Catalog No.
Product Name
Application
Product Information
Citations
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Antimicrobial Peptide
RW3 is a cationic antimicrobial hexapeptide that primarily targets the bacterial cytoplasmic membrane, disrupting cellular respiration and inhibiting cell wall synthesis. It demonstrates potent bioactivity against Gram-positive bacteria, including Bacillus subtilis 168, with a minimum inhibitory concentration (MIC) of 2 µg/mL. Additionally, RW3 induces morphological changes in murine erythrocytes. This reagent is suitable for applications in antimicrobial and antifungal research. -
Antimicrobial Peptide
Duramycin is an antimicrobial peptide derived from the lantibiotic produced by Streptomyces cinnamoneuma. It exhibits potent antimicrobial activity, particularly against gram-positive bacteria. Duramycin is utilized in research aimed at understanding and treating cystic fibrosis, making it a valuable reagent in studies of microbial infections and associated therapeutic strategies. -
Dipeptide Probe
EDA-DA TFA is a N-terminally tagged dipeptide probe designed for the selective labeling of bacterial peptidoglycan (PG). This compound utilizes click chemistry principles, featuring an alkyne group that facilitates copper-catalyzed azide-alkyne cycloaddition (CuAAc) reactions with azide-containing molecules. EDA-DA TFA is invaluable in bacterial research, providing insights into cell wall biochemistry and the development of antibacterial strategies. -
Protease Peptide Substrate
FA-Gly-Leu-NH2 (FAGLA) is a dipeptide substrate specifically designed for proteases. It exhibits hydrolysis by thermophilic and neutral proteases, with pH-dependent variations in catalytic efficiency (kcat/Km). This compound is primarily utilized in biochemical research to study protease activity and functionality. -
Antimicrobial Peptide
Esculentin 1A is an antimicrobial peptide derived from frog skin, specifically designed to target gram-negative bacteria. It exhibits strong in vitro activity against Pseudomonas aeruginosa, making it a valuable tool for research into antimicrobial resistance and peptide-based therapeutics. Its broad-spectrum antimicrobial properties can be applied in studies focused on infection control and novel drug development. -
Amphipathic Peptide Antibiotic
LAH4 is an amphipathic peptide antibiotic characterized by its alpha-helical structure. It demonstrates potent antimicrobial properties, along with effective nucleic acid transfection and enhanced cell penetration capabilities. LAH4 shows a strong affinity for anionic lipids present in the outer membranes of bacteria, making it a valuable tool for plasmid DNA delivery in various research applications. -
PACE4 Inhibitor
PACE4 Inhibitory Peptide C23 (Ac-(DLeu)LLLRVK-Amba) is a potent peptidomimetic compound that selectively inhibits the proprotein convertase PACE4. This peptide demonstrates significant antiproliferative effects on prostate cancer cell lines with a Ki value of 5 nM and IC50 values of 25 μM and 40 μM for DU145 and LNCaP cells, respectively. Additionally, PACE4 Inhibitory Peptide C23 is effective in suppressing tumor growth in vivo in LNCaP xenograft mouse models, making it a valuable tool for research in cancer biology and therapeutic development. -
Competence-stimulating Peptide
Competence-stimulating peptide activates the Com-dependent quorum sensing system in Streptococcus mutans. This peptide plays a crucial role in regulating competence and enhances bacteriocin production, making it a valuable tool for studies focused on microbial communication and pathogenesis. Applications include investigations into bacterial virulence, quorum sensing mechanisms, and potential therapeutic interventions against dental caries. -
Antimicrobial Peptide
Peceleganan is an artificial antimicrobial peptide comprising a hybrid of cecropin A (1-10) and melittin B (3-18). This peptide exhibits potent antimicrobial activity, making it effective in inhibiting wound infections. Its unique mechanism of action promotes the disruption of bacterial cell membranes, positioning Peceleganan as a valuable tool for research in antimicrobial strategies and wound healing applications. -
Macrocyclic Lipopeptide Antibiotic
Malacidin B is a macrocyclic lipopeptide antibiotic that exerts its antibacterial effects through a calcium-dependent mechanism. It has demonstrated significant activity against a range of Gram-positive bacteria, making it a valuable tool for researchers studying antibiotic resistance and developing new antimicrobial therapies. Its unique structure and mechanism of action provide avenues for exploring novel treatments in bacterial infections. -
