ADENYLATE CYCLASE TOXIN AND ADENYLATE CYCLASE ANTIGEN

Adenylate cyclase toxin (ACT) is an important virulence factor secreted by Bordetella pertussis. When a lung infection is underway, ACT interacts with tracheal epithelial cells, inserting itself into cytoplasmic membranes, aiding the adhesion of bacteria to the airway lining.  Host phagocytes responding to the site of infection are disabled by cAMP generated by ACT.  Encoded by the Bordetella pertussis cyaA gene, adenylate cyclase toxin is single 1706 amino acid polypeptide, with an apparent molecular weight of 220 kDa.  The N-terminal of this protein contains an adenylate cyclase domain which binds to host cell calmodulin and catalyzes unregulated conversion of cellular ATP to cAMP.  The C-terminal, receptor binding domain, contains numerous repeat in toxin (RTX) motifs and is responsible for binding to the cellular receptor on the surface of immune cells, translocation to the cell cytosol and creating cation-selective pores in the host cell membrane.

Adenylate cyclase toxin both suppresses and modulates the host immune system contributing to pathogenesis of B. pertussis.  This toxin is unusual in its ability to cross mammalian cell membranes and locate within the cytosol.  As a cell biology tool, adenylate cyclase has been used to deliver immunogenic epitopes, targeting antigen presenting cells.  ACT, product #188, and 188L are available from List Labs is an active enzyme, produced as a recombinant protein in E. coli.  These two adenylate cyclase products differ in that #188 is freeze dried and #188L is liquid.

A non-enzymatic, genetically detoxified ACT toxoid (CyaA-AC^–) has been produced. Although the catalytic activity in this toxoid is destroyed, it is still cell invasive and able to induce an immune response to co-administered pertussis antigens.  This toxoid has been shown to be capable of delivering vaccine antigens into the cytosol of major histocompatibility complex (MHC) class I antigen-presenting cells. CyaA-AC^– toxoid has been used as a tool to deliver antigens to T cells in anti-cancer immunotherapeutic vaccines.  Samples are available of the genetically detoxified CyaA-AC^– toxoid (Product #198L) and of an especially low endotoxin preparation of Adenylate Cyclase Toxin, Recombinant (Product #197L).

Bordetella pertussis virulence factors derived from native organisms and offered by List Labs, include Pertussis Toxin, Pertussis Toxin Subunits, Pertussis Toxin Mutant, Filamentous Hemagglutinin (FHA), Fimbriae 2/3, Pertactin (69 kDa protein), and B. pertussis Lipopolysaccharide (LPS).   More information about each of these products may be obtained through the links on the Pertussis Toxins and Virulence Factors.

(U.S. Patent #61/252,675)

Tetanus Toxoid is prepared by formaldehyde inactivation of pure neurotoxin. Each lot is verified to be non-toxic.

Information on the various uses of this and other Tetanus toxin products can be found on our blog.

This product is also an adjuvant. Information on all of our adjuvants can also be found on our blog.

Tetanus toxin is prepared from cultures of Clostridium tetani. In SDS-gel electrophoresis, the intact toxin migrates as a single band (150,000 Da). Upon reduction, the toxin migrates as two bands (100,000 and 50,000 Da) corresponding to the heavy and light chains, respectively. Tetanus toxin, in the reduced form, cleaves recombinant GST synaptobrevin 2 in in vitro assays.

Information on the various uses of this and other Tetanus toxin products can be found on our blog.

Tetanus toxin C-fragment is manufactured by enzyme digestion of native tetanus toxin produced in Clostridium tetani cultures. Each lot of C-fragment is tested for binding activity to G_T1b ganglioside. The FITC conjugate of C-fragment (C-FITC) also exhibits G_T1b ganglioside binding activity.

Information on the various uses of this and other Tetanus toxin products can be found on our blog.

Tetanus toxin C-fragment is manufactured by enzyme digestion of native tetanus toxin produced in Clostridium tetani cultures. Each lot of C-fragment is tested for binding activity to G_T1b ganglioside.

Information on the various uses of this and other Tetanus toxin products can be found on our blog.

PERTUSSIS TOXIN MUTANT

List Labs produces Pertussis Toxin Mutant, a genetically inactivated mutant of pertussis toxin.  The Pertussis Toxin Mutant contains a modified sequence encoding the enzyme subunit. Virulence of this pertussis mutant is greatly reduced relative to that found with the wild type.  The pertussis mutant protein is isolated from the TY-178 strain of Bordetella bronchiseptica which contains a genetically modified sequence encoding the S1 sub unit.  Site-directed mutagenesis was used to replace amino acid residues arginine-9 with lysine (R9K) and glutamic acid-129 with alanine (E129A).  Genetically inactivated toxin has reduced activity relative to the native toxin and may be used as an antigen or as a carrier to promote an immune response.

