Synonym |
Glucagon 19-29 |
Species |
Human, rat, porcine |
Protein Accession |
NA |
Purity |
≥ 95% |
Endotoxin Level |
< 0.1 EU per μg |
Biological Activity |
NA |
Expression System |
NA |
Fusion Tag |
NA |
Predicted Molecular Mass |
NA |
Formulation |
Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA with BSA as a carrier
protein |
Reconstitution |
Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.1-1.0 mg/ml.
Do not vortex. |
Storage & Stability |
Store lyophilized product at -20°C. Reconstituted product is stable for 3 months at -20°C. |
FAQ
What exactly is Glucagon (19-29) (human, rat, porcine), Minigluc, and how does it function
physiologically?
Glucagon (19-29), commonly known as Minigluc, is a segment of the natural
glucagon peptide hormone. Glucagon is produced by alpha cells in the pancreas and plays a crucial role
in blood glucose homeostasis by promoting the conversion of stored glycogen to glucose, a process known
as glycogenolysis, primarily occurring in the liver. This peptide segment, spanning amino acids 19 to
29, has been studied to understand its function and therapeutic potential. The sequence similarity
across species such as human, rat, and porcine indicates evolutionary conservation and functional
importance, suggesting that this peptide region is vital to its physiological role. Minigluc is
particularly interesting in research focused on metabolic disorders and is used as a tool to dissect
specific glucagon interactions due to its smaller size compared to the full glucagon molecule, which is
29 amino acids long. While the entire glucagon molecule facilitates its primary function of increasing
blood glucose levels during fasting states or hypoglycemia, Minigluc specifically provides insights into
receptor binding and activity, and structure-function relationships of the glucagon molecule.
Researchers exploit Minigluc to study the conformational changes required for optimal receptor
interaction, aiding in the design of glucagon analogs that could improve therapeutic outcomes in
conditions like diabetes and obesity. Furthermore, unraveling Minigluc's role gives insights into how
specific segments of hormones interact with their receptors and transport mechanisms within the body, an
understanding that opens doors to targeted design of more selective receptor agonists or antagonists.
This research is fundamental for developing advanced treatments that could modulate glucagon's effects
precisely, potentially offering a more granular control of metabolic diseases, while also minimizing
side effects that arise from generalized, non-specific hormone modulation. Thus, Glucagon (19-29) plays
a critical foundational role in scientific studies that seek to innovate therapeutic strategies for
better health outcomes.
How does Glucagon (19-29), Minigluc, serve in research, particularly
concerning metabolic disorders?
Glucagon (19-29), or Minigluc, is leveraged in research as a
pivotal tool to delve into the intricacies of metabolic disorders. It serves as a critical fragment of
the glucagon hormone allowing researchers to dissect and better understand the physiological functions
and pathophysiological impacts of glucagon signaling pathways. Its use in research primarily focuses on
its contribution to the regulation of blood glucose levels, which is fundamental in managing disorders
like diabetes mellitus. In understanding how glucagon functions at a molecular level, Minigluc helps
illuminate pathways regulating glucose production from the liver, thereby offering a clearer picture of
hyperglycemia and its development. This is particularly important because hyperglycemia is a defining
feature of both type 1 and type 2 diabetes. In addition, Minigluc is instrumental in exploring
deviations in glucagon action, which may lead to new therapeutic targets. For instance, understanding
how this peptide fragment binds to glucagon receptors enables researchers to design glucagon receptor
agonists or antagonists that could either enhance or inhibit glucagon action, opening potential
therapeutic avenues. Minigluc also assists in the structural alteration and development of analogs with
prolonged activity or increased receptor selectivity, which are thought to potentially usher in a new
era of diabetic treatments. By providing a detailed understanding of glucagon's mechanism of action,
metabolic processes like gluconeogenesis and glycogenolysis can be more comprehensively modulated,
aiding in precise therapeutic modulation to alleviate glucose imbalances. Furthermore, the study of
Minigluc in animal models and its synthetic analogs enables a platform for testing potential treatments
in vivo before commencing human trials, thus fast-tracking the validation of new therapeutic compounds.
As a reduced version of glucagon, Minigluc simplifies these studies due to its focused biological
actions, making it indispensable in the detailed exploration needed for innovative metabolic disorder
treatments.
What are the potential therapeutic applications of Minigluc in the medical
field?
