Taiy Chemical
β-MSH (porcine), β-Lipotropin (41-58) (porcine)
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.
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