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| Description | Balteatide is an antimicrobial peptide that can be found in the skin secretion of Phyllomedusa baltea (MCE, CAS 1630816-52-2). Its sequence is Leu-Arg-Pro-Ala-Ile-Leu-Val-Arg-Ile-Lys-NH2 (one-letter: LRPAILVRIK-NH2, 10 aa, C-terminally amidated), belonging to the family of cationic short-chain host defense peptides from amphibian skin. Molecular formula C55H104N18O10, molecular weight 1177.53 Da. Consistent with the amphibian skin antimicrobial peptide family, Balteatide exerts broad-spectrum antibacterial activity by electrostatically binding and disrupting bacterial cell membranes, making it a valuable tool for studying the amphibian skin immune defense system and developing novel antimicrobial peptide drugs. Widely used in antimicrobial peptide research, host defense peptide function studies, and novel antibacterial agent development. |
| Molecular formula | C₅₅H₁₀₄N₁₈O₁₀ |
| Molecular weight (Da) | 1177.53 |
| Structure type | Linear 10-aa peptide (C-terminally amidated, cationic short peptide) |
| Solubility | Freely 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) |
| Hc-CATH | Sea snake cathelicidin AMP; Hydrophis curtus-derived AMP | Antimicrobial peptide, broad‑spectrum antibacterial, endotoxin‑neutralizing, anti‑inflammatory, immunomodulation | Cathelicidin‑family AMP from Hydrophis curtus, with a cationic amphipathic α‑helical structure; potent broad‑spectrum bactericidal activity, neutralizes endotoxin LPS, inhibits the TLR4 inflammatory pathway, with pronounced anti‑inflammatory effects | C₁₇₆H₂₉₅N₅₁O₄₂S | 3854.23 | ~3856.8 | Acetate | 30 |
Physicochemical Solubility & Storage Parameters
| Product Code | Appearance | Long-term Storage | Short-term Storage | Solution Stability | Solid Powder Stability |
| PEP-HCCATH | White 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 dilute acetic acid and acidic buffers. α-helix has strong LPS binding capacity for endotoxin neutralization, active over a broad pH range. | 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-HCCATH | Hc-CATH sea snake peptide with potent antibacterial, endotoxin-neutralizing and anti-inflammatory activity | Hc-CATH is a cathelicidin family antimicrobial peptide from Hydrophis curtus, forming a cationic amphipathic α-helix. It has potent broad-spectrum bactericidal activity against Gram-positive, Gram-negative and drug-resistant bacteria, and also neutralizes endotoxin LPS to block the TLR4/NF-κB inflammatory pathway and inhibit cytokine storm, combining antibacterial and anti-inflammatory dual activities. | Sepsis & endotoxin research, anti-infective & anti-inflammatory peptides, cathelicidin family, marine natural products, immune regulation | LPS endotoxin neutralization; TLR4/NF-κB inflammatory pathway; broad-spectrum bacterial killing |
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