New Bacterial Toxins Available
The Native Antigen Company offers a range of highly purified bacterial toxins for use in a wide range of applications, including cell biology, assay development, and studying pathways in diseases such as cardiovascular disorders, cancer and diabetes. In addition to our established range, we now offer new toxins for Bordetella pertussis, Group A Streptococcus and Pasteurella multocida.
New: Bordetella Pertussis Adenylate Cyclase
- Active recombinant Bordetella pertussis toxin of Tohama strain.
- Expressed in E. coli from structural gene cyaA and its activator gene cyaC.
- Purified by calmodulin-sepharose 4B chromatography.
- Greater than than 90% purity by SDS-PAGE.
- Addition to medium significantly increases levels of cellular cAMP.
About this toxin
Adenylate cyclase toxin is a virulence factor produced by some members of the genus Bordetella. Together with the pertussis toxin it is the most important virulence factor of the causative agent of whooping cough, Bordetella pertussis.
New: Streptococcus Streptolysin O
- Active recombinant Streptolysin O toxin.
- Purified from E. coli to greater than 98% (by SDS-PAGE).
- Presented in PBS (-), 1 mM DTT, 50% glycerol, sterilized by filtration, with no additive nor carrier protein.
About this toxin
Streptolysin O (SLO) is part of the thiol-activated cytolysin family. It is hemolytically active only in a reversibly reduced state, interacting with cholesterol in the membrane of eukaryotic cells and usually results in β-hemolysis under the surface of blood agar. SLO targets myocardial cells, epithelial cells, platelets, and neutrophils and is thought to prevent the host immune system from clearing infection. The cytotoxic effects of SLO may also protect GAS from phagocytic killing and enhance bacterial virulence, particularly of strains that may be relatively deficient in hyaluronic acid capsule.
New: Pasteurella Multocida Toxin
- Active recombinant Pasteurella multocida toxin.
- Expressed in E. coli from the ToxA with N-terminal 6xHis-tag.
- >90% purity by SDS-PAGE (CBB staining).
- Mouse embryonic cells (Swiss 3T3) were treated with PMT at 10 ng/ml at 37℃ for 18 h. Foci formation by aggregation of cells is observed.
About this toxin
P. multocida toxin (PMT) activates various heterotrimeric G proteins and substrates of the toxin. PMT is a 146-kDa toxin, comprising different domains that are involved in cellular uptake and intracellular action: The receptor-binding and translocation domains are located in the N-terminus (1-574aa). So far, the cell surface receptor of PMT is not known, though it can be used as a transporter to carry a fusion non-cell-permeating protein (DTa) into the cytosol of host cells.
Bordetella Pertussis Toxin
About this product
- Native active Bordetella pertussis toxin, strain ACTC 9797.
- >98% purity by SDS-PAGE.
- Presented in lyophilised, frozen and glycerol formats.
- Double-round FHA removal and validation in CHO cell assay.
About this toxin
Pertussis toxin (PTX) is a 105kDa oligomer composed of 6 subunits (named S1-5, with two copies of S4), making it one of the most complex bacterial toxins known. PTX’s subunits are organized in an A-B structure, whereby S1 comprises the enzymatic A domain and subunits S2-5 comprise the B domain in a pentameric ring. By modulating cAMP activity, PTX is able to disrupt cellular signalling mechanisms and prevent a robust immune response. One of the common effects of B. pertussis infection is a build-up of cAMP in phagocytes, which inhibits typical immune responses to bacterial infection, such as phagocytosis and induction of nitric oxide synthesis.
Bordetella Pertussis FHA
About this product
- Native Bordetella pertussis filamentous haemagglutinin (FHA), strain ACTC 9797.
- >98% purity by SDS-PAGE.
- 95% original form, with 5% product breakdown.
- Presented lyophilized in Tris-HCL buffer, pH 8.5.
About this toxin
As a cell surface protein of Bordetella pertussis, FHA functions as an adhesin. FHA is often used in combination with pertussis toxin for diagnostic screening purposes, whereas highly pure B. pertussis toxin alone is used predominantly for the monitoring of vaccination programmes.
Clostridium Difficile Toxin A
About these products
- Native active C. difficile toxin A, strain VPI10463, ribotypes 027 and 078.
