Synonym |
ACTH (2-24) |
Species |
Human, Bovine, Rat |
Protein Accession |
N/A |
Purity |
≥95% |
Endotoxin Level |
<1.0 EU per µg |
Biological Activity |
N/A |
Expression System |
Chemical synthesis |
Fusion Tag |
N/A |
Predicted Molecular Mass |
7504.9 Da |
Formulation |
Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA |
Reconstitution |
Centrifuge vial before opening. Reconstitute in 5mM HCl to a concentration of 0.1-1.0 mg/ml |
Storage & Stability |
Store at -20°C. Stable for up to 3 months from date of receipt at -20°C |
FAQ
What is ACTH (2-24) (human, bovine, rat) and how does it function in biological research?
ACTH
(2-24) represents a fragment of the Adrenocorticotropic hormone, which is a key component involved in
the stress response and is utilized primarily for research purposes across various species including
humans, bovines, and rats. This peptide sequence, C75H106N20O19S, provides insight into the role of ACTH
fragments in stimulating the adrenal cortex leading to the production of glucocorticoids. In research,
ACTH (2-24) enables scientists to specifically probe the peptide’s effect without triggering the entire
cascade that might arise with full-length ACTH. This fragment specifically lacks the first amino acids
that are involved in binding to the melanocortin receptor, which assists in lucidly observing the
exclusive functions related to adrenal stimulation. Researchers are particularly keen on this fragment
because it avoids some of the additional, broader physiological effects stimulated by full-length
ACTH.
Given its targeted application, ACTH (2-24) is crucial in experimental contexts where the
precise modulation of cortisol levels is required without activating melanocortin pathways that could
confound results. Especially in studies involving stress-response or adrenal function, ACTH (2-24) is
valuable as it circumvents non-specific pathways and focuses on the specific adrenal activation
functions. This is of particular importance in laboratory settings exploring endocrine responses and
adaptations to stress, immunological investigations, and metabolic studies. For researchers exploring
evolutionary biology, this hormone fragment provides a unique window into understanding differences
amongst species and how similar hormonal sequences can lead to varied metabolic processes. Ultimately,
ACTH (2-24) serves as an instrumental tool in both physiological research and the development of novel
treatments that might draw from its specific impacts on endocrine functions.
How does the
structure of ACTH (2-24) contribute to its stability and function in research applications?
The
structure of ACTH (2-24) is a result of careful peptide engineering, which serves to enhance both its
stability and precision in research contexts. Being a fragment of a larger peptide hormone, its
structural modification inherently lends itself to certain stability and functional attributes. This
sequence loses none of its functionality concerning the stimulation of the adrenal cortex but gains in
stability owing to the absence of the N-terminal amino acid sequence present in the complete hormone.
Excluding the first residues found in full-length ACTH translates to decreased enzymatic degradation,
making ACTH (2-24) relatively more stable during storage and when introduced into biological systems for
study.
The role of this truncated peptide segment in research is fundamentally tied to its
ability to evoke a consistent physiological response within the adrenal glands without triggering
additional melanocortin receptor pathways. This results in a cleaner interpretation of data without the
noise that could arise from reactions induced by the broader activity spectrum of the full ACTH hormone.
Additionally, this structural refinement allows greater versatility in research designs, from in vitro
assays aimed at unraveling the specifics of adrenal-related enzymatic reactions to in vivo models
crafted to study adrenal hyperactivity or hypoactivity.
Furthermore, the relatively simple
structure of ACTH (2-24) makes it a robust candidate in experimental studies. Its resilience at various
pH levels and alongside diverse biological matrices enhances its applicability across a wide array of
studies, allowing longer time frames for both exposure and observation without significant degradation.
This structural stability ensures reliable repeatability of experiments, which is a hallmark of credible
scientific investigation. Through its carefully curated sequence, ACTH (2-24) maximizes the capability
to dissect the hormonal regulation of adrenal function and offers a dependable platform for exploring
therapeutic potentials in disorders related to dysfunctional adrenal or stress responses.
What
are some of the challenges researchers face while working with ACTH (2-24) in laboratory
settings?
Working with peptide fragments like ACTH (2-24) in a research setting is not without
challenges, even considering its tailored suitability for specific experiments. One key challenge
researchers face is the need for specialized equipment and techniques to accurately quantify the
physiological changes this peptide induces. Unlike vibrant physiological responses to full-length
hormones, responses elicited by fragments require sensitive measurement techniques to detect subtle
changes in metabolic markers, hormone levels, or enzymatic activity. Such sensitivity often demands
high-quality, well-calibrated analytical instruments, which can be costly and require specialist
knowledge to operate effectively.
Moreover, ACTH (2-24), while structurally stable under certain
conditions, still requires precise environmental control. Factors such as temperature, pH, and exposure
to light can subtly affect its activity. Maintaining consistent experimental conditions is crucial, and
deviations may lead to inconsistent results. Storage and handling conditions, including preventing
contamination and degradation during experimentation, are also critical, often necessitating strict
adherence to protocols that may be more demanding than typical laboratory practices.
