Synonym |
C-Peptide |
Species |
Porcine |
Protein Accession |
N/A |
Purity |
> 95% |
Endotoxin Level |
< 1.0 EU per 1 μg of protein |
Biological Activity |
N/A |
Expression System |
Escherichia coli |
Fusion Tag |
N/A |
Predicted Molecular Mass |
6964 Da |
Formulation |
Lyophilized from a 0.2 μm filtered solution of 20 mM Tris, 150 mM NaCl, pH 8.0 |
Reconstitution |
Centrifuge vial before opening. It is recommended to reconstitute the lyophilized product with
sterile water at a concentration of 0.1 mg/ml, which can be further diluted into other aqueous
solutions. |
Storage & Stability |
Store lyophilized protein at -20°C. Store reconstituted protein at 4°C for 2-7 days. For
long-term storage, aliquot and store at -20°C or -80°C. Avoid repeated freeze-thaw cycles. |
FAQ
What is Proinsulin C-Peptide (31-63) and how does it differ from other forms of
proinsulin?
Proinsulin C-Peptide (31-63) refers to a specific segment of proinsulin, which is a
precursor molecule to insulin. In mammals, proinsulin is synthesized in beta cells of the pancreas and
is made up of three primary segments: the A chain, B chain, and connecting peptide known as C-Peptide.
The C-Peptide is cleaved from proinsulin during the conversion to insulin. The numbers 31-63 represent
the specific amino acid sequence in the C-Peptide from porcine sources, which is important because amino
acid sequences can differ across species, slightly altering biological properties and
applications.
Proinsulin C-Peptide (31-63) is particularly valuable in research settings for its
role in the biosynthesis of insulin, serving as a marker to evaluate pancreatic function and beta-cell
activity. Unlike insulin, which directly regulates glucose metabolism, C-Peptide has been shown to have
its own physiological effects on various tissues, influencing renal, cardiovascular, and neural
functions. This adds a layer of complexity and potential therapeutic interest in
studies.
Historically, C-Peptide was considered inactive, merely a byproduct of insulin
production. However, recent research has recognized its physiological roles, some of which are still
being explored. The porcine form is significant in research due to the high degree of similarity to
human C-Peptide, though slight variations exist. These differences can be crucial when considering the
potential effects in translational research.
In contrast with other sections of proinsulin or
synthetic C-Peptide, the natural porcine variant involves considerations of bioavailability, specific
activity, and potential immune reactions. When utilizing such peptides in research or therapeutic
contexts, these factors are essential to account for, especially as they pertain to experimental design
and interpretation of results.
The choice to use Proinsulin C-Peptide (31-63) (porcine) in
research implies a focus on detailed interspecies comparisons, the exploration of biological activity of
sequences conserved across evolution, and the probing of potential therapeutic applications stemming
from C-Peptide’s ability to ameliorate dysfunctions in systems impacted by diabetes and other endocrine
disorders. Thus, the utilization of Proinsulin C-Peptide (31-63) goes far beyond simple biochemical
testing, positioning it as an investigational avenue into understanding and potentially exploiting its
functions for clinical benefit.
How can studies involving Proinsulin C-Peptide (31-63) improve
our understanding of diabetes management and treatment?
Studies involving Proinsulin C-Peptide
(31-63) can significantly enhance our understanding of diabetes management and treatment by elucidating
the role of this peptide in the pathophysiology and treatment of diabetes. Traditionally, medical
research emphasized insulin, often neglecting C-Peptide as a mere byproduct. However, increasing
evidence suggests that C-Peptide has potential biological functions that could contribute to diabetic
therapy and management.
First, one area where Proinsulin C-Peptide (31-63) may impact diabetes
management is its role in microvascular function. Patients with diabetes, particularly those with type 1
diabetes, often suffer from microvascular complications, such as diabetic neuropathy and nephropathy.
Studies have illustrated that C-Peptide might possess properties that aid in vascular repair and
neuroprotection, reducing or preventing the progression of these complications. In animal models, the
peptide showed a tendency to improve nerve conduction velocity and renal function, which are typically
impaired in diabetic conditions.
Secondly, the peptide's potential impact on metabolic control
cannot be overstated. There is burgeoning interest in how C-Peptide may contribute to glucose metabolism
autonomously or synergistically alongside insulin. By exploring Proinsulin C-Peptide (31-63) (porcine)
in research or clinical models, scientists can dissect the biochemical pathways that underpin its
effects and interactions with receptors within the human body.