- Greater than 95% purity by SDS-PAGE.
- Presented in 0.05M hepes, 0.15M NaCl, 5% sucrose.
- Activity tested on Vero cells.
About this toxin
C. diff toxin A (TcdA) is a 308kDa protein, comprising for major functional domains: ABCD. The N-terminal domain (domain A) is biologically active and contains the glucosyltransferase (GT) activity responsible for modifying target proteins; The C-terminal domain (domain B) is thought to be responsible for cell surface receptor recognition and binding; Domain C is an autoprotease (APD) domain that facilitates cleavage and the release of domain A; Domain D is likely involved in the delivery (TD) of the toxins from the endosome to the cytosol.
Clostridium Difficile Toxoid A
About this product
- Native Clostridium difficile Toxoid A, strain VPI10463.
- Inactivated with formaldehyde, with inactivation conferred by vero cell assay.
- Greater than 90% purity by SDS-PAGE
- Presented in 0.05M hepes, 0.15M NaCl, 5% sucrose.
About this toxin
C. diff toxin A (TcdA) is a 308kDa protein, comprising for major functional domains: ABCD. The N-terminal domain (domain A) is biologically active and contains the glucosyltransferase (GT) activity responsible for modifying target proteins; The C-terminal domain (domain B) is thought to be responsible for cell surface receptor recognition and binding; Domain C is an autoprotease (APD) domain that facilitates cleavage and the release of domain A; Domain D is likely involved in the delivery (TD) of the toxins from the endosome to the cytosol.
Clostridium Difficile Toxin B
About these products
- Native active C. difficile Toxin B, strain VPI10463, ribotypes 027 and 078.
- Greater than 95% purity by SDS-PAGE.
- Presented in 0.05M hepes, 0.15M NaCl, 5% sucrose.
- Activity tested on Vero cells.
About this toxin
C. diff toxin B (TcdB) is a 270kDa protein, comprising for major functional domains: ABCD. The N-terminal domain (domain A) is biologically active and contains the glucosyltransferase (GT) activity responsible for modifying target proteins; The C-terminal domain (domain B) is thought to be responsible for cell surface receptor recognition and binding; Domain C is an autoprotease (APD) domain that facilitates cleavage and the release of domain A; Domain D is likely involved in the delivery (TD) of the toxins from the endosome to the cytosol.
Clostridium Difficile Toxoid B
About this product
- Native Clostridium difficile Toxoid B, strain VPI10463.
- Inactivated with formaldehyde and validated by Vero cell assay.
- Greater than 95% purity by SDS-PAGE.
- Presented in 0.05M hepes, 0.15M NaCl, 5% sucrose.
About this toxin
C. diff toxin B (TcdB) is a 270kDa protein, comprising for major functional domains: ABCD. The N-terminal domain (domain A) is biologically active and contains the glucosyltransferase (GT) activity responsible for modifying target proteins; The C-terminal domain (domain B) is thought to be responsible for cell surface receptor recognition and binding; Domain C is an autoprotease (APD) domain that facilitates cleavage and the release of domain A; Domain D is likely involved in the delivery (TD) of the toxins from the endosome to the cytosol.
Diphtheria Toxin
About this product
- Native active toxin from C. diphtheriae, strain NCTC 10648.
- Greater than 98% purity by SDS-PAGE.
- Each batch is activity tested in a DEREG mouse model system.
- Lyophilised in 0.01 M Tris and 0.001 M Na2EDTA, 0.05% D-lactose, pH 7.5.
About this toxin
Diphtheria toxin (DT) is a potent exotoxin and member of the family of ADP-ribosylating bacterial toxins. DT is secreted by strains of the gram-positive bacterium C. diphtheriae carrying a lysogenic bacteriophage, which contains the toxin gene. The toxin is secreted as a single polypeptide chain of 535 amino acids containing two major functional domains, known as domains A and B: The amino terminal A domain (1-193) carries the catalytic domain for ADP-ribosylation of elongation factor 2 (EF2); The carboxyl terminal B domain (194-535) is further divided into receptor (R) binding and transmembrane (T) domains. The B domain promotes binding of DT to cells, the internalization of DT by receptor-mediated endocytosis and the entry of the A polypeptide chain into the cytosolic compartment.
