Acetyl Tetrapeptide-9
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Acetyl Tetrapeptide-9

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Acetyl Tetrapeptide-9 can promote skin remodeling and help achieve firm and plump skin effects. It can promote the production of human membrane glycans and type I collagen, promote dermal remodeling and skin firmness.

Cosmetic Peptides
Catalog number
CAS number
Molecular Formula
Molecular Weight
Acetyl Tetrapeptide-9
(3S)-3-[[(2S)-2-acetamido-5-amino-5-oxopentanoyl]amino]-4-[[(2S)-1-[[(1S)-1-carboxy-2-(1H-imidazol-5-yl)ethyl]amino]-3-methyl-1-oxobutan-2-yl]amino]-4-oxobutanoic acid
(2S,5S,8S,11S)-2-((1H-imidazol-4-yl)methyl)-11-(3-amino-3-oxopropyl)-8-(carboxymethyl)-5-isopropyl-4,7,10,13-tetraoxo-3,6,9,12-tetraazatetradecanoic acid; Dermican; Ac-Gln-Asp-Val-His-OH; [acetyl]-QDVH-OH; N-acetyl-L-glutaminyl-L-alpha-aspartyl-L-valyl-L-histidine; Acetyl Tetrapeptide 9
1.383±0.06 g/cm3(Predicted)
Boiling Point
Store at 2-8°C
InChI Key
Canonical SMILES
1. Mechanisms and Dynamics of Protein Acetylation in Mitochondria
Josue Baeza, Michael J Smallegan, John M Denu Trends Biochem Sci. 2016 Mar;41(3):231-244. doi: 10.1016/j.tibs.2015.12.006. Epub 2016 Jan 25.
Reversible protein acetylation is a major regulatory mechanism for controlling protein function. Through genetic manipulations, dietary perturbations, and new proteomic technologies, the diverse functions of protein acetylation are coming into focus. Protein acetylation in mitochondria has taken center stage, revealing that 63% of mitochondrially localized proteins contain lysine acetylation sites. We summarize the field and discuss salient topics that cover spurious versus targeted acetylation, the role of SIRT3 deacetylation, nonenzymatic acetylation, and molecular models for regulatory acetylations that display high and low stoichiometry.
2. Current trends in protein acetylation analysis
Issa Diallo, Michel Seve, Valérie Cunin, Frédéric Minassian, Jean-François Poisson, Sylvie Michelland, Sandrine Bourgoin-Voillard Expert Rev Proteomics. 2019 Feb;16(2):139-159. doi: 10.1080/14789450.2019.1559061. Epub 2018 Dec 24.
Acetylation is a widely occurring post-translational modification (PTM) of proteins that plays a crucial role in many cellular physiological and pathological processes. Over the last decade, acetylation analyses required the development of multiple methods to target individual acetylated proteins, as well as to cover a broader description of acetylated proteins that comprise the acetylome. Areas covered: This review discusses the different types of acetylation (N-ter/K-/O-acetylation) and then describes some major strategies that have been reported in the literature to detect, enrich, identify and quantify protein acetylation. The review highlights the advantages and limitations of these strategies, to guide researchers in designing their experimental investigations and analysis of protein acetylation. Finally, this review highlights the main applications of acetylomics (proteomics based on mass spectrometry) for understanding physiological and pathological conditions. Expert opinion: Recent advances in acetylomics have enhanced knowledge of the biological and pathological roles of protein acetylation and the acetylome. Besides, radiolabeling and western blotting remain also techniques-of-choice for targeted protein acetylation. Future challenges in acetylomics to analyze the N-ter and K-acetylome will most likely require enrichment/fractionation, MS instrumentation and bioinformatics. Challenges also remain to identify the potential biological roles of O-acetylation and cross-talk with other PTMs.
3. Lysine acetylation and cancer: A proteomics perspective
Jeovanis Gil, Alberto Ramírez-Torres, Sergio Encarnación-Guevara J Proteomics. 2017 Jan 6;150:297-309. doi: 10.1016/j.jprot.2016.10.003. Epub 2016 Oct 13.
Lysine acetylation is a reversible modification controlled by two groups of enzymes: lysine acetyltransferases (KATs) and lysine deacetylases (KDACs). Acetylated lysine residues are recognized by bromodomains, a family of evolutionarily conserved domains. The use of high-resolution mass spectrometry-based proteomics, in combination with the enrichment of acetylated peptides through immunoprecipitation with anti-acetyl-lysine antibodies, has expanded the number of acetylated proteins from histones and a few nuclear proteins to more than 2000 human proteins. Because acetylation targets almost all cellular processes, this modification has been associated with cancer. Several KATs, KDACs and bromodomain-containing proteins have been linked to cancer development. Many small molecules targeting some of these proteins have been or are being tested as potential cancer therapies. The stoichiometry of lysine acetylation has not been explored in cancer, representing a promising field in which to increase our knowledge of how this modification is affected in cancer. In this review, we will focus on the strategies that can be used to go deeper in the characterization of the protein lysine acetylation emphasizing in cancer research.
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