Synonym |
β-MSH (porcine), β-LPH (41-58) (porcine) |
Species |
Porcine |
Protein Accession |
P05774 |
Purity |
> 95% |
Endotoxin Level |
< 1 EU/μg |
Biological Activity |
Not determined |
Expression System |
E. coli |
Fusion Tag |
None |
Predicted Molecular Mass |
2.3 kDa |
Formulation |
Lyophilized from a 0.2 μm filtered solution of 20 mM Tris, 50 mM NaCl, pH 7.5 |
Reconstitution |
Centrifuge vial before opening. Reconstitute in sterile ddH2O 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 β-MSH (porcine) and β-Lipotropin (41-58) (porcine), and how are they different from other
peptides?
β-MSH (porcine) and β-Lipotropin (41-58) (porcine) are bioactive peptides derived from
pig (porcine) sources and are part of the larger proopiomelanocortin (POMC) molecule. They are of
significant interest in research due to their roles in the physiological processes, which include the
regulation of energy balance, pigmentation, and lipid metabolism. β-MSH, or beta-melanocyte-stimulating
hormone, is a specific peptide known to influence pigmentation. It binds to melanocortin receptors to
induce melanin production in the skin's melanocytes. This function is crucial in studying skin color
changes and potential therapeutic applications for pigmentary disorders. β-Lipotropin, on the other
hand, is a larger peptide that contains within its sequence β-MSH, and spans positions 41 to 58 in the
propeptide chain. β-Lipotropin has been known to play a role in fat metabolism; it influences lipolysis
and the release of fatty acids into the bloodstream. This makes it especially pertinent for research
related to obesity and metabolic syndromes.
What sets β-MSH (porcine) and β-Lipotropin (41-58)
apart from other peptides is their specificity and origin. Derived from porcine sources, these peptides
have specific structural characteristics that can influence how they bind to and interact with
receptors, potentially making them more effective or preferable for certain types of research compared
to non-porcine peptides. Their unique composition can allow researchers to explore specific pathways
related to pigmentation or metabolism more effectively within biological models. Additionally, their
study offers insights into comparative physiology between human and animal models, which is beneficial
for translational research that aims to develop therapeutic interventions in humans. As part of the POMC
family, these peptides also offer a connection between endocrinology and other bodily systems, such as
the immunological or neuroendocrine pathways, enriching their potential applications across a broad
spectrum of research areas.
How do β-MSH (porcine) and β-Lipotropin (41-58) (porcine) influence
skin pigmentation?
β-MSH (porcine) is directly involved in the regulation of skin pigmentation
through its action on melanocytes in the skin. Melanocytes are specialized cells that produce melanin,
the pigment responsible for skin color. β-MSH achieves this by binding to melanocortin 1 receptors
(MC1R) on the surface of melanocytes. When β-MSH binds to these receptors, it triggers a series of
cellular events that lead to the increased production and distribution of melanin pigment within the
skin. This cascade involves the activation of adenylate cyclase, an increase in cyclic AMP levels, and
subsequent activation of the enzyme tyrosinase, which is essential for melanin synthesis. These
processes contribute towards darker pigmentation in human and animal models. This discovery of β-MSH's
role in pigmentation has significant implications for understanding pigmentary disorders and developing
treatments for conditions like vitiligo, where skin depigmentation occurs.
β-Lipotropin (41-58)
also plays a part in pigment production indirectly. Although its primary functions are related to
metabolism and the mobilization of lipids, its biochemical structure possesses the β-MSH sequence,
allowing it to potentially engage in similar interactions with melanocortin receptors. Research into
β-Lipotropin and its relation to skin pigmentation could provide insights into the systemic regulation
of pigmentation, lending a broader perspective on how skin color adaptation can be influenced by
metabolic changes or health status. Understanding this dual functionality of β-MSH and β-Lipotropin has
the potential to bridge gaps in our current knowledge of how systemic conditions or metabolic imbalances
could influence skin color over time. Furthermore, by comprehending this interaction, the development of
targeted therapies that control pigmentation, either by augmenting or reducing melanin production,
becomes a feasible pursuit in dermatological research.
Can β-MSH (porcine) and β-Lipotropin
(41-58) (porcine) aid in obesity research?
Indeed, β-MSH (porcine) and β-Lipotropin (41-58) are
crucial in the context of obesity research, particularly because of their roles in energy homeostasis
and lipid metabolism. One of the significant functions of β-MSH is as a regulator of appetite and energy
expenditure. It exercises these effects by acting on the melanocortin 4 receptor (MC4R) in the brain,
particularly within the hypothalamus, a region responsible for regulating hunger and satiety. Activation
of MC4R by β-MSH leads to decreased appetite and increased energy expenditure, thus maintaining energy
balance. This makes β-MSH a peptide of interest for studying mechanisms underlying appetite regulation
and its potential therapeutic implications for tackling obesity and related metabolic
disorders.
β-Lipotropin, known to influence the release and mobilization of fatty acids, further
complements this research area. As the larger precursor to β-MSH and other opioid peptides, β-Lipotropin
is involved in lipolysis, the breakdown of lipids and the release of fatty acids from adipose tissue.
