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| Description | Citrullinated LL-37 5cit is the fully citrullinated derivative of LL-37 in which all 5 arginine residues (R7, R19, R23, R29, R34) are converted to citrulline: LLGDFF(Cit)KSKEKIGKEFK(Cit)IVQ(Cit)IKDFL(Cit)NLVP(Cit)TES (Sci Rep 2020, PMC7012854), molecular weight ~4498.2 Da, net charge reduced from +6 to +1. Full citrullination essentially abolishes the cationic character of LL-37, greatly weakening its electrostatic interactions with bacterial/viral membranes and significantly reducing its antibacterial and antiviral activities; this modified form is found in neutrophil extracellular traps (NETs) during airway inflammation and is associated with citrullinated LL-37 autoantibody/autoreactive T-cell responses in diseases such as psoriasis, systemic lupus erythematosus (SLE), and rheumatoid arthritis (PMC7345132; PMC12014627). Citrullinated LL-37 5cit is an essential tool for studying the impact of complete citrullination on host defense peptide function and autoimmunity mechanisms. |
| Molecular formula | C₂₀₉H₃₂₈N₅₂O₆₁ (approx.) |
| Molecular weight (Da) | ~4498.2 |
| Structure type | Linear 37-aa peptide (LL-37, all 5 Arg→Cit) |
| Solubility | Soluble in water and PBS |
| Storage | -20°C, dry, protected from light |
Product Basic Information Table
| Product Standard English Name | Product Abbreviation / Alias | Function Tags (comma-separated) | Core Structure | Molecular Formula | Exact Mass (Da) | Average MW (Da) | Salt Form | Length (aa) |
| Zelkovamycin | Zelkovamycin; streptomycete 16-membered cyclic peptide antibiotic | Cyclic peptide antibiotic, Gram-positive targeting, protein synthesis inhibition, antibacterial, natural product | 16-membered cyclic peptide antibiotic from Streptomyces, a ribosomally synthesized and post-translationally modified natural product; selectively binds the bacterial 50S ribosomal subunit to inhibit protein synthesis, with selective activity against Gram-positive bacteria | C₇₉H₁₁₃N₁₇O₁₃ | 1487.86 | ~1489.0 | Free peptide | 16 (cyclic peptide) |
Physicochemical Solubility & Storage Parameters
| Product Code | Appearance | Long-term Storage | Short-term Storage | Solution Stability | Solid Powder Stability |
| PEP-ZELK | White crystalline powder | Store at -20°C, sealed, dry and protected from light. Aliquot for storage. | Stable for 1 month at 2–8°C in sealed dry condition; stable for shipping at ambient temperature. | Stable for 7 days at 4°C. Soluble in methanol, DMSO and dilute acetic acid. Macrocyclic peptide is structurally stable and protease-resistant, with low polarity and poor water solubility. | Stable for 2 years at -20°C, dry and protected from light. |
Functional Description
| Product Code | Frontend Short Summary (for search list display) | Detailed Biological Function Description | Applicable Research Areas (comma-separated) | Targets / Pathways |
| PEP-ZELK | Zelkovamycin cyclic peptide antibiotic inhibiting protein synthesis | Zelkovamycin is a 16-membered macrocyclic peptide antibiotic from Streptomyces, a ribosomally synthesized and post-translationally modified natural product. It selectively binds the bacterial 50S ribosomal subunit to inhibit peptide bond formation and block protein synthesis, with selective activity against Gram-positive bacteria. | Gram-positive infections, ribosome function studies, natural cyclic peptide antibiotics, protein synthesis inhibition, antibacterial agents | Bacterial 50S ribosomal subunit; peptide bond formation inhibition; protein synthesis blockade |
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