Insulin Glargine is a recombinant human insulin analog with long-acting, blood glucose-lowering activity. Insulin glargine, like regular types of human insulin, regulates glucose metabolism by binding to insulin receptors on muscle and fat cells, thereby facilitating the cellular uptake of glucose. This lowers blood glucose levels. At the same time, insulin glargine inhibits the liver's conversion of stored glycogen into glucose, which also contributes to lower blood glucose levels. Insulin glargine also inhibits lipolysis in adipose tissue, inhibits proteolysis, and enhances protein synthesis.
CAT No: 10-101-331
CAS No:160337-95-1
Synonyms/Alias:L-phenylalanyl-L-valyl-L-asparagyl-L-glutaminyl-L-histidyl-L-leucyl-L-cysteinyl-glycyl-L-seryl-L-histidyl-L-leucyl-L-valyl-L-alpha-glutamyl-L-alanyl-L-leucyl-L-tyrosyl-L-leucyl-L-valyl-L-cysteinyl-glycyl-L-alpha-glutamyl-L-arginyl-glycyl-L-phenylalanyl-L-phenylalanyl-L-tyrosyl-L-threonyl-L-prolyl-L-lysyl-L-threonyl-L-arginyl-L-arginine (7->7'),(19->20')-bis(disulfide) compound with glycyl-L-isoleucyl-L-valyl-L-alpha-glutamyl-L-glutaminyl-L-cysteinyl-L-cysteinyl-L-threonyl-L-seryl-L-isoleucyl-L-cysteinyl-L-seryl-L-leucyl-L-tyrosyl-L-glutaminyl-L-leucyl-L-alpha-glutamyl-L-asparagyl-L-tyrosyl-L-cysteinyl-glycine (6'->11')-disulfide
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)-4-amino-2-[[(2S)-2-[[(2S)-2-amino-3-phenylpropanoyl]amino]-3-methylbutanoyl]amino]-4-oxobutanoyl]amino]-5-oxopentanoyl]amino]-3-(1H-imidazol-4-yl)propanoyl]amino]-4-methylpentanoyl]amino]-53-(2-amino-2-oxoethyl)-62-(3-amino-3-oxopropyl)-77-[(2S)-butan-2-yl]-24,56-bis(2-carboxyethyl)-47-(carboxymethylcarbamoyl)-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)-1-[[2-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S,3R)-1-[(2S)-2-[[(2S)-6-amino-1-[[(2S,3R)-1-[[(2S)-5-carbamimidamido-1-[[(1S)-4-carbamimidamido-1-carboxybutyl]amino]-1-oxopentan-2-yl]amino]-3-hydroxy-1-oxobutan-2-yl]amino]-1-oxohexan-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]-5-carbamimidamido-1-oxopentan-2-yl]amino]-5-oxopentanoic acid
Insulin glargine is a synthetic long-acting insulin analog widely utilized in biochemical and pharmacological research to investigate insulin receptor signaling, glucose metabolism, and the structural-functional relationships of peptide hormones. As a recombinant peptide, it is engineered to mimic the molecular actions of endogenous human insulin while exhibiting distinct pharmacokinetic properties that extend its duration of action. Its unique amino acid modifications confer altered solubility and absorption characteristics, making it a valuable tool for exploring the impact of structural changes on peptide hormone function. Researchers leverage insulin glargine to dissect the mechanisms of insulin action, evaluate receptor-ligand interactions, and model the effects of sustained insulin exposure in various experimental systems.
Receptor signaling studies: Insulin glargine is frequently employed in studies aimed at elucidating the molecular mechanisms underlying insulin receptor activation and downstream signaling cascades. Its ability to bind and activate the insulin receptor, while maintaining a prolonged activity profile, enables researchers to assess sustained signaling events, phosphorylation patterns, and gene expression changes in cultured cells or tissue models. These investigations contribute to a deeper understanding of insulin-mediated cellular processes, including glucose uptake, metabolism, and cell growth regulation.
Comparative peptide analysis: Due to its engineered amino acid sequence and altered pharmacodynamic profile, insulin glargine serves as a reference compound in comparative studies of insulin analogs and related peptides. Researchers utilize it to examine how specific structural modifications influence receptor affinity, biological potency, and metabolic stability. Such comparative analyses are critical for mapping structure-activity relationships, optimizing peptide design, and advancing the development of next-generation insulin analogs or therapeutic peptides for research use.
Protein engineering research: The distinct modifications present in insulin glargine make it a model system for protein engineering and synthetic biology applications. By studying its altered solubility, aggregation behavior, and stability under various conditions, scientists gain insights into the effects of amino acid substitutions and peptide backbone alterations. These findings inform the rational design of novel peptide hormones and biopharmaceuticals with tailored pharmacokinetic and physicochemical properties, supporting innovation in the field of peptide-based drug development and research reagents.
In vitro metabolic assays: Insulin glargine is utilized in a range of in vitro assays designed to probe glucose uptake, glycogen synthesis, and metabolic enzyme regulation in cultured cells or isolated tissues. Its prolonged activity profile enables the modeling of chronic insulin exposure, facilitating studies of cellular adaptation, insulin resistance mechanisms, and metabolic flux. These assays provide critical data for understanding the biochemical pathways influenced by insulin and for evaluating the metabolic consequences of sustained peptide hormone signaling.
Analytical method development: The unique structural features and stability of insulin glargine make it a suitable standard for the development and validation of analytical techniques, such as high-performance liquid chromatography (HPLC) and mass spectrometry, for peptide quantification and characterization. Researchers employ it to optimize separation protocols, assess detection sensitivity, and calibrate instrumentation for the analysis of insulin analogs and related peptides. Such methodological advancements are essential for ensuring reproducibility and accuracy in peptide research and quality control workflows.
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