Insulin Aspart is a recombinant human insulin analog with rapid-acting, blood glucose-lowering activity. Insulin aspart, acting faster than regular 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 aspart inhibits the liver's conversion of stored glycogen into glucose, which also contributes to lower blood glucose levels. Insulin aspart also inhibits lipolysis in adipose tissue, inhibits proteolysis, and enhances protein synthesis.
CAT No: 10-101-330
CAS No:116094-23-6
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-alpha-aspartyl-L-lysyl-L-threonine (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-L-asparagine (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]-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)-1-[[2-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S,3R)-1-[[(2S)-1-[[(2S)-6-amino-1-[[(1S,2R)-1-carboxy-2-hydroxypropyl]amino]-1-oxohexan-2-yl]amino]-3-carboxy-1-oxopropan-2-yl]amino]-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 aspart is a synthetic peptide analog of human insulin, distinguished by a single amino acid substitution that enhances its rapid-acting pharmacokinetic profile. As a recombinant protein engineered through site-directed mutagenesis, it exhibits a modified B-chain in which proline at position 28 is replaced with aspartic acid. This structural alteration reduces self-association, resulting in faster absorption and onset of action compared to native human insulin. Insulin aspart is extensively utilized in biochemical and physiological studies to elucidate the dynamics of insulin receptor activation, glucose metabolism, and peptide engineering. Its unique properties make it a valuable tool for researchers investigating the molecular mechanisms of insulin action, receptor-ligand interactions, and peptide-based drug design.
Receptor Binding Studies: The rapid dissociation and receptor binding characteristics of this insulin analog enable detailed investigations into the kinetics of insulin receptor activation and downstream signaling pathways. Researchers use it to analyze the molecular determinants of ligand-receptor affinity, specificity, and conformational changes upon binding. Such studies provide deeper insight into the mechanisms governing insulin-mediated cellular responses and can inform the rational design of next-generation peptide therapeutics targeting the insulin receptor or related pathways.
Glucose Metabolism Research: Due to its well-characterized rapid-acting profile, the analog serves as a model compound for dissecting the acute effects of insulin on glucose uptake, transport, and metabolic flux in cellular and tissue-based systems. Experimental use in in vitro and ex vivo models allows for precise temporal control of insulin exposure, facilitating studies on glucose transporter translocation, glycogen synthesis, and metabolic enzyme regulation. These applications are critical for advancing the understanding of insulin's role in metabolic homeostasis and energy balance.
Peptide Engineering and Structure-Function Analysis: As a prototypical example of a site-specifically modified insulin molecule, this analog is widely employed in structure-function studies of peptide hormones. Researchers leverage its sequence variation to probe the impact of specific amino acid substitutions on peptide folding, stability, aggregation propensity, and biological activity. Such investigations are instrumental in guiding the rational engineering of peptide therapeutics with tailored pharmacokinetics and receptor selectivity.
Analytical Method Development: The distinct physicochemical and chromatographic properties of this recombinant peptide make it a reliable standard in developing and validating analytical methods for insulin and its analogs. Laboratories utilize it in high-performance liquid chromatography (HPLC), mass spectrometry, and immunoassay platforms to assess assay specificity, sensitivity, and reproducibility. Its inclusion as a reference material supports accurate quantification and quality control in research and industrial settings where peptide hormone measurement is required.
Cell Signaling and Functional Assays: The rapid action and predictable bioactivity of this analog enable its use in cell-based assays designed to monitor insulin-stimulated signaling cascades, including phosphorylation of downstream effectors such as Akt and ERK. Researchers apply it to dissect temporal aspects of insulin-induced cellular responses, evaluate signal transduction efficiency, and study feedback regulation within insulin-responsive pathways. These applications are fundamental to advancing knowledge of insulin biology and the modulation of metabolic signaling networks in health and disease models.
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