Bordetella pertussis virulence factors derived from native organisms and offered by List Labs, include Pertussis Toxin, Pertussis Toxin Subunits, Filamentous Hemagglutinin (FHA), Fimbriae 2/3, Pertactin (69 kDa protein), Adenylate Cyclase Toxin (ACT), Adenylate Cyclase Antigen and B. pertussis Lipopolysaccharide (LPS).  More information about each of these products may be obtained through the links on the Bordetella Virulence Factors page.

This product is also an adjuvant. For more information on adjuvants from List Labs, read our blog.

Pertussis Toxin

Pertussis toxin (PT), a virulence factor produced by Bordetella pertussis, is a multi-subunit toxin which binds to most cultured mammalian cells and targets specific G protein, inhibiting the ability of the G protein to function in signaling pathways.  Depending on the function of the G protein, the effects of PT can vary.  This ability to inhibit pathways utilizing the Gi family of protein-coupled receptors is the basis of the use of PT as a tool in cell biology.  PT plays a role in infection by suppressing and modulating various host immune responses to Bordetella pertussis.  PT has been used to stimulate experimental autoimmune diseases in rodent models, such as experimental auto immune encephalitis (EAE).

Native pertussis toxin is provided as a consistent product in three different formulations.  Pertussis toxin is lyophilized either in buffer (Product # 180) or in pure water (Product # 181).  Additionally, pertussis toxin is sold in a glycerol solution (Product # 179).  These products are listed below.

List Labs sells a genetically inactivated form of pertussis toxin, Pertussis Toxin Mutant. This protein may be used as antigens and as carrier proteins for other antigens.  Although an amino acid in the enzyme active site is altered and activity is diminished, this mutant retains some of the activity of the native toxin.  For more details about the genetically inactivated toxin follow the link to Pertussis Toxin Mutant.

Pertussis toxin is a multi-component protein composed of six non-covalently bound subunits ranging in molecular weight from approximately 9 to 28 kDa.  These subunits are designated as S1, S2, S3, S4 and S5 and occur in native pertussis toxin in a ratio of 1:1:1:2:1, where the subunit S4 is present in two copies.  The largest subunit S1, also called the A protomer, is responsible for the ADP-ribosyltransferase activity; the A protomer alone will transfer the ADP ribose from NAD⁺ to α subunits of G proteins of the class Gα_i, Gα_o or Gα_t.  The crystal structure of PTX reveals a pyramid-like shape with the A protomer situated on top of the S5 subunit which rests on two dimers, S2-S4 and S3-S4. Together the five subunit platform is called the B oligomer and under certain conditions PTX dissociates into just two parts, the enzymatic A protomer and the five subunit, binding complex, the B oligomer. This B oligomer allows PTX to enter most cells, attaching to glycan residues present on receptor proteins including TLR4 and glycoprotein Ib. After entering the cell via receptor-mediated endocytosis, PTX is transported retrogradely via the endosomal pathway and Golgi complex to the endoplasmic reticulum.   A protomer is released from the toxin and translocates through the membrane of the endoplasmic reticulum where the toxin inactivates the target membrane-bound G proteins.

Bordetella pertussis virulence factors derived from native organisms and offered by List Labs, include Pertussis Toxin Subunits, Pertussis Toxin Mutant, Filamentous Hemagglutinin (FHA), Fimbriae 2/3, Pertactin (69 kDa protein), Adenylate Cyclase Toxin (ACT), Adenylate Cyclase Antigen and B. pertussis Lipopolysaccharide (LPS).   More information about each of these products may be obtained through the links on the Bordetella Virulence Factors.

Pertussis Toxin

Pertussis toxin (PT), a virulence factor produced by Bordetella pertussis, is a multi-subunit toxin which binds to most cultured mammalian cells and targets specific G protein, inhibiting the ability of the G protein to function in signaling pathways.  Depending on the function of the G protein, the effects of PT can vary.  This ability to inhibit pathways utilizing the Gi family of protein-coupled receptors is the basis of the use of PT as a tool in cell biology.  PT plays a role in infection by suppressing and modulating various host immune responses to Bordetella pertussis.  PT has been used to stimulate experimental autoimmune diseases in rodent models, such as experimental auto immune encephalitis (EAE).