Diphtheria Toxin, CRM197 Mutant
About this product
- Expressed in the cytoplasm of E. coli as a soluble, correctly folded ~58kDa recombinant protein.
- Manufactured to >99% purity, <1% dimer by SEC HPLC, endotoxin levels <10 EU/mg.
- Lyophilised and presented in 100mM NaC1, 20mM HEPES pH8.0, 10% glycerol.
About this toxin
Diphtheria toxin CRM197 mutant is a recombinant, genetically detoxified diphtheria toxin. It contains a single base change in the structural gene resulting in the substitution of glutamic acid for glycine which blocks ADP-ribosylation. CRM197 has no enzymatic activity but is immunologically indistinguishable from diphtheria toxin. CRM197 is widely used as a carrier protein in conjugate vaccines, including effective conjugate vaccines against Streptococcus pneumoniae, Haemophilus influenzae b and Neisseria meningitidis (meningococcus).
Diphtheria Toxoid
About this product
- Native active toxin from C. diphtheriae, strain NCTC 10648.
- >98% pure by SDS-PAGE.
- Presented frozen in 0.01 M Tris pH 7.5 and 0.001 M Na2EDTA.
- Inactivated by incubation with formaldehyde for 3-weeks.
- Cytotoxicity assay used to confirm loss of activity by measuring its effect on cell viability in Chinese Hamster Ovary (CHO) cells.
About this toxin
Diphtheria toxin (DT) is a potent exotoxin and member of the family of ADP-ribosylating bacterial toxins. DT is secreted by strains of the gram-positive bacterium C. diphtheriae carrying a lysogenic bacteriophage, which contains the toxin gene. The toxin is secreted as a single polypeptide chain of 535 amino acids containing two major functional domains, known as domains A and B: The amino terminal A domain (1-193) carries the catalytic domain for ADP-ribosylation of elongation factor 2 (EF2); The carboxyl terminal B domain (194-535) is further divided into receptor (R) binding and transmembrane (T) domains. The B domain promotes binding of DT to cells, the internalization of DT by receptor-mediated endocytosis and the entry of the A polypeptide chain into the cytosolic compartment.
Cholera Toxin, Subunit B
About this product
- Recombinant Vibrio cholerae serotype 01 toxin, subunit B, comprising amino acids 22-124 (NCBI Accession Number: P01556).
- Expressed in HEK293 cells with a C-terminal His-tag.
- Greater than 90% purity by SDS-PAGE.
About this toxin
Cholera toxin is an oligomeric complex made up of six protein subunits: a single copy of the A subunit and five copies of the B subunit. Subunit B binds to the cell surface via GM1 gangliosides on the surface of target cells. Once bound, the entire toxin complex is endocytosed by the cell and the cholera toxin A1 (CTA1) chain is released by the reduction of a disulfide bridge. Once inside the cell subunit A activates G protein which then activates adenylate cyclase, eventually leading to enhanced efflux of chloride ions from the intestinal cells, and rapid water loss via the intestine. Cholera toxin subunit B (CTXB) has been used as a marker for neuronal cells due to its high affinity for the GM1 ganglioside cell surface receptor on these cells. CTXB has no toxic activity by itself, and can therefore be used in cell culture.
Tetanus Toxoid, Heavy Chain Fragment C
About this product
- Carboxyl fragment of tetanus toxin heavy chain expressed in the cytoplasm of E. coli as a properly-folded, soluble protein.
- Purified in 20mM HEPES, l00mM NaCl, 10% glycerol, pH7.2.
- Manufactured to >98% purity by SEC HPLC.
About this toxin
Tetanus toxoid (TT) is frequently used as a carrier protein for conjugate vaccines, in addition to being a component of the DPT vaccine. TT contains strong T cell epitopes. However, as a toxoided protein, many of the surface lysines are blocked by the toxoiding process. Furthermore, TT is not a uniform product, since each manufacturer has its own specific toxoiding and purification process. Tetanus toxoid also tends to aggregate with age and is not generally affordable in the quantities needed for research and early clinical work. Recombinant TT combines the advantages of the toxoid with the reproducibility of a recombinant protein.