Splenopentin exhibits the full bioactivity of the hormone splenin. Splenopentin increases white blood-cell production if suppressed, in addition to other immune-regulating compounds, which includes interleukin-3 and macrophage colony-stimulating factors.
CAT No: 10-101-41
CAS No:75957-60-7 (net), 105184-37-0 (acetate)
Synonyms/Alias:Splenopentin Acetate;105184-37-0;acetic acid;4-[[6-amino-2-[[2-amino-5-(diaminomethylideneamino)pentanoyl]amino]hexanoyl]amino]-5-[[1-[[1-carboxy-2-(4-hydroxyphenyl)ethyl]amino]-3-methyl-1-oxobutan-2-yl]amino]-5-oxopentanoic acid;
Splenopentin Acetate is a synthetic pentapeptide derived from the spleen that has garnered significant attention for its unique biochemical properties and potential research applications. This peptide mimics a naturally occurring sequence found in splenic extracts, making it a valuable tool for exploring immunological pathways and cellular interactions in vitro and in vivo. Its structure confers stability and specificity, allowing researchers to design experiments that probe the complexities of immune modulation and peptide signaling. Splenopentin Acetate is soluble in aqueous solutions, which facilitates its integration into a variety of experimental protocols, including cell culture studies and molecular assays. As a result, it has become a staple in immunological research, offering a versatile approach to dissecting the roles of small peptides in biological systems.
Immunology Research: Splenopentin Acetate serves as a critical reagent in immunology research, where it is frequently employed to investigate the mechanisms underlying immune cell activation, differentiation, and communication. By introducing this peptide to cultured immune cells, scientists can monitor changes in cell surface markers, cytokine production, and gene expression patterns, thereby elucidating how short peptide sequences influence the immune response. Its use enables the identification of novel signaling pathways and potential targets for immune modulation, which is fundamental for advancing basic immunological knowledge.
Cellular Signaling Studies: In the context of cellular signaling, Splenopentin Acetate is utilized to dissect the intricate communication networks between immune cells and other cell types. Researchers leverage its structure to probe receptor-ligand interactions on the cellular membrane, providing insights into how external peptide signals are transduced into intracellular responses. This application is particularly valuable for mapping the downstream effects of peptide-receptor engagement, including kinase activation and transcription factor mobilization, which are essential for understanding cell fate decisions.
Peptide Drug Discovery: Splenopentin Acetate plays an instrumental role in the early stages of peptide drug discovery, especially as a prototype for designing novel immunomodulatory agents. By studying its interaction with immune cells and receptors, medicinal chemists can identify structural features that enhance biological activity or selectivity. This information is then applied to the rational design of new peptide analogs with improved pharmacological profiles. The use of Splenopentin Acetate in this context accelerates the identification and optimization of lead compounds for further preclinical investigation.
Biomarker Validation: In biomarker research, Splenopentin Acetate is applied as a reference compound to validate the specificity and sensitivity of immunoassays. Researchers incorporate it into assay development pipelines to benchmark detection systems for peptide-based biomarkers in biological samples. Its defined sequence and reproducible effects make it an ideal standard for calibrating assays, optimizing detection limits, and reducing background noise. This application is crucial for ensuring that novel biomarkers are reliably detected and quantified during exploratory and validation studies.
Protein Interaction Mapping: Scientists employ Splenopentin Acetate to map protein-protein and protein-peptide interactions within the immune system. By labeling the peptide or using it in pull-down assays, researchers can identify binding partners and elucidate the molecular architecture of immune complexes. This approach supports the discovery of previously uncharacterized interactions and provides a platform for screening potential modulators of these complexes. Such studies are foundational for understanding the dynamic networks that govern immune surveillance and response.
Splenopentin Acetate continues to be a cornerstone in the toolkit of immunologists, molecular biologists, and pharmaceutical researchers. Its versatility in experimental design, combined with its ability to mimic endogenous peptide sequences, makes it an indispensable asset for advancing the understanding of immune regulation, peptide signaling, and protein interactions. As research in immunology and peptide therapeutics evolves, the applications of Splenopentin Acetate are expected to expand, driving innovation in both basic science and translational research settings.
Splenopentin (SP-5, Arg-Lys-Glu-Val-Tyr) and thymopentin (TP-5, Arg-Lys-Asp-Val-Tyr) are synthetic immunomodulating peptides corresponding to the region 32-34 of a splenic product called splenin (SP) and the thymic hormone thymopoietin (TP), respectively. TP was originally isolated as a 5-kDa (49-amino acids) protein from bovine thymus while studying effects of the thymic extracts on neuromuscular transmission and was subsequently observed to affect T cell differentiation and function. TP I and II are two closely related polypeptides isolated from bovine thymus. A radioimmunoassay for TP revealed a crossreaction with a product found in spleen and lymph node. This product, named splenin, differs from TP only in position 34, aspartic acid for bovine TP and glutamic acid for bovine splenin and it was called TP III as well. Synthetic pentapeptides (TP-5) and (SP-5), reproduce the biological activities of TP and SP, respectively. It is now evident that various forms of TPs were created by proteolytic cleavage of larger proteins during isolation, cDNA clones have been isolated for three alternatively spliced mRNAs that encodes three distinct human T cell TPs. The immunomodulatory properties of TP, SP, TP-5, SP-5 and some of their synthetic analogs reported in the literature have been briefly reviewed.
Singh, V. K., Biswas, S., Mathur, K. B., Haq, W., Garg, S. K., & Agarwal, S. S. (1998). Thymopentin and splenopentin as immunomodulators. Immunologic research, 17(3), 345-368.
Splenopentin, Arg-Lys-Glu-Val-Tyr (SP-5) and its synthetic analogs; Arg-d-Lys-Glu-Val-Tyr (pentapeptide 1), Lys-Lys-Glu-Val-Tyr (2), d-Lys-Lys-Glu-Val-Tyr (3), Arg-Lys-Gly-Val-Tyr (4), and Arg-Lys-Gln-Val-Tyr (5) have been examined for augmentation of human natural killer (NK) cell activity and human T-cell transformation response. Pentapeptides 2 and 3 were found to significantly augment the in vitro human NK cell activity. However, none of them had any effect on lymphocyte proliferative responses.
Rastogi, A., Singh, V. K., Biswas, S., Haq, W., Mathur, K. B., & Agarwal, S. S. (1993). Augmentation of human natural killer cells by splenopentin analogs. FEBS letters, 317(1-2), 93-95.
2. Cell-based adhesion assays for isolation of snake venom’s integrin antagonists
4. Urinary Metabolites Associated with Blood Pressure on a Low-or High-Sodium Die
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