By using advanced models to study
Proinsulin C-Peptide (31-63), researchers can provide insights into how this peptide might be used in
conjunction with insulin therapy for better overall control of blood glucose levels. Understanding
whether and how C-Peptide can mitigate some adverse effects of insulin therapy, such as hypoglycemia, is
of particular interest.
Furthermore, cross-species comparisons involving the porcine peptide help
in exploring the evolutionary conservation and function of this sequence across different organisms.
This knowledge assists in speculating about intrinsic evolutionary functions that may hint at broader
biological roles.
Lastly, C-Peptide has been linked to anti-inflammatory effects, potentially
mitigating chronic inflammation commonly seen in diabetic patients. Inflammation is a hallmark of many
diabetic complications, and thus, studies designed to evaluate the anti-inflammatory properties of
Proinsulin C-Peptide (31-63) might open new therapeutic avenues.
The overarching goal of this
research is to pioneer integrative strategies in diabetes management. Proinsulin C-Peptide (31-63) might
illuminate therapeutic opportunities that extend beyond glycemic control, enriching patient care
frameworks with interventions aimed at comprehensive management of diabetic complications, possibly
heralding a paradigm shift in our approach to diabetes therapeutics.
What are the potential
therapeutic applications of Proinsulin C-Peptide (31-63) in non-diabetic conditions?
The
potential therapeutic applications of Proinsulin C-Peptide (31-63) extend beyond diabetic treatments,
due to its multiple physiological activities discovered in recent research. While initially labeled as a
byproduct of insulin synthesis with no significant function, it has gained attention for its broader
implications in various systemic diseases and health conditions.
One potential application lies
in its role in renal health. Studies have indicated that Proinsulin C-Peptide (31-63) might aid in
ameliorating renal blood flow and glomerular filtration rates. This could have implications for patients
with kidney diseases characterized by microvascular dysfunctions beyond diabetes, potentially
representing a therapeutic pathway for general renal protection or enhancement.
In cardiovascular
health, C-Peptide has garnered interest due to observed improvements in endothelial function and
potential benefits in ischemic conditions. When administered in experimental settings, it has shown
capacity to enhance myocardial blood flow and protect against ischemia-reperfusion injury, which is
relevant in heart disease management. If validated in broader patient cohorts, these attributes might be
leveraged in therapies designed to improve outcomes in cardiovascular diseases, especially those
featuring compromised blood supply and vascular health.
The peptide’s influence on neural tissue
also opens interesting therapeutic avenues outside the realm of diabetes. Observations of neurotrophic
effects raise the possibility of using Proinsulin C-Peptide (31-63) in neurodegenerative diseases or as
a supportive treatment in traumatic nerve injury. Animal studies have demonstrated improvements in
sensory and motor nerve functions, suggesting a possible role in enhancing neuronal recovery and
function.
Additionally, the anti-inflammatory properties of C-Peptide could be applied in
managing chronic inflammatory disorders. Given the broad impact of inflammation across various diseases,
this peptide might offer a novel approach to mitigate chronic inflammatory processes, potentially
benefiting conditions like arthritis or inflammatory bowel diseases.
C-Peptide's interaction with
nitrogen monoxide and subsequent reduction of oxidative stress gives it a protective edge in conditions
characterized by oxidative damage. This could contribute to therapeutic protocols for diseases where
oxidative stress is a core component, thereby increasing the resilience of tissues against oxidative
damage.
It is worth emphasizing that while these potential applications are promising, they still
demand extensive research to establish safety, efficacy, and specific clinical protocols. Careful
studies, including clinical trials, are needed to translate these potential benefits into viable medical
interventions.
Nevertheless, the evolving understanding of Proinsulin C-Peptide (31-63) enriches
the landscape of potential treatment options extending beyond its traditional context. This not only
underscores the biological significance of previously underestimated components like C-Peptide but also
invites a reassessment of current views on peptide functions within human physiology.
How does
Proinsulin C-Peptide (31-63) contribute to the research of metabolic pathways?
Proinsulin
C-Peptide (31-63) contributes significantly to the research of metabolic pathways by offering insights
into alternative mechanisms of cellular activity beyond the well-characterized actions of insulin.
