Taiy Chemical
Boc-(β-Ala13)-Gastrin (13-17)
Synonym Boc-(β-Ala13)-Gastrin (13-17)
Species Human
Protein Accession NA
Purity >95%
Endotoxin Level <1 EU/μg
Biological Activity NA
Expression System Chemical synthesis
Fusion Tag Boc-(β-Ala13)
Predicted Molecular Mass 1606.91 Da
Formulation Supplied as a trifluoroacetate salt
Reconstitution It is recommended to reconstitute the lyophilized product with sterile water at a concentration of 0.1 mg/ml, which can then be further diluted in other aqueous solutions.
Storage & Stability Store at -20°C upon receipt. Upon reconstitution, store at 4°C for up to 2 weeks or aliquot and store at -20°C.
FAQ
What is Boc-(β-Ala13)-Gastrin (13-17) and what is its primary application?

Boc-(β-Ala13)-Gastrin (13-17) is a synthetic peptide derivative known for its potential applications in medical and biochemical research. The peptide includes a specific sequence that mimics a portion of the naturally occurring gastrin hormone, which is involved in various physiological processes such as stimulating gastric acid secretion and promoting gastrointestinal tract motility. The addition of Boc (tert-butyloxycarbonyl) and β-Ala to its structure enhances its stability and allows for differential interactions in experimental settings. Research indicates that this peptide could be instrumental in studying the mechanisms of gastrin receptor interactions, revealing insights into digestive health and disease conditions. Its stability and modified structure make it a valuable tool for laboratory researchers interested in gastrin's broader physiological roles beyond traditional secretion activities.

The primary application of Boc-(β-Ala13)-Gastrin (13-17) is centered around scientific inquiry into its role in the gastrointestinal system and potential therapeutic applications. Researchers are particularly interested in its ability to interact with gastrin receptors on parietal cells and deeper insights into its downstream pathways. By using this peptide, scientists can investigate cellular responses such as proliferation, migration, or differentiation, all of which are crucial to understanding gastric cancers, Zollinger-Ellison syndrome, and peptic ulcer disease.

Furthermore, Boc-(β-Ala13)-Gastrin (13-17) can be used in developing assays that test its agonistic or antagonistic properties on gastrin receptors, providing crucial insights for drug discovery and development. By analyzing the binding affinity, intracellular signaling pathways, and physiological outcomes, researchers can develop pharmacological agents that better manipulate gastrin levels in the body to treat related disorders. This specificity is essential when considering the background of gastric diseases allied with improper gastrin levels or its receptor activity. Consequently, Boc-(β-Ala13)-Gastrin (13-17) can act as a pioneer structure in therapeutic designs aimed at niche yet impactful health challenges, making it an indispensable component of modern peptide research.

What are the benefits of modified peptides like Boc-(β-Ala13)-Gastrin (13-17) over natural peptides in scientific research?

Modified peptides like Boc-(β-Ala13)-Gastrin (13-17) provide significant advantages over natural peptides in scientific research, primarily owing to their enhanced stability, versatility, and customizability. One of the substantial benefits is their increased resistance to enzymatic degradation. Natural peptides often face rapid breakdown in biological systems due to the action of peptidases and proteases, which can significantly limit their utility in long-term studies or applications. The introduction of modifications such as the Boc group and β-alanine in Boc-(β-Ala13)-Gastrin (13-17) offers structural protection against such enzymatic activity, ensuring the peptide remains active longer and maintains its intended function during experiments.

Another significant advantage is improved specificity and target binding. Synthetic modifications allow researchers to fine-tune the peptide's interaction with its target receptor or protein, enabling the study of specific interactions with a level of precision difficult to achieve with natural peptides. This specificity aids in reducing off-target effects and helps in elucidating the precise mechanisms underlying receptor-ligand interactions. This ability is particularly beneficial in drug development and pharmacokinetics, where understanding specific binding dynamics is crucial for the success of therapeutic interventions.

