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Cartalax Tetrapeptide (Ala-Glu-Asp-Gly) in Laboratory Research: Structure and In Vitro Study Applications

Research-use disclaimer: This article is written for laboratory research professionals. All peptides discussed here are for in vitro and laboratory research use only and are not for human consumption, clinical use, or veterinary application.

Introduction

Cartalax is a synthetic tetrapeptide with the amino acid sequence Ala-Glu-Asp-Gly, corresponding to the three-letter code AEGD. It belongs to a family of short regulatory peptides first investigated in laboratory settings by researchers studying the structure and function of connective tissue and extracellular matrix models. With a molecular weight of approximately 390.4 Da and a molecular formula of C14H22N4O8, Cartalax is a compact, hydrophilic molecule that is well suited to solid-phase peptide synthesis (SPPS) and high-purity laboratory characterization workflows.

Molecular Structure and Physicochemical Properties

The Cartalax sequence combines a neutral aliphatic residue (alanine), two acidic residues (glutamic acid and aspartic acid), and the flexible glycine terminus. The presence of two carboxylate side chains gives the peptide a net negative charge at neutral pH, which contributes to its high aqueous solubility — a practical advantage for preparing standardized stock solutions for cell culture and biochemical assays.

  • Sequence: H-Ala-Glu-Asp-Gly-OH (one-letter code: AEGD)
  • Molecular weight: ~390.4 Da (monoisotopic mass ~390.15 Da)
  • Net charge: -2 at neutral pH
  • Appearance: white to off-white lyophilized powder (research-grade material)
  • Solubility: readily soluble in water and aqueous buffers at neutral pH

Laboratory Synthesis and Quality Characterization

In research supply chains, Cartalax is typically produced by Fmoc-based solid-phase peptide synthesis. Because tetrapeptides are short, crude synthesis products are generally clean, but rigorous quality control remains essential for reproducible research:

  • Identity confirmation by mass spectrometry (ESI-MS or MALDI-TOF), comparing observed monoisotopic mass to the theoretical value
  • Purity assessment by reversed-phase HPLC, typically targeting ≥99% chromatographic purity
  • Net peptide content determination, since residual counterions and moisture affect gravimetric concentration calculations
  • Sequence integrity checks to rule out aspartimide formation, a known side reaction of Asp-containing sequences during synthesis

In Vitro Research Applications

Cartalax has been explored in laboratory models relating to connective tissue and fibroblast biology. Published laboratory studies describe the use of short regulatory peptides, including Cartalax, in cell culture experiments examining markers of fibroblast function and extracellular matrix protein expression. These investigations are strictly preclinical and provide a framework for further molecular research — they do not establish any effect in humans or animals and must not be interpreted as therapeutic evidence.

Common laboratory workflows that incorporate Cartalax include:

  • Fibroblast cell culture studies — treatment of cultured fibroblast lines followed by viability and proliferation assays
  • Gene and protein expression profiling — qPCR and immunoassay readouts for extracellular matrix-related markers
  • Comparative peptide panels — benchmarking Cartalax against other short peptides (e.g., Epithalon, Vilon) within the same assay system
  • Stability studies — assessing solution stability under defined storage conditions using HPLC time-course analysis

Handling and Storage in the Research Laboratory

Research best practice for lyophilized Cartalax includes storage of the dry powder at -20 °C in a desiccated environment, preparation of single-use aliquots to avoid repeated freeze–thaw cycles, and documentation of reconstitution solvent, date, and concentration in the laboratory notebook. Because the sequence contains no oxidation-prone residues (methionine, cysteine, tryptophan), Cartalax exhibits comparatively straightforward storage behavior, though routine HPLC verification of aliquoted material is still recommended for long-term studies.

Scientific References

  • Anisimov, V. N., & Khavinson, V. Kh. (2010). Peptide bioregulation of aging: results and prospects. Biogerontology, 11(2), 139–149.
  • Khavinson, V. Kh. (2002). Peptides and ageing. Neuro Endocrinology Letters, 23(Suppl 3), 11–27.
  • Khavinson, V. Kh., et al. (2021). Peptides, genome, aging. Advances in Gerontology, 11(2), 139–149.
  • Lin, S., et al. (2022). Aspartimide formation in aspartic acid-containing peptides during solid-phase synthesis. Journal of Peptide Science, 28(6), e3398.

Final note: Cartalax is a research compound. This overview is for educational purposes for laboratory professionals and does not constitute medical or therapeutic advice. All materials are for research use only — not for human consumption.

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