This function is vital for energy balance, especially in states of increased energy demand or caloric
restriction. The potential modulation of β-Lipotropin levels or activity may elucidate pathways by which
we can influence adipose tissue function, providing a viable research path for obesity treatment. These
peptides are not merely isolated agents; their actions are intertwined with various hormonal and
regulatory mechanisms, making them ideal candidates for examining the complex etiology of
obesity.
In terms of therapeutic use, research into β-MSH and β-Lipotropin could advance our
understanding of peptide-based treatments for obesity, promoting the development of drugs that can
modulate their activities or mimic their actions. The ability to fine-tune these pathways opens
possibilities for interventions that help manage or reduce obesity-related risks. Given the increasing
global concern over obesity and its health implications, understanding how these naturally occurring
peptides can be leveraged offers a promising avenue that can lead to more natural and less invasive
treatments for weight management.
How do β-MSH (porcine) and β-Lipotropin (41-58) interact with
the body’s stress response mechanisms?
β-MSH (porcine) and β-Lipotropin (41-58) are part of a
larger family of peptides derived from proopiomelanocortin (POMC), which are intimately connected to the
body’s stress response mechanisms. The POMC gene encodes several peptides, including adrenocorticotropic
hormone (ACTH), essential for stimulating the adrenal cortex to produce glucocorticoids, such as
cortisol. Cortisol is a primary hormone released during stress, contributing to the body's ability to
manage stress by modulating various physiological processes, including immune response, energy
metabolism, and fluid balance.
While β-MSH primarily stimulates melanin production, it also has
secondary roles linked to the stress response due to its precursor relationship with ACTH. This
relationship indicates a shared pathway that can influence stress management indirectly through systemic
physiological alterations. The interaction of β-MSH with the central nervous system via melanocortin
receptors also suggests its potential role in modulating emotional and stress responses, albeit to a
lesser extent compared to its direct effects on pigmentation or appetite
regulation.
β-Lipotropin's involvement in stress response mechanisms is reflected in its ability
to release endorphins and other opioid peptides. Endorphins are known for their ability to modulate pain
perception and induce feelings of well-being, commonly termed as the "runner's high" phenomenon. This
modulation of opioid pathways can impact the body's stress levels by promoting relaxation and reducing
perceived stress or pain. Additionally, as β-Lipotropin influences lipolysis, it ensures adequate energy
supply during periods when the body encounters stressors, thus aiding in maintaining homeostasis. The
cross-functional nature of these peptides highlights the interconnectedness of oxidative stress
responses, energy metabolism, and neuroendocrine functions within the body.
By engaging with
these pathways, research into β-MSH and β-Lipotropin can provide an understanding of how stress
influences various bodily systems and lead to therapeutic strategies aiming at relieving stress-related
dysfunctions. This intersection of stress response and metabolic regulation through melanocortin
signaling offers insights that can lead to novel methodologies aiming at improving resilience to stress
and enhancing general well-being.
Are there therapeutic applications for β-MSH (porcine) and
β-Lipotropin (41-58) (porcine)?
The potential therapeutic applications for β-MSH (porcine) and
β-Lipotropin (41-58) (porcine) are diverse, given their involvement in vital physiological processes.
β-MSH's role in pigmentation opens possibilities for its use in treating pigmentary disorders. Diseases
like vitiligo or melasma, characterized by skin depigmentation or hyperpigmentation, could benefit from
therapies that modulate melanocyte activity and melanin production. By understanding and manipulating
the melanocortin receptors, particularly MC1R, researchers could develop therapies that promote
repigmentation in conditions where melanin levels are lacking or provide regulation in states of
excessive pigmentation.
Additionally, β-MSH's involvement in appetite and energy regulation marks
it as a suitable candidate for addressing obesity and metabolic disorders. The knowledge of its action
through MC4R in the central nervous system indicates the potential for developing appetite suppressants
that work by enhancing the peptide's natural appetite-reducing signals. This insight could lead to safer
weight management therapies with fewer side effects compared to traditional pharmacological
interventions, considering their basis in regulatory biochemical pathways known to the body.
For
β-Lipotropin, therapeutic applications may revolve around its ability to influence lipid metabolism and
energy homeostasis. Its action in promoting lipolysis means that it could be leveraged to enhance fat
metabolism in metabolic conditions characterized by excessive fat accumulation, such as nonalcoholic
fatty liver disease or obesity. Furthermore, through the generation of endorphins and other opioid
peptides, β-Lipotropin's connection to pain and stress modulation could open avenues for its role in
managing chronic pain or mood disorders.
The scope for therapeutic application extends as
research continues to unlock intricate details about how these peptides interact with bodily systems.
Through peptide therapeutics, there exists the potential to craft personalized medicine protocols that
consider individual differences in peptide expression or receptor profiles. As biotech advances expand
peptide delivery methods and receptor-targeting precision, the integration of β-MSH and β-Lipotropin
into therapeutic regimens could see increase, highlighting their utility across dermatological,
metabolic, and neuroendocrine health domains.