Synonym |
parathyroid hormone (44-68) (human) |
Species |
Human |
Protein Accession |
P01270 |
Purity |
> 95% |
Endotoxin Level |
< 1.0 EU per µg |
Biological Activity |
Fully biologically active when compared to standard |
Expression System |
E. coli |
Fusion Tag |
None |
Predicted Molecular Mass |
Approximately 3.9 kDa |
Formulation |
Lyophilized from a 0.2 μm filtered solution in PBS |
Reconstitution |
Centrifuge vial before opening. Reconstitute in sterile PBS, pH 7.4 to a concentration of
0.1-1.0 mg/ml |
Storage & Stability |
Store at -20°C. For long-term storage, store at -80°C. Stable for 12 months after receipt |
FAQ
What is pTH (44-68) (human), and how does it work in the human body?
pTH (44-68) (human) refers
to a specific fragment of the human parathyroid hormone (PTH), which is a key regulator of calcium and
phosphate metabolism in the body. This particular fragment encompasses amino acids 44 to 68 of the full
PTH sequence. Unlike the intact hormone, which comprises 84 amino acids, the fragment 44-68 is a smaller
segment that has been studied for specific biological activities distinct from the full-length protein.
The main role of PTH, and by extension its fragments, is to maintain stable levels of calcium in the
blood. It does so by influencing bone resorption and formation, balancing renal tubular reabsorption of
calcium, and regulating the conversion of 25-hydroxyvitamin D to its active form, calcitriol. These
functions are critical to maintaining bone health and ensuring vital cellular processes that depend on
calcium ions proceed correctly. pTH (44-68) has been studied for its potential effects on cellular
signaling pathways that are less prominent with the intact hormone or other fragments, implying
potential therapeutic and research utility. These studies often explore its impact on tissues like bone
or kidney, where full PTH exerts significant effects. By isolating and understanding these interactions,
researchers can begin to decipher whether pTH (44-68) exhibits unique properties that could be harnessed
pharmaceutically or biomedically. Understanding how this peptide might influence cellular responses
differently from the full hormone could aid in developing refined therapeutic strategies that target
specific pathways without some systemic effects associated with full PTH administration. Research into
specific fragments like pTH (44-68) can open new pathways for drug development, diagnostic tools, or
therapeutic interventions. This curiosity also helps explain how hormonal regulation works at a
molecular level, furthering our understanding of cellular communication and homeostasis.
What
potential therapeutic applications does pTH (44-68) (human) possess?
pTH (44-68) (human), due to
its unique segment of the parathyroid hormone structure, may offer several therapeutic applications that
are distinct from the intact hormone. One such area is osteoporosis management. PTH, in general, plays a
significant role in bone remodeling, a process that involves both the resorption and formation of bone.
The fragment pTH (44-68) may exert specific signaling pathways that influence bone density positively,
making it a candidate for treating osteoporosis, a condition characterized by weak and brittle bones. By
understanding its effects on bone cells, researchers can potentially target these interactions to
stimulate bone growth or reduce resorption rates, offering an alternative or adjunctive treatment to
existing therapies like bisphosphonates or other PTH analogs. Another promising application is in the
field of kidney function regulation. Given that parathyroid hormone influences calcium reabsorption in
the kidney, exploring how the fragment pTH (44-68) affects renal pathways may provide insights into
treating conditions like hypercalcemia or secondary hyperparathyroidism, which often complicate chronic
kidney disease. By refining the action of PTH to more specific effects via pTH (44-68), treatments might
offer enhanced safety profiles and reduced side effects.
Moreover, this peptide could have
implications in cardiovascular health, as calcium ions play a pivotal role in myocardial function. The
fragment's specific interaction with cellular processes governing calcium fluxes can lead to novel
treatments addressing cardiac dysfunctions or calcium-related anomalies impacting heart health. Finally,
as fragments like pTH (44-68) provide insights into hormone-receptor interactions at a granular level,
this could lead to diagnostic advancements. Specific binding assays or imaging techniques could benefit
from utilizing this fragment to analyze parathyroid disorders or other endocrine abnormalities. All
considered, these applications underscore the importance of specific PTH fragments in developing
targeted, effective therapies with potentially fewer side effects compared to systemic PTH
treatments.
How does pTH (44-68) (human) differ from the full-length parathyroid
hormone?
pTH (44-68) (human) differs from the full-length parathyroid hormone (PTH), which
consists of 84 amino acids, in structure, function, and potential therapeutic application. While both
are derived from the same PTH sequence, the full-length hormone and its fragment exhibit varying
biological activities and interaction profiles owing to their structural differences. The full-length
PTH is a primary regulatory peptide involved in maintaining calcium and phosphate homeostasis. It
operates mainly by acting on bone and kidneys to regulate the concentration of calcium ions in the
blood. The complete sequence allows it to bind with its receptor PTH1R comprehensively, triggering a
cascade of biochemical pathways that influence mineral metabolism extensively and robustly.