Although initially overlooked, C-Peptide's roles in various physiological processes have opened avenues
for exploring less understood metabolic pathways, providing crucial biochemical insights.
Much of
the interest in Proinsulin C-Peptide (31-63) stems from its interaction with cellular receptors and
subsequent intracellular signaling cascades. C-Peptide binds to specific cell surface receptors,
initiating cascades similar in some respects to insulin but with distinct differences that warrant
investigation. These pathways often involve mitogen-activated protein kinases (MAPKs) and
phosphatidylinositol 3-kinase (PI3K), both of which are critical components of cellular growth and
survival signaling networks.
Through modulation of these pathways, C-Peptide may exert effects on
glucose uptake, cytoskeletal rearrangement, and gene expression, thus highlighting its non-redundant
role in metabolic regulation. Understanding these effects can not only reveal the intricacies of
metabolic regulation but also identify potential targets for drug development.
Furthermore,
research on Proinsulin C-Peptide (31-63) has contributed to the understanding of its antioxidative
properties through pathways that generate nitric oxide. Nitric oxide plays a critical role in vascular
function and cytoprotection. Analysis of how C-Peptide mediates these pathways helps illuminate broader
metabolic events tied to oxidative stress responses and could inform therapeutic strategies against
disorders related to oxidative stress.
Particularly fascinating is Proinsulin C-Peptide’s
potential role in metabolic disorders outside of diabetes, like metabolic syndrome, obesity, and even
some forms of cancer, where metabolism is profoundly altered. Exploring these roles could uncover how
the peptide influences systemic metabolic balance and its interaction with insulin and other metabolic
hormones.
Ultimately, by providing a detailed map of how Proinsulin C-Peptide (31-63) impacts
metabolic signaling, researchers can better understand disease mechanisms where these processes are
disrupted. Each insight gained adds to a comprehensive model of cellular metabolism, offering prospects
for engineering metabolic interventions not only in diabetes but also in other metabolic
disorders.
What are the implications of using Proinsulin C-Peptide (31-63) in clinical
research?
The implications of using Proinsulin C-Peptide (31-63) in clinical research are
far-reaching, as this peptide is increasingly being recognized for its potential therapeutic roles in
diverse physiological contexts. Understanding its implications can be dissected into several key areas:
disease treatment, diagnostic applications, and fundamental biochemical research.
Firstly,
considering the physiological roles that C-Peptide plays in the body, clinical research could elucidate
potential therapeutic applications. There have been investigations into its efficacy in ameliorating
conditions typically arising in diabetic patients, like neuropathy and nephropathy. Clinical trials
focusing on safety, dosage, and long-term effects could potentially lead to broader acceptance of
C-Peptide as an adjunct therapy in managing chronic diabetic complications. Demonstrating clinical
benefits in contexts such as improved nerve function or kidney protection could revolutionize the
standard of care for diabetic patients, expanding beyond traditional insulin
treatments.
Additionally, C-Peptide’s documented anti-inflammatory properties should be noted.
Clinical research can confirm whether these can be leveraged in managing autoimmune or inflammatory
diseases. Pursuing such avenues may open an array of interventional strategies in conditions where
inflammation plays a central role, such as rheumatoid arthritis or irritable bowel syndrome.
From
a diagnostic perspective, the measurement of C-Peptide levels helps in evaluating residual beta-cell
function in diabetic patients, a factor crucial for both diagnosis and treatment adjustment. Utilizing
Proinsulin C-Peptide (31-63) in research can enhance the sensitivity and accuracy of assays designed for
clinical diagnostics, potentially leading to more personalized treatment strategies based on individual
beta-cell activity.
The research implications extend to exploring C-Peptide’s mechanisms of
action at the cellular and molecular levels. Clinical studies that translate bench findings can confirm
and possibly expand on the mechanistic insights gained from preclinical research. Unveiling how
C-Peptide interacts with cellular structures and receptors in humans as opposed to model organisms is
crucial for designing therapeutics and understanding different human pathophysiologies.
Finally,
exploring Proinsulin C-Peptide (31-63) in clinical research underlines the importance of considering
endogenous peptides beyond their primary assumed roles, urging a more integrated biological
understanding. The outcomes of such research could transform medical paradigms regarding peptide
functions in health and disease, pushing boundaries in metabolic research and therapy development in
ways that were hitherto unforeseen.