Mating Pheromone-encoding Peptide
SP1 is an α-peptide encoded by the mating pheromone MFα1 gene in Candida albicans, primarily targeting the mating type locus MTLa. This compound induces cell growth arrest in Candida albicans, making it a valuable tool for investigating the mechanisms of mating and biological signaling in this organism. Additionally, SP1 is applicable in research focused on the prevention and treatment of Candida albicans infections. -
Polypeptide Antibiotics
Polymyxin B2 Sulfate is a polypeptide antibiotic that exerts its antibacterial effects primarily against gram-negative bacteria. Its mechanism of action involves binding to lipopolysaccharide molecules on the bacterial cell membrane, leading to membrane disruption and leakage of cellular contents. This compound is valuable in antibiotic development and the treatment of drug-resistant bacterial strains. -
Peptide Antibiotic
A83586C is a novel peptide antibiotic that specifically targets Gram-positive bacteria. It exhibits potent antibacterial activity, making it a valuable tool for studying bacterial infections and developing new therapeutic strategies. Its unique mode of action allows researchers to explore mechanisms of resistance and efficacy in various biological contexts. -
Antimicrobial Peptide
Bac8c is an antimicrobial peptide that targets bacterial membranes, exhibiting potent antibacterial activity against both Gram-negative and Gram-positive bacteria. Its minimum inhibitory concentrations (MIC) demonstrate effectiveness against Staphylococcus aureus, MRSA, Staphylococcus epidermidis, Escherichia coli, and Pseudomonas aeruginosa at 2, 8, 4, 4, and 4 μg/mL, respectively. Bac8c is valuable for research in antibacterial resistance and the development of novel antimicrobial therapies. -
Antibiotic Peptide
BMAP-28 is an antibiotic peptide that acts as an inducer of the mitochondrial permeability transition pore. It triggers cell death by promoting the opening of this pore, making it a valuable tool for studying microbial infections and cancer mechanisms. Researchers can utilize BMAP-28 to explore its potential therapeutic applications and the underlying processes involved in cell apoptosis. -
Antibiotic/Antimicrobial Peptide
Aurein 2.4 is an antibiotic antimicrobial peptide that primarily targets Gram-positive bacteria. It exhibits potent antibacterial activity, making it a valuable reagent for research focused on antimicrobial resistance and the development of novel antibacterial therapies. Its unique mechanism of disrupting bacterial membranes positions Aurein 2.4 as a relevant tool in studies investigating the efficacy of peptide-based antibiotics. -
Antibiotic/Antimicrobial Peptide
Aurein 5.2 is an antimicrobial peptide with potent antibiotic properties. It exhibits broad-spectrum activity against various bacterial strains, making it a valuable tool in studies related to infection control and antibiotic resistance. Its mechanism of action involves disrupting bacterial cell membranes, leading to cell lysis. Aurein 5.2 is applicable in research focused on antimicrobial development and the understanding of peptide-based therapeutics. -
Bioactive Peptide
NRC-16 is a bioactive peptide that functions as a pleurocidin-like cationic antimicrobial peptide (AMP). It exhibits potent antimicrobial activity against a range of pathogens, making it a valuable tool for research in infectious diseases and host defense mechanisms. Its unique properties facilitate studies in peptide structural biology and the development of novel antimicrobial therapies. -
antimicrobial peptides
LZ1 peptide is an antimicrobial peptide that exhibits antimalarial activity. It demonstrates the ability to inhibit the growth of Plasmodium species, making it a valuable candidate for research in malaria treatment and prevention strategies. This peptide can be utilized in studies focusing on the development of novel antimicrobial agents and the mechanisms of host-pathogen interactions. -
Tool Peptide
SP2 is a 14-amino acid synthetic tool peptide that functions by inducing growth arrest in MTLa cells of Candida albicans through modulation of cell cycle regulation. This peptide is valuable for research applications focusing on fungal biology, specifically in understanding the mating type locus and associated regulatory mechanisms. Its unique properties make it an essential reagent for studies investigating cell growth and development in yeast models. -