In
contrast, the pTH (44-68) fragment is simply a portion of the full hormone, containing only the amino
acid sequence spanning from positions 44 to 68. Its truncated nature means it may not perform all the
biological activities attributed to full-length PTH. Thus, it might not engage the receptor in the same
manner or to the same extent as the full hormone, potentially activating different intracellular
signaling mechanisms. These differences in interaction and binding affinity might translate into
distinct downstream effects, potentially offering niche clinical or research applications. Such
fragments can help study specific portions of receptor activation pathways without the broad systemic
effects observed with the intact hormone.
Furthermore, by narrowing down hormone functionality
to specific segments like pTH (44-68), researchers can clarify the role of secondary or less prominent
pathways mediated by PTH. Future therapeutic developments might involve this fragment's potential to
engage with cellular receptors in a way that beneficially modulates metabolic functions while mitigating
undesired side effects encountered with full PTH hormone application. Thus, pTH (44-68) provides an
opportunity to dissect PTH-associated pathways more precisely, aiding in better-targeted therapeutic
strategies and enhancing our understanding of hormone biology.
Are there any known side effects
or risks associated with pTH (44-68) (human)?
As of current research and clinical observations,
specific side effects or risks associated with pTH (44-68) (human) are not extensively documented,
primarily because its use as a therapeutic agent is still largely investigational. This peptide, a
truncated form of the parathyroid hormone, is subject to ongoing analysis to delineate its unique
biological activities compared to the full hormone. The understanding of potential side effects largely
derives from observing how full PTH or its analogs have been applied in clinical settings, particularly
concerning bone metabolism and calcium homeostasis. Full-length PTH treatments, such as those used in
osteoporosis therapy, often bring side effects like hypercalcemia, dizziness, nausea, and potential bone
cancer risk with long-term usage in certain populations.
With this background, researchers
proceed cautiously in exploring pTH (44-68) due to its effects on similar pathways in calcium metabolism
and the potential for analogous side effects. Yet, it must be noted that pTH (44-68) might exhibit a
distinct interaction profile on a molecular level, which could translate to a different safety and side
effect profile. During experimental applications, care is taken to monitor calcium and phosphate levels
and assess any physiological impacts on the cardiovascular, renal, or skeletal systems; these are areas
typically influenced by calcium fluctuation and parathyroid function. Another focus of risk evaluation
is potential allergenicity or unwanted immune responses, as with any peptide-based
therapeutic.
However, current studies remain promising that using specific hormone fragments
could potentially offer reduced side effects. By targeting particular cellular responses or minimizing
systemic exposure, there might be less risk of adverse outcomes that plague full hormone use.
Additionally, dosage, administration routes, and treatment durations are critical factors influencing
the safety profile, and these parameters remain under careful scrutiny in clinical and preclinical
trials. For now, anyone considering or researching pTH (44-68) should do so in a well-controlled,
monitored setting to ensure any risks are quickly identified and addressed through medical intervention
or adjustments in therapeutic strategy.
What challenges exist in developing pTH (44-68) (human)
into a therapeutic agent?
Developing pTH (44-68) (human) into a therapeutic agent presents
several challenges spanning scientific, regulatory, and logistical realms. One primary scientific
challenge is understanding the precise mechanism of action and biological activity of this peptide
fragment. Unlike the full parathyroid hormone, which has been well-studied and characterized concerning
its effects on calcium and phosphate metabolism, fragments like pTH (44-68) may operate through less
understood pathways. Uncovering how this specific segment interacts with cellular receptors and
influences metabolic processes is crucial in determining its therapeutic potential and ensuring
predictable safety and efficacy.
Another related challenge pertains to optimizing dosage and
administration routes. Peptide-based therapies often face hurdles in bioavailability and stability, as
peptides can be metabolized rapidly in the gastrointestinal tract and have difficulties crossing
cellular membranes. Thus, researchers must develop suitable formulations and delivery mechanisms that
maintain the fragment's integrity and functionality in vivo. Additionally, achieving the correct
therapeutic dose that balances efficacy with minimal side effects is critical yet often complicated by
individual variability in response.
Regulatory challenges also arise when bringing pTH (44-68)
(human) from research to clinical application. Rigorous testing in preclinical and clinical trials is
necessary to meet approval criteria, ensuring that the fragment's benefits outweigh any potential risks.
This process involves extensive safety profiling, efficacy assessments, and the establishment of clear
therapeutic endpoints. Furthermore, as a new agent, manufacturers must address any regulatory hurdles
related to production, such as ensuring consistent peptide synthesis and validating manufacturing
processes to meet quality standards.
On a logistical level, the development of peptide-based
therapeutics is resource-intensive, requiring significant investment in research and development. The
need for specialized facilities for peptide synthesis and purification can also inflate cost and
development time, posing additional barriers to widespread application. As these agents progress through
the development pipeline, companies must consider the logistics of large-scale production, distribution,
and integration into existing treatment frameworks. Each of these challenges necessitates collaboration
among scientists, regulatory bodies, and pharmaceutical companies to navigate the complex process of
translating a promising peptide fragment into an approved and effective therapeutic option.