Cartalax peptide is a synthetic tripeptide bioregulator with the defined sequence Ala-Glu-Asp (AED), produced through controlled peptide synthesis. It is supplied as a 20mg lyophilized powder in a sealed vial, with ≥99% purity confirmed by independent HPLC testing and a Certificate of Analysis for every batch. Cartalax is characterized in laboratory research on chondrocyte aging, chondrogenic differentiation, and fibroblast extracellular matrix remodeling. It is also studied in renal cell culture models and in research on how short peptides interact with DNA and influence gene expression.
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Cartalax belongs to the family of short regulatory peptides described by the St. Petersburg Institute of Bioregulation and Gerontology. In the research literature it appears as AED peptide and under the earlier designation T-31.
The compound is a linear L-tripeptide of alanine, glutamic acid, and aspartic acid. Two of its three residues carry acidic side chains, which gives the molecule a net negative charge at neutral pH.
As a Cartalax bioregulator, AED is examined in cartilage, skin fibroblast, kidney, and mesenchymal stem cell cultures. Researchers use it to study senescence markers, extracellular matrix proteins, and sirtuin expression under controlled laboratory conditions.
Store the lyophilized compound at -20°C, protected from light and moisture.
After reconstitution, store at 2–8°C and use promptly.
Maintain aseptic handling to preserve compound integrity.
Lyophilized Format
This compound ships in lyophilized (freeze-dried) form. Freeze-drying supports long-term storage stability and preserves compound integrity. No fillers are added.
Research Use Disclaimer
Cartalax is supplied for research use only. It is not a drug, food, cosmetic, or dietary supplement and has not been evaluated by the FDA. By purchasing, the buyer confirms the compound will be used solely for in vitro research.
Frequently Asked Questions
What Is Cartalax Peptide?
Cartalax peptide is a synthetic tripeptide bioregulator with the sequence Ala-Glu-Asp (AED). It is studied in laboratory models of chondrocyte aging, fibroblast matrix remodeling, and renal cell senescence.
What Is the CAS Number of Cartalax?
The CAS Number of Cartalax (Ala-Glu-Asp) is 85806-95-7, and its PubChem CID is 87815447. The compound has the molecular formula C₁₂H₁₉N₃O₈ and a molecular weight of 333.29 g/mol.
How Does Cartalax Differ From BPC-157?
Cartalax is a three-residue peptide (Ala-Glu-Asp), while BPC-157 is a separate fifteen-residue peptide with an unrelated sequence. The two compounds have different identifiers and are characterized in different areas of laboratory research.
What Research Areas Is Cartalax Studied In?
Cartalax is studied in chondrocyte and mesenchymal stem cell cultures, aging skin fibroblast models, and renal cell cultures. Research focuses on senescence markers, extracellular matrix proteins, sirtuin expression, and peptide interaction with DNA.
How Is Cartalax 20mg Supplied and Stored?
Cartalax 20mg is supplied as a lyophilized white powder at ≥99% purity, with a Certificate of Analysis for every batch. The lyophilized compound is stored at -20°C and protected from light.
Research Overview
Cartalax research centers on chondrocyte models. In aging chondrocyte cultures, AED normalized the synthesis of p16, p21, p53, TNF-α, IL-1α, and SIRT1, the markers that make up the senescence-associated secretory phenotype [1].
In mesenchymal stem cells during replicative aging, AED at 200 ng/mL increased gene expression and protein synthesis of the chondrogenic markers SOX9, aggrecan, type II collagen, and COMP [2].
Fibroblast cultures form a second research thread. In aging skin fibroblasts, AED inhibited MMP-9 synthesis, raised expression of Ki-67 and CD98hc, and suppressed caspase-dependent apoptosis [3].
In replicatively aged skin fibroblasts, AED activated the synthesis of sirtuin-1, sirtuin-6, and collagen I [4].
Beyond cartilage and skin, AED has been examined in kidney cultures and in studies of gene regulation.
