Antibiotic Peptides

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SRP3013 Beta D-4 human recombinant, expressed in E. coli, ≥98% (HPLC), suitable for cell culture Defensins (alpha and beta) are cationic peptides with a broad spectrum of antimicrobial activity that comprise an important arm of the innate immune system. Recombinant human BD-4 is a 6.0 kDa protein containing 50 amino acid residues.
SRP3011 Beta D-1 (36 aa) human recombinant, expressed in E. coli, ≥98% (SDS-PAGE), ≥98% (HPLC), suitable for cell culture Defensins (alpha and beta) are cationic peptides with a broad spectrum of antimicrobial activity that comprise an important arm of the innate immune system. Recombinant human BD-1 is a 3.9 kDa protein containing 36 amino acid residues.
SRP3012 Beta D-1 (47 aa) human recombinant, expressed in E. coli, ≥98% (SDS-PAGE), ≥98% (HPLC), suitable for cell culture Defensins (alpha and beta) are cationic peptides with a broad spectrum of antimicrobial activity that comprise an important arm of the innate immune system. Recombinant human BD-1 is a 5.0 kDa protein containing 47 amino acid residues.
C6830 Cecropin A ≥97% (HPLC), powder Antibacterial peptide originally identified in moths (Hyalophora cecropia) and later in pig intestine.
Cecropin A interacts with cell membranes and makes it permeable for electrolytes. Cecropin A thus, favors cytolysis and finally cell death in the hepatocellular carcinoma and lymphoma. The synthetic cecropin A in transgenic rice confers protection against bacterial as well as fungal pathogens.
C1796 Cecropin B ≥97% (HPLC), powder Antibacterial peptide originally identified in moths (Hyalophora cecropia) and later in pig intestine.
C7927 Cecropin P1 Porcine ≥95% (HPLC), powder Antibacterial peptide originally identified in moths (Hyalophora cecropia) and later in pig intestine.
Cecropin P1 can inhibit the growth of enterotoxigenic Escherichia coli in porcine. It also can inhibit the growth of human fungal pathogen Candida albicans. Cecropin P1 also blocks the release of viral particles and impairs virus-induced apoptosis. Cecropins are cationic anti-microbial peptides (AMPs). It can inactivate microorganisms by forming an α-helical chain which punctures the cell membrane. Cecropins may be used in food preservation as it is non-cytotoxic to mammalian cells.
D2043 Defensin HNP-1 human ≥80% (HPLC) Human neutrophil peptides (HNPs) is involved in endothelial cell dysfunction at the time of early atherosclerotic development. HNP 1−3 can regulate the growth of atherosclerosis. HNP 1−3 levels are usually high in inflammation, including sepsis and acute coronary vascular disorders.
This is an endogenous antibiotic peptide and monocyte chemotactic peptide produced by human neutrophils. Defensins are a family of 3-4 kDa (29-34 amino acids) peptides found in the granules of mammalian phagocytes. The members of this family are variably arginine-rich and share six conserved cysteine residues that participate in intramolecular disulfide bonds.
D6790 Defensin HNP-2 human ≥95% (HPLC) This is an endogenous antibiotic peptide and monocyte chemotactic peptide produced by human neutrophils. Defensins are a family of 3-4 kDa (29-34 amino acids) peptides found in the granules of mammalian phagocytes. The members of this famuly are variably arginine-rich and all share 6 conserved cysteine residues that participate in intramolecular disulfide bonds.
M7152 Magainin I ≥97% (HPLC) Antibiotic peptide. Thought to preferentially bind to anionic phospholipids abundant in bacterial membranes with the formation of dynamic peptide-lipid supramolecular pore and cell permeabilization, magainins are positively charged and amphiphatic. Binding to artificial neutral membranes has also been demonstrated.
Magainin is a 23-residue peptide, and is naturally found on the skin of African clawed frog. It has a broad spectrum specificity towards many gram-negative bacteria. It has the ability to make transmembrane pores on the bacterial cell membrane, which leads to cell lysis. It is considered nontoxic to mammalian cells.
M7402 Magainin II ≥97% (HPLC) Antibiotic peptide. Magainins are positively charged and amphiphatic. Thought to preferentially bind to anionic phospholipids abundant in bacterial membranes with the formation of dynamic peptide-lipid supramolecular pore and cell permeabilization. Binding to artificial neutral membranes has also been demonstrated.
Magainin II acts as an antibiotic in a variety of organisms. Magainin II exhibits cytotoxic and anti-proliferative effects via pore formation in bladder cancer cells. In mice, it acts as an anti-tumor agent in several cancer cell lines and tumors. Magainin II facilitates lactate dehydrogenase discharge from mammalian cells. It directly interacts with certain cell membranes via amphiphilic α-helix and forms permeable ion channels, which results in depolarization and irreversible cytolysis and finally cell death. At low concentrations, Magainin II retards the growth of bacterial and fungal species and it promotes cytolysis in protozoa.
SRP3126 NP-1 human recombinant, expressed in E. coli, ≥98% (SDS-PAGE), ≥98% (HPLC), suitable for cell culture Neutrophil peptide-1 (NP-1) exhibits antimicrobial activity. It also has a chemotactic function in dendritic cells. It has a role in the growth and metastasis of cancer cells. The protein acts as multifunctional co-receptor and interacts with various signaling cascades. NP-1 associates with epithelial growth factor (EGF) and its receptor (EGFR). It also interacts with hepatocyte growth factor (HGF) and its receptor c-Met.