Taiy Chemical
GRP (18-27) (human, Porcine, Canine), Neuromedin
Synonym GRP (18-27)
Species Human, Porcine, Canine
Protein Accession P07492
Purity > 95%
Endotoxin Level < 1.0 EU per 1 μg of protein
Biological Activity Stimulates the release of growth hormone in rats
Expression System E. coli
Fusion Tag None
Predicted Molecular Mass 1231 Da
Formulation Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA
Reconstitution Reconstitute in water to a concentration of 0.1-1.0 mg/ml
Storage & Stability Store lyophilized protein at -20°C. Aliquot and store at -20°C for long-term stability. Avoid repeated freeze-thaw cycles.
FAQ
What is GRP (18-27) and what are its applications in research?

Gastrin-Releasing Peptide (GRP) is a peptide that plays a crucial role in various physiological processes, including the regulation of gastric acid secretion and modulation of neuronal communication. GRP (18-27) refers to a specific segment of this peptide, which has been studied for its potential roles and applications in medical research. This peptide can be derived from human, porcine, and canine sources, making it versatile for comparative studies across species. Researchers have utilized GRP (18-27) to explore its effects on cancer cell proliferation, particularly in gastrointestinal, lung, and prostate cancer. By binding to the GRP receptor, it can activate multiple intracellular pathways that influence cell growth and differentiation. In neurobiology, GRP (18-27) is investigated for its potential neuroprotective effects, impact on memory and cognition, and its roles in behavior and stress responses. Animal studies often employ porcine and canine variants to understand the peptide's mechanisms in species that have physiological similarities to humans. This flexibility enhances its utility in preclinical models of disease. Researchers interested in understanding metabolic regulation and digestive processes also study GRP (18-27), as it may influence the secretion of other hormones and enzymes involved in digestion. Overall, GRP (18-27) offers a rich area of study for exploring mechanisms of disease, therapeutic targets, and the evolution of peptide function across different organisms.

How does the GRP (18-27) sequence differ between human, porcine, and canine origins, and why is this important?

The GRP (18-27) sequence varies slightly between humans, pigs (porcine), and dogs (canine), which reflects evolutionary adaptations that may impact its binding affinity to the GRP receptor and the resulting physiological effects. These differences can be subtle, as the peptide's core function remains largely conserved across these species. For researchers, these variations hold significant importance, particularly in cross-species study contexts. In human-based studies, using the human version of GRP (18-27) ensures that experimental outcomes are directly relevant to human physiology, minimizing translational discrepancies when advancing from preclinical trials to human applications. Porcine GRP is utilized frequently due to pigs being a viable model for human digestion and metabolic studies, owing to similarities in their gastrointestinal morphology and function. The canine version helps in veterinary studies and comparative biology, as dogs exhibit certain physiological and behavioral parallels to humans. Cross-species examination can reveal how small sequence variations result in differences in receptor interaction, peptide stability, and downstream signaling. Such findings can uncover evolutionary insights and inform the development of therapeutics. In the context of pharmaceutical development, understanding these differences allows for the formulation of species-specific drugs or enhances drug design to maximize effectiveness across multiple species. Thus, studying these sequence variations and their functional repercussions is not only crucial for unraveling biological mysteries but also in optimizing translational and therapeutic research.

What are the molecular functions of Neuromedin in relation to GRP (18-27)?

Neuromedin is a group of neuropeptides with broad physiological functions, one of which closely relates to the activity of Gastrin-Releasing Peptide (GRP). Like GRP, Neuromedin can influence neural communication, digestive processes, and hormone release. The relationship between Neuromedin and GRP (18-27) is particularly notable in their overlapping receptor activity. Both peptides can activate similar pathways by interacting with neuromedin B receptors and GRP receptors, indicating a shared or synergistic role in modulating physiological responses. Neuromedin can facilitate neurotransmitter release and influence synaptic plasticity, key processes in learning and memory. When co-studied with GRP (18-27), researchers can investigate potential combinatory effects on neural circuits, providing insights into how these peptides may jointly regulate complex behaviors such as stress response and emotion regulation. In digestion, Neuromedin acts similarly to GRP by promoting gastric and pancreatic secretions. This dual action suggests possible interactions where Neuromedin and GRP (18-27) may regulate appetite and enzyme secretion in a complementary manner. Understanding these interactions can provide insights into developing anti-obesity therapies and treatments for digestive disorders. Given the multiple roles that even a single related peptide like GRP (18-27) can affect, Neuromedin’s overlapping functions further broaden the spectrum of possible physiological pathways and therapeutic targets. Therefore, studying Neuromedin in conjunction with GRP (18-27) can expand our understanding of these peptides' roles in health and disease, leading to more effective therapeutic strategies.

Can GRP (18-27) be used in the study of metabolic disorders?