Native pertussis toxin is provided as a consistent product in three different formulations.  Pertussis toxin is lyophilized either in buffer (Product # 180) or in pure water (Product # 181).  Additionally, pertussis toxin is sold in a glycerol solution (Product # 179).  These products are listed below.

List Labs sells a genetically inactivated form of pertussis toxin, Pertussis Toxin Mutant. This protein may be used as antigens and as carrier proteins for other antigens.  Although an amino acid in the enzyme active site is altered and activity is diminished, this mutant retains some of the activity of the native toxin.  For more details about the genetically inactivated toxin follow the link to Pertussis Toxin Mutant.

Pertussis toxin is a multi-component protein composed of six non-covalently bound subunits ranging in molecular weight from approximately 9 to 28 kDa.  These subunits are designated as S1, S2, S3, S4 and S5 and occur in native pertussis toxin in a ratio of 1:1:1:2:1, where the subunit S4 is present in two copies.  The largest subunit S1, also called the A protomer, is responsible for the ADP-ribosyltransferase activity; the A protomer alone will transfer the ADP ribose from NAD⁺ to α subunits of G proteins of the class Gα_i, Gα_o or Gα_t.  The crystal structure of PTX reveals a pyramid-like shape with the A protomer situated on top of the S5 subunit which rests on two dimers, S2-S4 and S3-S4. Together the five subunit platform is called the B oligomer and under certain conditions PTX dissociates into just two parts, the enzymatic A protomer and the five subunit, binding complex, the B oligomer. This B oligomer allows PTX to enter most cells, attaching to glycan residues present on receptor proteins including TLR4 and glycoprotein Ib. After entering the cell via receptor-mediated endocytosis, PTX is transported retrogradely via the endosomal pathway and Golgi complex to the endoplasmic reticulum.   A protomer is released from the toxin and translocates through the membrane of the endoplasmic reticulum where the toxin inactivates the target membrane-bound G proteins.

Bordetella pertussis virulence factors derived from native organisms and offered by List Labs, include Pertussis Toxin Subunits, Pertussis Toxin Mutant, Filamentous Hemagglutinin (FHA), Fimbriae 2/3, Pertactin (69 kDa protein), Adenylate Cyclase Toxin (ACT), Adenylate Cyclase Antigen and B. pertussis Lipopolysaccharide (LPS).   More information about each of these products may be obtained through the links on the Bordetella Pertussis Virulence Factors.

PERTUSSIS TOXIN

Pertussis toxin (PT), a virulence factor produced by Bordetella pertussis, is a multi-subunit toxin which binds to most cultured mammalian cells and targets specific G protein, inhibiting the ability of the G protein to function in signaling pathways.  Depending on the function of the G protein, the effects of PT can vary.  This ability to inhibit pathways utilizing the Gi family of protein-coupled receptors is the basis of the use of PT as a tool in cell biology.  PT plays a role in infection by suppressing and modulating various host immune responses to Bordetella pertussis.  PT has been used to stimulate experimental autoimmune diseases in rodent models, such as experimental auto immune encephalitis (EAE).

Native pertussis toxin is provided as a consistent product in three different formulations.  Pertussis toxin is lyophilized either in buffer (Product # 180) or in pure water (Product # 181).  Additionally, pertussis toxin is sold in a glycerol solution (Product # 179).  These products are listed below.

List Labs sells a genetically inactivated form of pertussis toxin, Pertussis Toxin Mutant. This protein may be used as antigens and as carrier proteins for other antigens.  Although an amino acid in the enzyme active site is altered and activity is diminished, this mutant retains some of the activity of the native toxin.  For more details about the genetically inactivated toxin follow the link to Pertussis Toxin Mutant.

Pertussis toxin is a multi-component protein composed of six non-covalently bound subunits ranging in molecular weight from approximately 9 to 28 kDa.  These subunits are designated as S1, S2, S3, S4 and S5 and occur in native pertussis toxin in a ratio of 1:1:1:2:1, where the subunit S4 is present in two copies.  The largest subunit S1, also called the A protomer, is responsible for the ADP-ribosyltransferase activity; the A protomer alone will transfer the ADP ribose from NAD⁺ to α subunits of G proteins of the class Gα_i, Gα_o or Gα_t.  The crystal structure of PTX reveals a pyramid-like shape with the A protomer situated on top of the S5 subunit which rests on two dimers, S2-S4 and S3-S4. Together the five subunit platform is called the B oligomer and under certain conditions PTX dissociates into just two parts, the enzymatic A protomer and the five subunit, binding complex, the B oligomer. This B oligomer allows PTX to enter most cells, attaching to glycan residues present on receptor proteins including TLR4 and glycoprotein Ib. After entering the cell via receptor-mediated endocytosis, PTX is transported retrogradely via the endosomal pathway and Golgi complex to the endoplasmic reticulum.   A protomer is released from the toxin and translocates through the membrane of the endoplasmic reticulum where the toxin inactivates the target membrane-bound G proteins.