Antibiotic/Antimicrobial Peptide
Aurein 2.3 is an antibiotic antimicrobial peptide targeting bacterial ATPases, primarily inhibiting E. coli ATPase activity. This compound demonstrates significant antibacterial activity, effectively suppressing cell growth in susceptible bacterial strains. Aurein 2.3 serves as a valuable tool in microbiological studies and the development of new antimicrobial therapies. -
Antibiotic Peptide
Aurein 1.1 is an antibiotic peptide derived from the skin of the Australian Bell Frog (Litoria raniformis). It demonstrates potent antimicrobial activity against a variety of Gram-positive and Gram-negative bacteria. This peptide is valuable for research applications in the field of antimicrobial resistance and the development of new therapeutic agents targeting bacterial infections. -
Antibiotic Peptide
Aurein 2.1 is an antibiotic peptide derived from the skin secretions of Australian Bell Frogs, specifically Litoria aurea and Litoria raniformis. It exhibits significant antimicrobial activity against a range of bacterial strains, making it a valuable tool for research in antibiotic development and investigations into novel antimicrobial mechanisms. This peptide is of particular interest for studies related to infection control and the exploration of natural antimicrobial agents. -
Cationic antimicrobial peptide
Omiganan is a cationic antimicrobial peptide that exhibits potent activity against both gram-positive and gram-negative bacteria, as well as Candida species. As an analogue of indolicidin, Omiganan is valuable for studying its effects on microbial infections. Its applications extend to research on conditions such as acne and addressing issues related to alcohol-induced nasal problems. -
Skin-Antimicrobial Peptide
Human β-defensin-1 (HβD-1) is a cationic skin-antimicrobial peptide that targets a broad spectrum of bacteria. It is produced by various epithelial surfaces as well as circulatory and reproductive tract cells. This peptide exhibits significant antimicrobial activity, making it a valuable reagent for research applications focused on innate immunity and skin defense mechanisms. -
Polypeptide Antibiotic
Colistin is a polypeptide antibiotic primarily targeting Gram-negative bacteria. It demonstrates potent activity against multidrug-resistant strains such as Pseudomonas aeruginosa, Acinetobacter baumannii, and Klebsiella pneumoniae. Due to its nephrotoxic potential, careful consideration is required during research. Colistin is valuable for studying infections caused by Gram-negative bacilli and exploring antibiotic resistance mechanisms. -
Lipoglycopeptide Antibiotic
Dalbavancin is a semisynthetic lipoglycopeptide antibiotic targeting Gram-positive bacteria. It exhibits potent bactericidal activity, with minimal inhibitory concentrations (MIC90) of 0.06 μg/mL against Staphylococcus aureus and 0.25 μg/mL against Bacillus anthracis. This compound is primarily utilized in research applications focused on bacterial infections and the development of novel antimicrobial therapies. -
Polypeptide Antibiotics
Polymyxin B2 is a polypeptide antibiotic that primarily targets the cell membrane of gram-negative bacteria. It exerts its antibacterial effect by binding to lipopolysaccharide components, leading to membrane disruption and subsequent cell lysis. This compound is relevant for antibiotic research and development, particularly in addressing drug-resistant bacterial strains. -
Antibiotic Peptide
Aurein 1.2 is an antibiotic peptide derived from amphibian sources, exhibiting potent antimicrobial and anticancer properties. This peptide targets bacterial membranes, leading to disruption and cell death, making it valuable in the study of antibiotic resistance and cancer therapeutics. Aurein 1.2 is ideal for research applications focused on the development of novel antimicrobial agents and exploring mechanisms of cancer cell apoptosis. -
Glycopeptide Antibiotic
A40926 is a glycopeptide antibiotic that targets the bacterial cell wall peptidoglycan precursor D-alanyl-D-alanine (D-Ala-D-Ala). It functions by irreversibly inhibiting cell wall synthesis through competitive binding, demonstrating significant bactericidal activity against Gram-positive bacteria, including Staphylococcus and Streptococcus, as well as Neisseria gonorrhoeae, with MIC values ranging from 0.06 to 2 μg/mL. Additionally, A40926 is effective against penicillin-resistant strains, disrupting peptidoglycan cross-linking and leading to bacterial lysis and death. The compound's fat-soluble fatty acid structure enhances serum concentrations and extends its duration of action, with a terminal half-life of 61.22 hours in rats. -