GRP (18-27) holds considerable promise in studying metabolic disorders due to its regulatory role in digestive processes and metabolic signaling. By acting on the GRP receptor, GRP (18-27) influences the secretion of digestive hormones and enzymes, thereby playing a potential role in energy balance, appetite regulation, and nutrient absorption—key factors implicated in metabolic diseases such as obesity, diabetes, and metabolic syndrome. Research into GRP (18-27) can elucidate how modulation of gastric acid secretion and pancreatic enzyme activity affects nutrient metabolism. This understanding is crucial, given that dysregulation in these processes is a hallmark of many metabolic disorders. Studies have shown that GRP and its peptides might influence insulin secretion and action, key elements in the pathophysiology of diabetes. By examining GRP (18-27) in experimental models of metabolic disorders, researchers can gain insights into its potential to affect glucose homeostasis and insulin sensitivity. Furthermore, its role in appetite regulation suggests possibilities for exploring GRP (18-27) as a target for anti-obesity drugs. For instance, by affecting the signaling pathways that mediate satiety and hunger, GRP (18-27) could be leveraged to develop treatments that help regulate body weight. Additionally, understanding how this peptide interfaces with other hormonal and neural pathways in different species—human, porcine, and canine—can aid in the design of cross-species therapies aimed at metabolic diseases. The peptide's role in influencing neurotransmitter systems also implicates it in the broader metabolic regulation seen in conditions like anorexia and cachexia. Ultimately, research into GRP (18-27) and its interactions with metabolic pathways can potentially pave the way for novel therapeutic applications that address the growing global issue of metabolic disorders.

How might GRP (18-27) affect cancer progression and what does this mean for therapeutic development?

The Gastrin-Releasing Peptide (GRP) and specifically the sequence GRP (18-27) have been the focus of research related to cancer progression due to their role in cellular proliferation, differentiation, and survival. GRP binding to its receptor can activate several intracellular signaling pathways, including MAPK/ERK and PI3K/AKT, which are critical for cell growth and survival. These pathways are frequently dysregulated in cancer, leading to increased tumor growth and resistance to apoptosis. GRP (18-27) has been shown to have proliferative effects on cancer cells, particularly in cancers of the gastrointestinal tract, lung, and prostate. Its involvement in neuroendocrine stimulation suggests a potential autocrine or paracrine mechanism where tumor cells produce GRP to promote their proliferation and survival. This makes GRP (18-27) a potential target for cancer therapeutics. By understanding these mechanisms, researchers can develop drugs that block GRP receptors or inhibit the peptide's production, thus impeding tumor growth. Another avenue of research is the use of GRP (18-27) analogs to explore receptor antagonism. These analogs could act as decoys to block the receptor and interrupt the growth-promoting signals in cancer cells. Additionally, as GRP receptors are often overexpressed in certain cancers, GRP (18-27) can serve as a targeting ligand in the development of radiolabeled compounds or GRP-linked chemotherapeutics that deliver toxic agents specifically to tumor cells, minimizing damage to healthy tissue. These strategies highlight the diagnostic as well as the therapeutic potential of GRP (18-27) in oncology. Continued research in this area can offer innovative cancer treatments that exploit the unique mechanisms of peptide-receptor interactions and signaling pathways that GRP (18-27) influences. Therefore, GRP (18-27) not only helps us understand cancer biology better but also serves as a potent focal point for developing targeted cancer therapies.

What are the challenges and considerations in using GRP (18-27) in preclinical and clinical studies?

The use of GRP (18-27) in preclinical and clinical studies presents several challenges that require careful consideration. One of the primary challenges is the inherent variability in peptide synthesis and stability. As a biologically active peptide, GRP (18-27) must be synthesized with high purity and precision to ensure reliable results. Moreover, peptides can be susceptible to degradation by proteases in biological systems, which can complicate in vivo studies. Therefore, research must incorporate stabilization strategies, such as peptide modifications or delivery systems that protect the peptide from rapid degradation. The cross-species differences in GRP (18-27) between human, porcine, and canine origins can pose another challenge, as these differences may affect the peptide's interaction with receptors and thus its biological effects. For translational studies, it's essential to choose the appropriate animal models and consider how species variations may influence outcomes. Moreover, GRP receptors may be expressed differently in various tissues, requiring precise targeting to achieve the desired therapeutic effect without off-target consequences. There's also the potential for variable expression levels of GRP receptors in pathological versus normal tissues, affecting both efficacy and safety profiles of GRP-targeted therapies. Another consideration is the side effect profile of therapies targeting GRP (18-27), particularly given its involvement in numerous physiological processes like digestion and nervous system function. Preclinical safety assessments must thoroughly evaluate potential adverse effects. In clinical studies, regulatory approvals necessitate comprehensive data on pharmacokinetics and pharmacodynamics. Ethical considerations, especially in human studies, require a delicate balance between potential benefits and risks. Despite these challenges, GRP (18-27) research continues to advance, with technological improvements in peptide chemistry and drug delivery systems furthering our capacity to overcome these obstacles. Addressing these considerations ensures the successful integration of GRP (18-27) research from bench to bedside, enhancing the therapeutic landscape for conditions impacted by GRP-related pathways.
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