilities of ACTH (1-16) in immunomodulation. Given its potential to interact with melanocortin receptors on immune cells, this peptide could help manage inflammation or autoimmune conditions, augmenting the immune response while minimizing excessive inflammation. In dermatology, ACTH (1-16)'s potential role in pigmentation offers another therapeutic avenue, particularly in treating pigmentary disorders. Melanocortins like ACTH (1-16) can stimulate melanocytes, providing treatment strategies for conditions involving pigmentation, including vitiligo or albinism, by enhancing melanin production. Consequently, the therapeutic applications of ACTH (1-16) are multifaceted, rendering it a noteworthy subject in interdisciplinary research aimed at novel treatment paradigms capable of addressing complex multifaceted clinical conditions with precision-focused interventions. Its ongoing exploration in clinical studies may yield innovative therapeutic modalities, offering clinician-researchers new tools to enhance patient health outcomes in diverse medical fields.
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