The potential therapeutic applications of Minigluc, a fragment of the glucagon peptide,
are gaining attention due to its promising role in modulating metabolic functions and addressing
relevant medical conditions. In the sphere of diabetes management, Minigluc stands out as a critical
component in developing new treatments aimed at controlling hyperglycemia. By understanding its
interaction with glucagon receptors, researchers can formulate receptor-specific treatments capable of
modulating gluconeogenesis and glycogenolysis, providing more precise blood glucose regulation. This
specificity is crucial in minimizing the side effects normally associated with broader glucagon
interventions, such as the excess release of glucose into the bloodstream, which can exacerbate
hyperglycemia rather than mitigate it. Furthermore, Minigluc's role in glucagon receptor signaling makes
it a suitable candidate for exploring therapeutic applications in metabolic syndrome, a cluster of
conditions that increase heart disease, stroke, and type 2 diabetes risk. Understanding and manipulating
Minigluc's receptor interactions could lead to breakthroughs in targeting these conditions, potentially
regulating lipid metabolism and reducing insulin resistance. Beyond its application in glucose
metabolism, Minigluc's ability to influence energy balance and fat metabolism also opens doors to
obesity treatment strategies. By modulating hormonal pathways involved in appetite and energy storage,
therapies incorporating Minigluc derivatives could facilitate weight management, which is pivotal in
combating obesity-related comorbidities. Another promising avenue is the potential role of Minigluc in
treating heart failure. Glucagon's positive inotropic effects on heart muscle contraction, primarily
mediated through cyclic adenosine monophosphate (cAMP) release, may be fine-tuned using Minigluc to
avoid negative cardiovascular impact while harnessing beneficial heart stimulation. As scientists
continue to unravel the signaling pathways and receptor interactions involving Minigluc, this peptide
fragment stands at the forefront of developing innovative, specialized treatments that address core
issues in metabolic dysfunction and broader systemic disorders where glucagon action plays a crucial
role.
Why is Minigluc considered advantageous in peptide-based research compared to other
glucagon fragments?
Minigluc holds a unique advantageous position in peptide-based research
primarily due to its size and functional characteristics. By focusing on the Glucagon (19-29) sequence,
researchers can examine a smaller, yet functionally significant segment of the full glucagon peptide.
This reduction in size translates to a simplification that affords a clearer understanding of specific
peptide-receptor interactions and activity, without the additional complexities introduced by
non-essential sequences in the full-length peptide. When it comes to receptor binding studies, Minigluc
is invaluable as it allows for the resolution of how particular sequences within glucagon contribute to
receptor affinity and signaling, providing a detailed perspective crucial for drug development. The
conservation of this sequence across human, rat, and porcine species further emphasizes its foundational
role in glucagon's action, making it suitable for cross-species studies, which are vital in preliminary
research stages before human clinical trials. Additionally, studying Minigluc facilitates the precise
mapping of functional domains and understanding which motifs in glucagon are responsible for initiating
specific cellular responses. This knowledge is instrumental when designing selective glucagon receptor
agonists or antagonists, particularly in achieving desirable therapeutic outcomes with minimized
off-target effects. Moreover, due to its short sequence, Minigluc is more amenable to synthetic
modifications, enabling researchers to design analogs with altered functionalities, improved stability,
or enhanced receptor specificity. This flexibility ultimately accelerates the development cycle by
providing a robust platform for testing a variety of modifications in silico, in vitro, and in vivo.
Crucially, the use of Minigluc allows researchers to better connect structure and function at a
fundamental level, driving innovation in peptide-based therapeutics aimed at addressing metabolic
diseases and disorders reliant on glucagon signaling. Therefore, the directed focus on this specific
glucagon segment harnesses a balance of simplicity, specificity, and versatility, which collectively
underscores Minigluc's advantageous role in peptide research and therapeutic development.
How
does the conservation of the Glucagon (19-29) sequence across multiple species influence research and
medical applications?
The conservation of the Glucagon (19-29) sequence across species like
human, rat, and porcine significantly influences research and medical applications by providing a
foundation of evolutionary insight and cross-species relevance crucial for translational medicine. This
conservation implies that the sequence plays a critical role in glucagon's biological function, one that
has been preserved through evolution, highlighting its fundamental importance in physiological processes
such as metabolism and homeostasis. For researchers, this evolutionary conservation offers a robust
model for studying glucagon's interaction with its receptors and the subsequent signaling pathways. It
increases the reliability of animal models used in preclinical studies, thus enhancing the predictive
value of such studies when they are transferred to human contexts. The cross-species conservation allows
insights gleaned from research conducted on animals, such as rats and pigs, to be more readily
applicable to human physiology, thereby optimizing the development workflow for potential therapeutic
agents. The insights gained also provide crucial information about receptor selective binding, allowing
researchers to develop therapeutics with enhanced specificity, reducing potential side effects caused by
non-specific glucagon activity. In medical applications, this conserved sequence facilitates the design
of pan-species therapeutic agents, which can benefit both veterinary and human medicine, ensuring that
drugs developed can have wide-ranging impacts. The wide evolutionary landscape allows pharmaceutical
development to employ bioinformatics and molecular biology approaches to predict and assess drug
interactions across different biological systems. Consequently, this conservation acts as a pivotal
nexus point linking basic research with applied therapeutic development, enabling a streamlined and more
accurate path from bench to bedside. In a broader sense, it enforces the paradigm that understanding
conserved sequences and their biological roles can spur innovation, driving new discoveries that meet
the demands and challenges posed by various metabolic disorders.