Renal Cell and Gene Expression Models
In young and aged renal cell cultures, AED increased proliferation, lowered expression of p16, p21, and p53, and raised SIRT-6 expression. Molecular modeling placed AED in the minor groove of d(ATATATATAT)2 DNA sequences [5].
In organotypic kidney tissue cultures from young and old rats, T-31 (AED) stimulated proliferation and reduced apoptosis, to a lesser degree than a kidney polypeptide complex [6].
In aging mesenchymal stem cell cultures, AED and two related short peptides were associated with a 3.5 to 5.6 fold increase in IGF1 gene expression [7]. Docking models identified the acct sequence as a DNA binding site for AED [8].
Research Area
In Vitro Application
Chondrocyte aging
Profiling p16, p21, p53, TNF-α, IL-1α, and SIRT1 in aging chondrocyte cultures
Chondrogenic differentiation
SOX9, aggrecan, type II collagen, and COMP expression in mesenchymal stem cells
Fibroblast matrix remodeling
MMP-9, collagen I, and sirtuin expression in aging fibroblast cultures
Renal cell senescence
Proliferation and apoptosis markers in kidney cell and tissue cultures
Peptide and DNA interaction
Molecular docking and gene expression studies of short peptides
References
Myakisheva SN, Linkova NS, Kozhevnikova EO, et al. (2023). [Peptides prevent the forming of secretory phenotype of chondrocytes associated with the aging.]. Advances in Gerontology, 36(2), 234–238. https://pubmed.ncbi.nlm.nih.gov/37356100/
Myakisheva SN, Linkova NS, Diatlova AS, et al. (2023). [The influence of peptides on the chondrogenic differentiation of human mesenchymal stem cells during replicative aging.]. Advances in Gerontology, 36(3), 383–390. https://pubmed.ncbi.nlm.nih.gov/37782646/
Lin’kova NS, Drobintseva AO, Orlova OA, et al. (2016). Peptide Regulation of Skin Fibroblast Functions during Their Aging In Vitro. Bulletin of Experimental Biology and Medicine, 161(1), 175–178. https://doi.org/10.1007/s10517-016-3370-x
Fridman NV, Linkova NS, Kozhevnikova EO, et al. (2020). Comparison of the Effects of KE and AED Peptides on Functional Activity of Human Skin Fibroblasts during Their Replicative Aging. Bulletin of Experimental Biology and Medicine, 170(1), 154–157. https://doi.org/10.1007/s10517-020-05022-1
Khavinson VKh, Tarnovskaia SI, Lin’kova NS, et al. (2014). [Tripeptides slow down aging process in renal cell culture]. Advances in Gerontology, 27(4), 651–656. https://pubmed.ncbi.nlm.nih.gov/25946838/
Chalisova NI, Lin’kova NS, Nichik TE, et al. (2015). Peptide Regulation of Cells Renewal Processes in Kidney Tissue Cultures from Young and Old Animals. Bulletin of Experimental Biology and Medicine, 159(1), 124–127. https://doi.org/10.1007/s10517-015-2906-9
Ashapkin V, Khavinson V, Shilovsky G, et al. (2020). Gene expression in human mesenchymal stem cell aging cultures: modulation by short peptides. Molecular Biology Reports, 47(6), 4323–4329. https://doi.org/10.1007/s11033-020-05506-3
Khavinson VKh, Lin’kova NS, Tarnovskaya SI. (2016). Short Peptides Regulate Gene Expression. Bulletin of Experimental Biology and Medicine, 162(2), 288–292. https://doi.org/10.1007/s10517-016-3596-7
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This content is provided strictly for research purposes and does not constitute an endorsement or recommendation for the non-laboratory application or improper handling of peptides designed for research. The information, including discussions about specific peptides and their researched benefits, is presented for informational purposes only and must not be construed as health, clinical, or legal guidance, nor an encouragement for non-research use. Peptides described here are solely for use in structured scientific study by authorized individuals. We advise consulting with research experts, medical practitioners, or legal counsel prior to any decisions about obtaining or utilizing these peptides. The expectation of responsible, ethical utilization of this information for legitimate investigative and scholarly objectives is paramount. This notice is dynamic and governs all provided content on research peptides.
