Insulin glulisine is an Insulin Analog. The chemical classification of insulin glulisine is Insulin.
CAT No: 10-101-332
CAS No:207748-29-6
Synonyms/Alias:B3-lysyl-B29-glutamylinsulin
Chemical Name:(4S)-4-[[2-[[(1R,6R,12S,15S,18S,21S,24S,27S,30S,33S,36S,39S,42R,47R,50S,53S,56S,59S,62S,65S,68S,71S,74R,77S,80S,83S,88R)-88-[[(2S)-5-amino-2-[[(2S)-2-[[(2S)-2-[[(2S,3S)-2-[(2-aminoacetyl)amino]-3-methylpentanoyl]amino]-3-methylbutanoyl]amino]-4-carboxybutanoyl]amino]-5-oxopentanoyl]amino]-6-[[(2S)-2-[[(2S)-2-[[(2S)-5-amino-2-[[(2S)-6-amino-2-[[(2S)-2-[[(2S)-2-amino-3-phenylpropanoyl]amino]-3-methylbutanoyl]amino]hexanoyl]amino]-5-oxopentanoyl]amino]-3-(1H-imidazol-4-yl)propanoyl]amino]-4-methylpentanoyl]amino]-47-[[(1S)-3-amino-1-carboxy-3-oxopropyl]carbamoyl]-53-(2-amino-2-oxoethyl)-62-(3-amino-3-oxopropyl)-77-[(2S)-butan-2-yl]-24,56-bis(2-carboxyethyl)-83-[(1R)-1-hydroxyethyl]-12,71,80-tris(hydroxymethyl)-33,50,65-tris[(4-hydroxyphenyl)methyl]-15-(1H-imidazol-4-ylmethyl)-27-methyl-18,30,36,59,68-pentakis(2-methylpropyl)-7,10,13,16,19,22,25,28,31,34,37,40,49,52,55,58,61,64,67,70,73,76,79,82,85,87-hexacosaoxo-21,39-di(propan-2-yl)-3,4,44,45,90,91-hexathia-8,11,14,17,20,23,26,29,32,35,38,41,48,51,54,57,60,63,66,69,72,75,78,81,84,86-hexacosazabicyclo[72.11.7]dononacontane-42-carbonyl]amino]acetyl]amino]-5-[[(2S)-5-carbamimidamido-1-[[2-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S,3R)-1-[(2S)-2-[[(2S)-4-carboxy-1-[[(1S,2R)-1-carboxy-2-hydroxypropyl]amino]-1-oxobutan-2-yl]carbamoyl]pyrrolidin-1-yl]-3-hydroxy-1-oxobutan-2-yl]amino]-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-2-oxoethyl]amino]-1-oxopentan-2-yl]amino]-5-oxopentanoic acid
Insulin glulisine is a synthetic peptide analog of human insulin, specifically engineered to exhibit rapid onset and short duration of action. Structurally, it differs from native insulin by the substitution of asparagine at position B3 with lysine, and lysine at position B29 with glutamic acid, modifications that enhance its absorption kinetics and bioactivity profile. As a recombinant peptide, insulin glulisine holds significant importance in biochemical research focused on insulin signaling, receptor interaction, and metabolic regulation. Its unique pharmacodynamic properties make it a valuable tool for investigating the molecular mechanisms of glucose uptake, insulin receptor activation, and downstream signaling pathways, supporting a broad spectrum of scientific and technical applications within metabolic and endocrinological research.
Peptide signaling research: Insulin glulisine is extensively utilized as a model compound in studies exploring the molecular dynamics of insulin receptor binding and activation. Its rapid-acting profile allows researchers to dissect the temporal aspects of insulin-mediated signal transduction, facilitating detailed analyses of receptor phosphorylation events, adaptor protein recruitment, and the activation of key downstream effectors such as PI3K and Akt. By enabling precise control over the timing and magnitude of insulin signaling, this analog supports investigations into the fine-tuning of metabolic pathways and the identification of modulators influencing insulin sensitivity.
Glucose metabolism studies: The compound is a critical reagent in experiments designed to elucidate the regulation of glucose uptake and utilization in various cellular and tissue models. Due to its swift action, insulin glulisine serves as an effective stimulus for probing the kinetics of GLUT4 translocation, glycogen synthesis, and glycolytic flux in adipocytes, myocytes, and hepatocytes. These studies are instrumental in advancing the understanding of metabolic homeostasis, insulin resistance mechanisms, and the interplay between insulin signaling and cellular energy balance.
Peptide structure-function analysis: The specific amino acid substitutions in insulin glulisine provide a unique framework for examining the structure-activity relationships of insulin peptides. Researchers employ this analog to investigate how modifications in the B-chain influence receptor affinity, aggregation behavior, and stability in solution. Such studies contribute to the rational design of novel insulin analogs with tailored pharmacokinetic properties and inform the broader field of peptide engineering, including the development of next-generation biotherapeutics and delivery systems.
Cell culture applications: In vitro systems frequently employ insulin glulisine as a defined supplement to stimulate insulin-responsive pathways in cultured cells. Its rapid and predictable action makes it particularly suitable for time-course experiments assessing acute metabolic responses, gene expression changes, and the modulation of anabolic processes. By providing a consistent and reproducible insulin stimulus, the analog enhances the reliability of cell-based assays investigating insulin-dependent phenomena, including differentiation, proliferation, and metabolic adaptation.
Analytical method development: The synthetic nature and well-characterized properties of insulin glulisine render it a valuable standard in the development and validation of analytical techniques for peptide quantification. It is often used in high-performance liquid chromatography (HPLC), mass spectrometry, and immunoassay calibration, supporting the accurate measurement of insulin analogs in complex biological matrices. Through these applications, the compound aids in advancing the precision and sensitivity of peptide detection methodologies, which are essential for both basic research and quality control in peptide synthesis workflows.
1. Store-operated Ca2+ entry sustains the fertilization Ca2+ signal in pig eggs
2. Adipose tissue is a key organ for the beneficial effects of GLP-2 metabolic function
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