Antibiotic Peptide
Dermcidin-1L (human) is an antibiotic peptide that targets microbial pathogens with its inherent antimicrobial activity. Secreted by sweat glands, it plays a crucial role in skin defense mechanisms. Research applications include studies of inflammatory skin disorders and the investigation of innate immune responses. -
Lipopeptide Antibiotic
Globomycin is a lipopeptide antibiotic that acts as an irreversible inhibitor of signal peptidase II (LspA). By binding to the peptidase, Globomycin disrupts the processing of prolipoproteins, demonstrating significant antibacterial activity against the mollicute Spiroplasma melliferum with a minimum inhibitory concentration (MIC) of 6.25-12.5 μM. This compound is valuable for research applications focused on bacterial protein processing and antibiotic resistance mechanisms. -
Glycopeptide Antibiotic
Chloroorienticin A is a glycopeptide antibiotic that inhibits bacterial cell wall synthesis by targeting the transglycosylation activity in gram-positive bacteria. This compound demonstrates potent antibacterial activity against staphylococci and streptococci, making it a valuable tool for research on antibiotic resistance and bacterial pathogenesis. Its efficacy in inhibiting the growth of these pathogens supports its use in studying the mechanisms of antibiotic action and resistance development in clinical strains. -
Glycopeptide Antibiotic
Phleomycin D1 is a glycopeptide antibiotic that targets DNA. It exerts its biological activity by binding to and cleaving DNA, leading to cell death. Additionally, Phleomycin D1 induces cell cycle arrest at the S phase, making it a valuable reagent for research applications in cancer biology and molecular genetics. -
Antifungal Peptide
Pezadeftide is a potent antifungal peptide that targets fungal cells by inducing a rapid mitochondrial response. This mechanism leads to hyperpolarization of the mitochondrial membrane, disrupting cellular function and contributing to antifungal activity. Pezadeftide is valuable for studying antifungal resistance and developing therapeutic strategies against fungal infections. -
Antibacterial Peptide
D2A21 is an antibacterial peptide derived from cecropins that exhibits potent antimicrobial activity. It has a minimum cidal concentration of 21.69 μg/mL against Chlamydia trachomatis, demonstrating its effectiveness in combating bacterial infections. This peptide is valuable for research applications aimed at developing novel antimicrobial therapies and studying bacterial resistance mechanisms. -
Glycopeptide Antibiotic
Balhimycin is a glycopeptide antibiotic that inhibits bacterial cell wall synthesis by binding to the D-alanine-D-alanine termini of precursor units. This compound exhibits potent antibacterial activity against strains of staphylococci and various anaerobic bacteria, making it valuable in the study of antibiotic resistance and infection management. Its application extends to research focused on the mechanisms of antibacterial action and the development of novel therapeutic agents. -
Herbicide
N-Acetyldemethylphosphinothricin tripeptide is a prodrug herbicide targeting amino acid biosynthesis in plants. Comprising the unique amino acid phosphinothricin and two alanine residues, this compound exhibits significant herbicidal activity by inhibiting the biosynthetic pathway of glutamine and glutamate. Its ability to penetrate bacterial cells via peptide uptake systems enhances its efficacy, making it a valuable tool in agricultural research and development related to herbicide mechanisms and plant growth regulation. -
Polypeptide
LL-37 SKE is a bioactive fragment of the human cathelicidin peptide LL-37, functioning primarily as an antimicrobial peptide. It exhibits significant antibacterial, antifungal, and antiviral properties, making it valuable for research in innate immunity and host defense mechanisms. LL-37 SKE is employed in studies exploring the modulation of immune responses and the development of therapeutic interventions for infectious diseases. -
Antibiotic/Antimicrobial Peptide
Aurein 3.2 is an antimicrobial peptide that exhibits potent antibiotic activity against a range of bacterial pathogens. In addition to its bactericidal properties, Aurein 3.2 demonstrates anticancer activity, making it a valuable compound for research in both infectious disease and cancer therapeutics. Its unique mechanism of action and dual functionality make it an important tool for exploring therapeutic applications in microbiology and oncology. -
