Taiy Chemical
Acetyl-(Ala10•11)-RANTES (1-14) Amide (human)
Synonym Acetyl-(Ala10-11)-RANTES (1-14) amide
Species Human
Protein Accession P13501
Purity ≥ 95% by SDS-PAGE
Endotoxin Level < 1 EU/μg
Biological Activity Fully biologically active when compared to standard. The specific activity was determined by the ability to chemoattract human T lymphocytes using a concentration range of 1.0-100 ng/ml.
Expression System E. coli
Fusion Tag None
Predicted Molecular Mass 1.5 kDa
Formulation Lyophilized from a 0.2 µm filtered solution in acetonitrile and TFA.
Reconstitution Centrifuge the vial prior to opening. Reconstitute in 20mM Tris, 150mM NaCl, pH 7.5 to a concentration of 0.1-1.0 mg/mL. Do not vortex.
Storage & Stability Store at -80°C. Avoid freeze/thaw cycles.
FAQ
What is Acetyl-(Ala10–11)-RANTES (1-14) amide (human) and how does it function in the human body?
Acetyl-(Ala10–11)-RANTES (1-14) amide (human) is a synthetic peptide that is often used in the field of immunology research due to its influence on chemokine activity. This peptide is a modified form of RANTES, which stands for "Regulated upon Activation, Normal T Cell Expressed and Presumably Secreted." RANTES itself is part of a family of chemokines, which are small signaling proteins critical for immune system function. These chemokines primarily mediate the migration of immune cells like T-cells and macrophages to areas of inflammation or injury, thus playing a pivotal role in the immune response. Acetyl-(Ala10–11)-RANTES amide modifies the chemokine's activity by blocking or altering specific signal transduction pathways, providing a tool for researchers studying immune system processes and pathways that can lead to diseases. By understanding these modifications, researchers can observe how the blockade or alteration of RANTES activity affects inflammation, immune cell migration, and ultimately, the development of immune-related diseases. Moreover, the controlled modification can provide insights into therapeutic potential for conditions like autoimmune diseases, chronic inflammation, and even cancer, where the modulation of immune cell traffic can have significant clinical outcomes. Researchers might also use this peptide to explore potential pathways for preventing organ transplant rejection or developing novel anti-inflammatory treatments. The acetylated modification of this peptide allows it to show selective inhibition or activation, helping researchers pinpoint its exact role and potential therapeutic uses. Overall, Acetyl-(Ala10–11)-RANTES amide serves as an influential tool in understanding and developing treatments targeting chemokine-related aspects of immunological diseases.

What are the potential research applications of using Acetyl-(Ala10–11)-RANTES (1-14) amide in scientific studies?
Acetyl-(Ala10–11)-RANTES (1-14) amide has a broad range of potential research applications, particularly in the fields of immunology, cancer research, and inflammatory disease studies. Because RANTES is a chemokine with pivotal roles in lymphocyte trafficking and immune response modulation, its derivatives, like Acetyl-(Ala10–11)-RANTES, have become important tools in scientific investigation. In immunology, researchers use this peptide to explore the mechanisms underlying immune cell signaling and movement, which is crucial for understanding diseases characterized by immune dysfunction, such as autoimmune diseases and HIV. By observing how modifications to the RANTES chemokine affect immune responses, scientists can identify potential therapeutic targets for minimizing harmful immune reactions while preserving necessary defenses. In cancer research, Acetyl-(Ala10–11)-RANTES amide presents opportunities to study the tumor microenvironment and the role of chemokines in tumor progression and metastasis. Since RANTES is known to be involved in promoting tumor cell survival and invasion, its modulation could reveal pathways crucial for cancer development and provide markers for prognosis or targets for therapy. Additionally, this peptide may assist in evaluating the efficacy of treatments aimed at disrupting chemokine signaling in oncology. Inflammation-related research benefits from this tool as well, given the role of RANTES in promoting the migration of leukocytes to sites of inflammation. Researchers can monitor how inhibiting or altering this process with Acetyl-(Ala10–11)-RANTES amide affects chronic inflammatory diseases like rheumatoid arthritis or inflammatory bowel disease. Such studies can inspire new therapeutic approaches that specifically target chemokine interactions, aiming to balance the reduction of inappropriate inflammation without impairing the body’s ability to fight infections. Overall, Acetyl-(Ala10–11)-RANTES amide represents a versatile and powerful component in the toolkit of biomedical research, advancing our understanding of complex disease mechanisms and the development of novel therapeutic strategies.

