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| Description | KR-12 human (CAS: 1218951-51-9) is a 12-residue synthetic C-terminally amidated fragment corresponding to residues 18-29 of the human cathelicidin LL-37, sequence Lys-Arg-Ile-Val-Gln-Arg-Ile-Lys-Asp-Phe-Leu-Arg-NH2. Molecular formula C71H127N25O15, MW 1570.93 Da. KR-12 is the shortest known LL-37 fragment retaining independent antimicrobial activity, with an MIC of ~66 uM against E. coli K-12. Compared with full-length LL-37, KR-12 retains anti-Gram-negative activity but shows markedly reduced hemolytic and cytotoxic activity against mammalian red blood cells. KR-12 is a core tool for the minimal LL-37 pharmacophore and low-toxicity human-derived antimicrobial peptidomimetics. |
| Structure type | Linear 12-mer (C-amidated human LL-37 18-29 minimal active fragment) |
| Solubility | Readily soluble in water, dilute acetic acid |
| Storage | Powder -20C, 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) |
| KR-12 (human) | KR-12; KRIVQRIKDFLR-NH2; LL-37 (18-29); human cathelicidin LL-37 core fragment; hCAP18-derived peptide | human antimicrobial peptide, LL-37 fragment, alpha-helical peptide, C-terminal amidated, cationic amphipathic peptide, anti-Gram-negative, anti-biofilm, immunomodulatory, antitumor, short AMP | Linear 12-aa cationic alpha-helical peptide, sequence KRIVQRIKDFLR (Lys-Arg-Ile-Val-Gln-Arg-Ile-Lys-Asp-Phe-Leu-Arg), corresponding to residues 18-29 of human cathelicidin LL-37 (hCAP18/LL-37), the minimal antimicrobial core; C-terminal Arg amidated; 3 Arg + 2 Lys vs 1 Asp plus free N-terminus, net charge ~+5; ~42% hydrophobic residues (Ile/Val/Ile/Phe/Leu); no Cys, no disulfide, no Met, no Trp, no His; amphipathic alpha-helix, high cationic charge enhances Gram-negative outer membrane penetration | C71H127N25O15 | 1569.99 | 1570.96 | TFA (trifluoroacetate); formula and MW calculated for free peptide (with C-terminal amide) | 12 |
Physicochemical Solubility & Storage Parameters
| Product Code | Appearance | Long-term Storage | Short-term Storage | Solution Stability | Solid Powder Stability |
| PEP-KR12-01 | White powder | -20°C, desiccated and sealed; no Cys/Met/Trp/His so high chemical stability; store dry; avoid repeated freeze-thaw | 2-8°C, desiccated, stable for several weeks | Highly cationic amphipathic peptide (net charge +5) with strong hydrophilicity; good aqueous solubility, directly soluble in sterile ultrapure water or neutral/weakly acidic buffers; solution stable at low concentrations; prepare fresh or aliquot and store at -20°C; no Trp so no strict light protection needed | solid is stable with no oxidizable residues; highly charged hydrophilic peptide is not hygroscopic; store dry and sealed |
Functional Description
| Product Code | Frontend Short Summary | Detailed Biological Function Description | Applicable Research Areas (comma-separated) | Targets / Pathways |
| PEP-KR12-01 | A 12-aa antimicrobial core fragment of human cathelicidin LL-37 (residues 18-29, KRIVQRIKDFLR-NH2), C-terminally amidated, net charge +5; the shortest bioactive LL-37-derived peptide, with broad-spectrum antibacterial, anti-biofilm and immunomodulatory activity and low mammalian cytotoxicity. | KR-12 is a 12-residue peptide corresponding to the N-terminal proximal core region (residues 18-29, KRIVQRIKDFLR) of human LL-37 (hCAP18/LL-37), the sole human cathelicidin antimicrobial peptide. It is one of the shortest LL-37-derived fragments that retains appreciable antimicrobial activity. LL-37 is constitutively stored in the secondary granules of neutrophils and is also inducibly expressed by epithelial cells during inflammation, serving as a key effector molecule of innate immunity. KR-12 preserves the amphipathic alpha-helical character of LL-37, and C-terminal amidation further enhances its cationic character (net charge +5) and membrane activity. Compared to full-length LL-37, KR-12 is shorter, cheaper to synthesize, and exhibits markedly lower mammalian cytotoxicity (no significant toxicity against normal mammalian cells up to 128 µg/mL), while retaining activity against Gram-negative bacteria (Escherichia coli, Pseudomonas aeruginosa) and some Gram-positive strains (Staphylococcus aureus). Beyond direct bacterial killing, KR-12 displays anti-biofilm activity, immunomodulatory effects (leukocyte chemotaxis, cytokine modulation), and anti-proliferative activity against tumor cells. Because KR-12 is derived from a human self-peptide, it has low immunogenicity, making it an attractive lead for novel anti-drug-resistant infection therapies and local anti-infective applications (e.g., skin wounds, pulmonary infections, orthopedic implant-associated infections). KR-12 and its lipidated derivatives have been extensively studied to improve protease resistance and cell selectivity. | human AMP biology, LL-37/cathelicidin research, anti-drug-resistant infection, anti-biofilm strategies, innate immunity, immunomodulatory peptides, novel antibiotic lead discovery, skin/pulmonary anti-infective therapy | bacterial cytoplasmic membrane (anionic phospholipids), Gram-negative outer membrane, biofilm matrix, immune cell chemotaxis receptors |
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