Another
significant challenge arises in replicating physiological in vivo conditions in vitro. Because ACTH
(2-24) primarily targets the adrenal function, successfully replicating the complexity of its in vivo
environment, with relevant receptors and downstream pathways, can be intricate. This often involves
culturing specific cell lines or developing animal models that can mimic the biological milieu
encountered within a living organism. Additionally, variability between species - as this peptide is
used in human, bovine, and rat models - can complicate the extrapolation of results. The physiological
and biochemical pathways differ across species, so interpreting results and applying them universally
requires a nuanced understanding of species-specific biology.
Interpretation of experimental
results involving ACTH (2-24) further demands expertise in endocrine and metabolic systems, as well as
proficiency in statistical analysis, to attribute biological effects correctly to the peptide. Given
these complexities, the challenge lies not only in conducting experiments but also in translating
laboratory findings into meaningful conclusions that can drive forward applications or therapeutic
interventions.
In what ways can ACTH (2-24) affect research outcomes related to stress and
endocrine disorders?
ACTH (2-24), in affording researchers the ability to study isolated elements
of the endocrine response to stress, can significantly enrich the exploration of stress and related
endocrine disorders. As a potent stimulator of the adrenal glands, ACTH (2-24) provides researchers with
a focused mechanism to modulate glucocorticoid production and, by extension, study its numerous
downstream effects linked to stress and metabolism. By isolating this pathway, researchers can decouple
the production of glucocorticoids from other hormonal functions that full-length ACTH would ordinarily
activate. This granularity is crucial for studies interested in understanding how specific endocrine
disruptions manifest in stress-related disorders.
For instance, experiments exploring the role of
glucocorticoids in stress can use ACTH (2-24) to precisely regulate these hormone levels, investigating
symptoms and systemic changes relating directly to elevated or repressed glucocorticoid activity. Such
focused research can delve into chronic stress implications, a major concern given its impact on mental
health and immune function. Understanding these connections can illuminate pathways linked to
depression, anxiety, and metabolic syndromes and how these may be treated or prevented through targeted
interventions.
Moreover, ACTH (2-24) can be instrumental in studying conditions such as Cushing’s
syndrome or Addison’s disease, where dysregulation in cortisol production is a hallmark. Researchers can
simulate conditions of elevated or diminished cortisol more precisely, which allows for a more detailed
mapping of symptoms and biochemical changes associated with these endocrine disorders. This specificity
fosters more nuanced research data, aiding the development of therapeutic strategies that can modulate
disease outcomes with increased precision.
It also opens a venue for exploring potential
therapeutic agents designed to act on the same pathways as ACTH (2-24). In doing so, it helps clarify
whether new treatments can selectively affect glucocorticoid production without the broader systemic
impacts associated with full-length hormone action, maximizing therapeutic efficacy while minimizing
side effects. Consequently, the application of this peptide in research can significantly elucidate the
complex webs between stress, endocrine regulation, and systemic diseases, guiding both fundamental
biological understanding and applied medical advancements.
How does ACTH (2-24) facilitate
comparative studies in different animal models?
In biological research, ACTH (2-24) is a valuable
tool for facilitating comparative studies across various species which include humans, bovine, and rats.
This peptide fragment allows researchers to explore the conserved and divergent elements of endocrine
systems, particularly concerning adrenal function and stress responses. The ability to work with the
same fragment across these different species provides a uniform platform, which is instrumental in
evaluating how similar peptides are leveraged in different animal models under physiological and
pathological conditions.
The use of ACTH (2-24) across different species enables comparative
studies that focus on conserved biochemical pathways while accounting for species-specific physiological
adaptations. For example, in human and rodent models, the peptide can be used to assess how adrenal
sensitivity and glucocorticoid production are regulated by relatively similar endocrine sequences. This
is particularly relevant for studies seeking to generalize findings related to stress physiology or
metabolic control from animal models to humans. Specific receptor interactions and downstream effects
can be meticulously compared, highlighting evolutionary adaptations and providing insights that could be
clinically relevant for treating human disorders.
Moreover, these comparative studies can
benchmark the potential variations in peptide metabolism and receptor affinity for ACTH (2-24) across
species. This can reveal differences in corticosteroid release patterns, half-life of the peptide, or
tissue-specific responses, contributing to a deeper understanding of both conserved hormonal mechanisms
and unique species characteristics. Such breadth in research establishes a foundation on which
cross-species hypotheses are built, particularly in pharmacological research, where translatability of
animal data to human outcomes is pivotal.
Finally, from a pharmacological standpoint, ACTH (2-24)
enables exploration of novel drug candidates aimed at modifying ACTH pathways. By using this peptide in
different models, research can validate the efficacy and safety of new pharmaceutical interventions,
ensuring robust preclinical data before advancing into human trials. This comparative framework thus
provides an inclusive approach to understanding endocrine processes across different organisms, with
implications for evolutionary biology, medicine, and therapeutic development.