How does Acetyl-(Ala10–11)-RANTES (1-14) amide (human) differ from unmodified RANTES in terms of structure and function?
The Acetyl-(Ala10–11)-RANTES (1-14) amide (human) differs from unmodified RANTES chiefly in its structural modifications, which, in turn, influence its function. The introduction of the acetyl group to specific alanine residues in its structure alters both its stability and interaction with other molecules. Structurally, the acetylation at positions 10 and 11 in the peptide leads to an increase in its stability against proteolytic degradation. This is significant because it allows for prolonged activity within biological systems, making it an excellent tool for extended studies in laboratory settings. Although these structural changes seem minute, they can significantly impact the molecule's biological function by modifying how it binds to chemokine receptors and interacts with other signaling components. Functionally, the acetylated form interferes differently with the signaling pathways than the native RANTES does. While unmodified RANTES is involved robustly in chemokine signal transduction that guides immune cell trafficking to sites of inflammation, the modified version can hinder this process, providing insight into potential therapeutic pathways for conditions where excess inflammation is a problem. For instance, in diseases marked by excessive immune activation or chronic inflammation, the modified peptide may serve as a means to deliberately downregulate or alter specific pathways, minimizing harm without broadly suppressing immune function. Moreover, because this analog may interact with a different spectrum or affinity with chemokine receptors, researchers can use it to parse out specific receptor-mediated actions, differentiate functions between receptor subtypes, or identify new pharmacological targets. Understanding the differences in binding dynamics and functional outcomes between the modified and unmodified forms enables detailed study into how selective inhibition or modulation can provide therapeutic benefits. Thus, Acetyl-(Ala10–11)-RANTES (1-14) amide, by altering both receptor engagement and signal transduction impact, serves as a crucial tool in the exploration of chemokine roles in immunity and inflammation.

What are the implications of using Acetyl-(Ala10–11)-RANTES (1-14) amide in therapeutic development?
The implications of using Acetyl-(Ala10–11)-RANTES (1-14) amide in therapeutic development are profound, as this peptide offers a strategic avenue for modulating immune responses, particularly within contexts where chemokine activity plays a pivotal role. Chemokines like RANTES are deeply enmeshed in processes of immune cell signaling and migration, which are crucial for normal immune function but are also implicated in a variety of pathological states when dysregulated. By harnessing the modified peptide, researchers can explore mechanisms for therapeutic intervention that offer precision in targeting pathological processes without excessively dampening overall immune capacity. For instance, in autoimmune diseases where immune cells mistakenly target the body’s own tissues, the selective modulation achieved via Acetyl-(Ala10–11)-RANTES could help to reduce destructive immune cell migration and maintain a state of tolerance. This therapeutic strategy could lead to treatments with fewer off-target effects compared to conventional immunosuppressants. Additionally, in the context of inflammatory diseases like psoriasis or asthma, where chemokine-mediated leukocyte infiltration into tissues contributes to pathology, moderated intervention using this peptide might effectively reduce symptoms and disease progression. In oncology, Acetyl-(Ala10–11)-RANTES amide aids in understanding the role of chemokines in tumor immunity, especially considering that many cancers exploit chemokine signaling to metastasize and evade immune detection. Adjusting chemokine activity with this modified peptide could potentially impair the recruitment and function of immune-suppressive cells within the tumor milieu, promoting better recognition and destruction of cancer cells by the immune system. Furthermore, it provides a foundation for new strategies aiming at enhancing the effectiveness of existing immunotherapies or resistance mechanisms. The ability to refine and target the actions of chemokines therapeutically underscores the utility of Acetyl-(Ala10–11)-RANTES in drug development pipelines. It represents a move towards targeted therapies that address specific pathways and interactions at the molecular level, heralding a new era of precision medicine in the treatment of complex diseases. Ultimately, by better understanding the nuanced roles of chemokines and effectively translating that knowledge into therapeutics, significant progress can be made in managing and treating diseases that have, so far, been resistant to conventional approaches.

