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.