Skin-Antimicrobial Peptide
Human β-defensin-2 (HβD-2) is a cysteine-rich cationic skin-antimicrobial peptide that primarily targets microbial pathogens. It exhibits significant antimicrobial activity against gram-negative bacteria and Candida species, while demonstrating limited efficacy against gram-positive Staphylococcus aureus. This peptide is valuable for research applications assessing its role in antimicrobial defense, particularly in models of colitis and skin-related disorders. -
Peptide
Urofollitropin is a recombinant form of follicle-stimulating hormone (FSH) targeting the follicle development pathway. It plays a crucial role in stimulating ovarian follicle maturation, making it essential for reproductive research and assisted reproductive technologies. Urofollitropin's biological activity supports studies in fertility treatments and the regulation of reproductive endocrinology. -
Antibacterial peptide
LL-37 GKE is an antibacterial peptide derived from the active domain of LL-37. It exhibits significant antibacterial activity, making it a valuable candidate for research in antibiotic development. LL-37 GKE’s properties offer potential applications in the study of infection control and the enhancement of antimicrobial therapies. -
Antimicrobial Peptide
Brevinin-1 is an antimicrobial peptide that targets microbial membranes. Isolated from the skin secretions of Rana esculenta, it demonstrates potent antibacterial and antifungal activity. Brevinin-1 is useful in microbiological studies and the development of novel antimicrobial treatments. -
Antibiotic/Antimicrobial Peptide
Aurein 3.1 is an antibiotic antimicrobial peptide that exhibits notable activity against Gram-positive bacteria. It demonstrates a minimum inhibitory concentration (MIC) of 80 μM against Micrococcus luteus and 50 μM against Staphylococcus aureus, Staphylococcus epidermidis, Streptococcus mutans, and Bacillus subtilis. Aurein 3.1 is valuable for research applications focused on combating bacterial infections and studying antimicrobial mechanisms. -
Antibiotic/Antimicrobial Peptide
Aurein 3.3 is an antimicrobial peptide with potent antibiotic properties. It exhibits a dual mechanism of action, targeting bacterial membranes and disrupting cellular integrity. Additionally, Aurein 3.3 demonstrates anticancer activity, making it a valuable resource for research into antimicrobial therapeutics and cancer biology. Its unique properties allow for diverse applications in the study of microbial resistance and cancer treatment strategies. -
Antibiotic/Antimicrobial Peptide
Aurein 2.2 is an antimicrobial peptide that exhibits broad-spectrum antibacterial activity, primarily targeting Gram-positive bacteria including Staphylococcus aureus and S. epidermidis. Isolated from the skin secretions of L. aurea, Aurein 2.2 demonstrates potential as an effective antibiotic, making it a valuable tool for research in microbiology and antimicrobial therapy. Its unique mechanism of action and efficacy against resistant strains underline its relevance in the study of infection control and antibiotic development. -
Peptide Antibiotic
Angiotensin III antipeptide is a peptide antibiotic that inhibits the activity of angiotensin II, a key regulator in the renin-angiotensin system. It exhibits biological activity by modulating blood pressure and fluid balance, making it a valuable tool in cardiovascular and renal research. Its applications include studying the effects of angiotensin peptides on physiological processes and exploring potential therapeutic interventions in related diseases. -
Antibiotic/Antimicrobial Peptide
Aurein 2.6 is an antimicrobial peptide that primarily targets Gram-positive bacteria. It exhibits significant antibacterial activity, with minimum inhibitory concentrations (MIC) of 25 to 30 μM against various strains, including Micrococcus luteus, Staphylococcus aureus, Staphylococcus epidermidis, Streptococcus mutans, and Bacillus subtilis. Aurein 2.6 is valuable for research applications involving antibiotic resistance studies and the development of new antimicrobial agents. -
Peptide Antibiotic
Clavanin A is a peptide antibiotic that disrupts the integrity of the cytoplasmic membrane in target cells. It demonstrates effective bactericidal activity against Micrococcus flavus, making it a valuable tool for studying bacterial membrane dynamics and antibiotic mechanisms. Researchers can utilize Clavanin A for investigations into microbial resistance and the development of new antimicrobial strategies.