Moreover, modified peptides can be engineered to have enhanced solubility and delivery properties. By altering the peptide's hydrophobic and hydrophilic balance through structural changes, researchers can better facilitate its administration in biological systems. This attribute is particularly important in the design of therapeutic peptides, as improved solubility can enhance the compound's bioavailability and efficacy in combating diseases.

In addition, these peptides offer enhanced study options regarding structure-activity relationships (SAR). With synthetic modifications, systematic variations can be introduced to investigate their roles in activity and stability comprehensively. Such studies help in designing better analogs with improved function and reduced side effects. By diversifying the chemical landscape available for experimentation, researchers can push the boundaries of what is known about peptide-receptor interactions, potentially unlocking novel therapeutic pathways and applications.

How does Boc-(β-Ala13)-Gastrin (13-17) influence gastric secretion and what implications does this have for research?

Boc-(β-Ala13)-Gastrin (13-17) is a modified peptide designed to study the influences on gastric secretion, a process known to be regulated by gastrin, a key digestive hormone. Gastrin primarily acts on the parietal cells of the gastric mucosa to stimulate the secretion of gastric acid. It interacts with receptors that trigger a signaling cascade resulting in increased acid production, which is essential for digestion and absorption of nutrients, as well as maintaining an acidic environment that prevents the growth of pathogenic microorganisms.

Studying Boc-(β-Ala13)-Gastrin (13-17) offers detailed insights into the dynamics of gastrin receptor interaction. The peptide’s modified structure allows researchers to explore its binding efficacy, receptor activation potential, and subsequent impact on cellular pathways. This is crucial for understanding gastric hypersecretion conditions, where excessive gastric acid can lead to ulcers or worsen gastrointestinal diseases. By observing how Boc-(β-Ala13)-Gastrin (13-17) influences acid secretion through in vitro studies or in vivo models, researchers can develop strategies to modulate this process, offering a pathway to novel treatments for acid-related disorders such as Zollinger-Ellison syndrome or peptic ulcer disease.

Moreover, the peptide’s influence on gastric secretion can also serve as a biomarker for monitoring the therapeutic potential of new drugs. Understanding how it modulates acid secretion provides a benchmark to assess whether new pharmacological interventions can produce desirable effects while minimizing harmful consequences. It could also facilitate the discovery of new antagonists or agonists, fine-tuned to balance gastric secretory activity in patients with disrupted gastric acid production.

In research contexts, leveraging Boc-(β-Ala13)-Gastrin (13-17) allows for the exploration of secondary effects on gastric mucosa and its regenerative properties. This is because gastrin also plays roles beyond acid secretion, including promoting mucosal growth and influencing gastric motility. Analyzing how this peptide affects these additional parameters could broaden the understanding of gastrin's role in gastrointestinal health and diseases, shaping new research avenues into mucosal repair and gastrointestinal stasis prevention. Therefore, Boc-(β-Ala13)-Gastrin (13-17) stands as a critical tool in both fundamental and applied gastric research, with implications that extend into therapeutic innovation.

In what ways is Boc-(β-Ala13)-Gastrin (13-17) utilized in the field of cancer research?

Boc-(β-Ala13)-Gastrin (13-17) finds prominent utilization in cancer research due to the significant role that gastrin and its derivatives play in tumorigenesis, especially within cancers of the gastrointestinal tract such as gastric, colorectal, and pancreatic cancer. Gastrin is not only a regulator of gastric acid secretion but also influences cell proliferation within the gastrointestinal lining. Its role in promoting epithelial cell growth can become detrimental when signaling goes awry, potentially leading to aberrant cell growth and tumor development.

In cancer research, Boc-(β-Ala13)-Gastrin (13-17) provides a valuable model for examining how gastrin-related pathways contribute to cancer cell proliferation, migration, and invasion. The peptide’s modified structure allows researchers to dissect its interaction with various cholecystokinin (CCK) receptors, especially the CCK-B receptor, which is overexpressed in several gastrointestinal tumors. By examining how this peptide modifies receptor pathways, researchers can better understand the relationship between gastrin signaling and oncogenic transformation.