How can Acetyl-(Ala10–11)-RANTES (1-14) amide contribute to understanding chronic inflammatory diseases?
Acetyl-(Ala10–11)-RANTES (1-14) amide contributes to the understanding of chronic inflammatory diseases by serving as a scientific probe to dissect the complex interplay of immune signaling that underpins such conditions. Chronic inflammation is often the result of sustained, dysregulated immune responses, where chemokines like RANTES play key roles in perpetuating leukocyte recruitment and activation within affected tissues. By employing this modified peptide, researchers can specifically alter chemokine pathways and observe resultant changes in disease models, thereby elucidating mechanisms that could be targeted therapeutically. In diseases such as rheumatoid arthritis, where continuous neutrophil and lymphocyte infiltration into joints exacerbates tissue damage, Acetyl-(Ala10–11)-RANTES amide facilitates the observation of how modified chemokine signaling can reduce such harmful cellular migrations, consequently alleviating inflammation. Detailed studies using this peptide can highlight necessary checkpoints in the inflammatory signaling cascade that, when targeted, alleviate the chronic aspect of inflammation without compromising necessary immune functions. Similarly, in conditions such as inflammatory bowel disease, characterized by persistent inflammation of the gastrointestinal tract, insights gained from research utilizing the amide can inform potential interventions aimed at modulating chemokine function to restore normal mucosal immunity and integrity. Beyond understanding the biochemical and cellular interactions involved, the peptide aids in identifying biomarkers indicative of disease stage or response to treatment by revealing new aspects of immune communication within inflamed tissues. Furthermore, by impacting chemokine interactions selectively, it helps simulate treatment scenarios in laboratory settings, predicting therapeutic outcomes, and optimizing dosage regimens by observing real-time immune responses. Treatment strategies aspiring to adjust these pathways can significantly alter disease outcomes, turning chronic, debilitating inflammation into manageable conditions by lessening the frequency and severity of flare-ups. By providing a platform for exploring the intricacies of chemokine biology in disease contexts, Acetyl-(Ala10–11)-RANTES serves as a cornerstone for the development of innovative therapeutic strategies aimed at mitigating the burdens of chronic inflammatory conditions, paving the way for breakthroughs that could translate into improved quality of life for patients afflicted by such illnesses.

What role does Acetyl-(Ala10–11)-RANTES (1-14) amide play in oncology research?
Acetyl-(Ala10–11)-RANTES (1-14) amide plays a significant role in oncology research by aiding in the dissection of chemokine-driven processes within the tumor microenvironment. Chemokines, including RANTES, are instrumental in the communication network between tumor cells and the immune system, and their dysregulation often aids in tumor development, immune evasion, and metastasis. By using this modified peptide, researchers can delve into the nuanced roles that chemokines play in oncogenesis and tumor progression. One critical application of this peptide in cancer research is the elucidation of mechanisms by which tumors manipulate immune system responses to support their growth. Cancer-associated fibroblasts, for instance, often secrete RANTES, stimulating tumor cell migration and the recruitment of immune-suppressive cells like regulatory T-cells and myeloid-derived suppressor cells, thereby fostering an immunosuppressive microenvironment. Through the modulation of RANTES activity with Acetyl-(Ala10–11)-RANTES, studies can determine how altering chemokine signaling affects tumor growth, structural integrity, and immune surveillance, providing insights into vulnerabilities that could be exploited therapeutically. Furthermore, this peptide aids in evaluating novel therapeutic approaches, such as chemokine receptor antagonists or inhibitors designed to block tumor-promoting signaling pathways. For instance, researchers can use Acetyl-(Ala10–11)-RANTES to mimic or inhibit chemokine action, creating models to test the efficacy of drugs aiming to re-educate the immune environment toward one that can recognize and destroy cancer cells. Another crucial role of the peptide is in enhancing the understanding of metastasis, the primary cause of cancer-related mortality. By altering chemokine pathways, it helps research elucidate how cancer cells detach, survive in circulation, and colonize distant organs, thus serving as a predictive model for studying metastasis-inhibiting strategies. Its impact extends into personalized medicine, where insights gained from such studies can inform the development of tailored treatment protocols that target specific chemokine-mediated interactions deemed critical for an individual’s cancer progression. Therefore, Acetyl-(Ala10–11)-RANTES facilitates advances in oncology by broadening the comprehension of chemokine roles in cancer biology, driving therapeutic innovation, and refining approaches to treatment that enhance efficacy and reduce adversity, ultimately translating into improved patient outcomes in the battle against cancer.
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