Bestim is a bioactive peptide with an arrangement of polar and hydrophobic residues that support receptor-engagement studies. Its flexible backbone allows diverse conformational sampling. Researchers test its binding characteristics and structural transitions. Applications include signaling-peptide research, structure-activity evaluation, and analog design.
CAT No: R2396
CAS No:66471-20-3
Synonyms/Alias:Bestim;66471-20-3;H-Glu(Trp-OH)-OH;gamma-glutamyltryptophan;L-Tryptophan, L-g-glutamyl-;gamma-Glu-Trp;L-gamma-glutamyl-L-tryptophan;H-D-Glu(Trp-OH)-OH;(2S)-2-amino-5-[[(1S)-1-carboxy-2-(1H-indol-3-yl)ethyl]amino]-5-oxopentanoic acid;N5-((S)-1-carboxy-2-(1H-indol-3-yl)ethyl)-L-glutamine;H-Gamma-D-Glu-Trp-OH;GEW dipeptide;GE-W dipeptide;SCV 07;Gamma-D-glutamyl-L-tryptophan;GGlu-Trp;MFCD00057875;L-gamma-Glu-L-Trp;SCHEMBL726291;CHEMBL4755761;L-Tryptophan, L-gamma-glutamyl-;DTXSID40945401;CHEBI:133028;gamma-Glutamate Tryptophan dipeptide;gamma-Glutamate-Tryptophan dipeptide;AKOS030623021;AC-35273;FG108040;TS-08415;HY-122357;CS-0084183;N-(4-Amino-4-carboxy-1-hydroxybutylidene)tryptophan;(2S)-2-amino-4-{[(1S)-1-carboxy-2-(1H-indol-3-yl)ethyl]carbamoyl}butanoic acid;(S)-2-amino-5-((S)-1-carboxy-2-(1H-indol-3-yl)ethylamino)-5-oxopentanoic acid;227275-47-0;
Bestim, also known as dipeptide immunomodulator or thymogen, is a synthetic peptide compound composed of L-glutamyl-L-tryptophan. As a short-chain peptide, Bestim is recognized for its ability to modulate immune function and regulate cellular processes through interaction with peptide receptors and signaling pathways. Its biochemical structure enables it to participate in a variety of experimental models, making it a valuable reagent in peptide research, immunological studies, and investigations into cell signaling mechanisms. Owing to its well-characterized sequence and defined bioactivity, Bestim is frequently utilized in laboratory settings to probe the molecular underpinnings of immune regulation and peptide-mediated cellular responses.
Immunological research: In immunology-focused laboratories, Bestim serves as a tool for dissecting the molecular mechanisms underlying immune cell activation, differentiation, and cytokine production. Researchers employ this dipeptide to examine how exogenous peptide modulators influence T-cell and macrophage responses in vitro, aiding in the elucidation of pathways involved in innate and adaptive immunity. Its defined sequence allows for reproducible studies on peptide-receptor interactions and downstream signaling events, contributing to a deeper understanding of immune modulation at the molecular level.
Peptide signaling studies: The compound is widely applied in the investigation of peptide-based signal transduction pathways. Its activity in modulating intracellular signaling cascades makes it a model system for studying receptor-mediated events, such as phosphorylation and gene expression changes in response to external peptide stimuli. By enabling controlled activation or inhibition of specific signaling routes, Bestim facilitates the mapping of peptide-responsive networks in various cell types, supporting research into the broader roles of bioactive peptides in cellular physiology.
Cellular differentiation assays: Bestim is utilized in cell culture experiments to explore its effects on the differentiation and maturation of immune and non-immune cell populations. Its modulatory properties provide insights into how short peptides can influence lineage commitment and phenotypic changes under defined experimental conditions. These studies are instrumental for researchers seeking to understand the cues that govern cell fate decisions and the contribution of peptide signals to tissue homeostasis and regeneration.
Peptide structure-activity relationship (SAR) analysis: The defined dipeptide sequence of Bestim makes it an ideal candidate for structure-activity relationship studies within peptide chemistry and pharmacology. Researchers employ it as a reference compound in comparative assays to investigate how modifications to peptide length, sequence, or side chain composition affect biological activity. Such SAR analyses are critical for the rational design of novel peptide analogs with tailored functional properties, informing both basic research and applied peptide engineering efforts.
Analytical method development: Bestim's stability and distinctive chemical characteristics render it a suitable standard or probe in the development and validation of analytical techniques for peptide quantification and detection. Laboratories leverage its properties to optimize chromatographic separation, mass spectrometric analysis, and peptide identification workflows. The use of this dipeptide in analytical method development supports advancements in peptide analytics, ensuring accurate and reproducible measurement of peptide compounds in complex biological matrices.
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