Furthermore, Boc-(β-Ala13)-Gastrin (13-17) can serve in the development of therapeutic strategies aiming to inhibit or alter the gastrin-mediated pathways implicated in tumor growth. This notion predicates on the hypothesis that blocking gastrin or its receptor interaction can mitigate tumor proliferation. Accordingly, the peptide can act as a template for creating gastrin-like antagonists or for designing small molecule inhibitors that specifically target overactive receptors in cancerous tissues.

Additionally, the peptide assists in understanding the role of gastrin as part of the tumor microenvironment. Cancer research increasingly recognizes the tumor microenvironment's impact on tumor progression, including factors like cytokines, growth factors, and their interactions. Boc-(β-Ala13)-Gastrin (13-17) may help unravel how gastrin contributes to this environment, influencing not only cancer cells but also stromal interactions that support tumor growth and metastasis.

Through such studies, Boc-(β-Ala13)-Gastrin (13-17) contributes to a more nuanced understanding of the complex biology underlying gastrointestinal malignancies. By bridging basic scientific research and clinical applications, this peptide supports the development of personalized cancer therapies, offering a pathway towards interventions that specifically harness or counteract gastrin’s role in cancer proliferation and survival. Thus, it plays a crucial role in the continual effort to translate molecular insights into effective cancer prevention and treatment strategies.

How does Boc-(β-Ala13)-Gastrin (13-17) compare to other gastrin analogs in research?

Boc-(β-Ala13)-Gastrin (13-17) represents a specialized category within gastrin analogs designed to enhance stability, specificity, and functionality compared to both natural and other synthetic gastrin-related peptides. One significant point of comparison lies in its improved biochemical stability. The Boc modification and incorporation of β-alanine potentially reduce susceptibility to enzymatic degradation, an advantage over unmodified gastrin which often faces rapid proteolytic breakdown in biological systems. This enhanced stability allows for more extended periods of utility within experimental frameworks, giving researchers time to observe longer-term effects or to conduct intricate longitudinal studies.

In research, different gastrin analogs are often evaluated based on their receptor affinity, efficacy, and intracellular signaling outcomes. Boc-(β-Ala13)-Gastrin (13-17) can be engineered to optimize these interactions, thereby offering more precise experimental control. This specificity is not always possible with other analogs or the native hormone, making Boc-(β-Ala13)-Gastrin (13-17) a potentially superior choice when a detailed understanding of receptor-specific functions or signaling pathways is required. Moreover, its modified configuration might allow for a nuanced study of partial receptor agonism/antagonism, opening doors to diverse pharmaceutical applications.

Another factor of comparison includes its ability to generate controlled biological responses. Some gastrin analogs may non-specifically bind to multiple receptor subtypes, complicating interpretations of experimental data. In contrast, Boc-(β-Ala13)-Gastrin (13-17) might be tailored through its modifications to preferentially bind certain receptor subpopulations, reducing off-target interactions and yielding clearer, more interpretable results.

Furthermore, Boc-(β-Ala13)-Gastrin (13-17) aids in more comprehensive structure-activity relationship studies. Utilizing this peptide, researchers can systematically vary peptide structures to observe corresponding changes in biological activity, allowing for a profound understanding of how different structural features influence physiological outcomes. This approach can be essential for drug development programs aiming to derive clinical candidates with refined pharmacodynamic and pharmacokinetic profiles from the gastrin scaffold.

While other analogs could be designed for particular purposes—such as reduced immunogenicity or increased solubility—it is the combination of stability, specificity, and targeted functionality that often makes Boc-(β-Ala13)-Gastrin (13-17) ideal in advanced research settings. This nuanced application underscores its role in driving forward both fundamental gastrin research and potential therapeutic innovations, offering a multifaceted tool highly valued in academic and commercial research spheres alike.
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