Bordetella pertussis virulence factors derived from native organisms and offered by List Labs, include Pertussis Toxin Subunits, Pertussis Toxin Mutant, Filamentous Hemagglutinin (FHA), Fimbriae 2/3, Pertactin (69 kDa protein), Adenylate Cyclase Toxin (ACT), Adenylate Cyclase Antigen and B. pertussis Lipopolysaccharide (LPS).   More information about each of these products may be obtained through the links on the Bordetella Virulence Factors.
Must ship standard or priority overnight.

PERTACTIN

Pertactin (PRN) is a 69 kDa surface-located protein produced by Bordetella pertussis.  Due to its immunogenic and protective properties, it is included in acellular pertussis vaccines.  The contribution of this protein to Bordetella pathogenesis is under investigation; however, it appears to play a role in overcoming neutrophil-mediated clearance of Bordetella during early stages of establishing an infection.   Pertactin is one of the most polymorphic B. pertussis proteins, occurring in the population in more than 13 variations.  Pertactin offered by List is isolated from native cultures of B. pertussis strain 165.

Bordetella pertussis virulence factors derived from native organisms and offered by List Labs, include Pertussis Toxin, Pertussis Toxin Subunits, Pertussis Toxin Mutant, Filamentous Hemagglutinin (FHA), Fimbriae 2/3, Pertactin (69 kDa protein), Adenylate Cyclase Toxin (ACT), Adenylate Cyclase Antigen and B. pertussis Lipopolysaccharide (LPS).   More information about each of these products may be obtained through the links on the Bordetella Virulence Factors.

Fimbriae 2/3

The initial step in establishing a Bordetella pertussis infection is attachment of the bacteria to the epithelial lining of the host respiratory tract.  Two B. pertussis virulence factors are key in this process, filamentous hemagglutinin (FHA) and fimbriae (Fim).  Fimbriae are extracellular proteins which like FHA participate in the attachment of bacteria to substrates.  Based on their reaction to sera, there are two fimbriae serotypes present in B. pertussis, fimbriae 2 (Fim 2) and fimbriae 3 (Fim 3).

Although fimbriae are long structures which serve to tether the bacterial to surfaces, they are composed of subunits which dissociate in SDS producing components with apparent molecular weights of 22,500 and 22,000 Da for Fim 2 and Fim 3, respectively.  Interestingly, antibodies raised to native Fim do not react well with SDS-denatured subunits.   Fim 2/3 produced and sold by List is isolated from cultures of a PRN^– mutant derived from the Bordetella pertussis Welcome strain 28 and consists of a mixture of fimbriae 2 and fimbriae 3.
Other Bordetella pertussis virulence factors derived from native organisms and offered by List Labs include Pertussis Toxin, Pertussis Toxin Subunits, Pertussis Toxin Mutant, Filamentous Hemagglutinin (FHA), Pertactin (69 kDa protein), Adenylate Cyclase Toxin (ACT), Adenylate Cyclase Antigen and B. pertussis Lipopolysaccharide (LPS).  More information about each of these products may be obtained through the links on the Bordetella Virulence Factors.

ADENYLATE CYCLASE TOXIN AND ADENYLATE CYCLASE ANTIGEN

Adenylate cyclase toxin (ACT) is an important virulence factor secreted by Bordetella pertussis. When a lung infection is underway, ACT interacts with tracheal epithelial cells, inserting itself into cytoplasmic membranes, aiding the adhesion of bacteria to the airway lining.  Host phagocytes responding to the site of infection are disabled by cAMP generated by ACT.  Encoded by the Bordetella pertussis cyaA gene, adenylate cyclase toxin is single 1706 amino acid polypeptide, with an apparent molecular weight of 220 kDa.  The N-terminal of this protein contains an adenylate cyclase domain which binds to host cell calmodulin and catalyzes unregulated conversion of cellular ATP to cAMP.  The C-terminal, receptor binding domain, contains numerous repeat in toxin (RTX) motifs and is responsible for binding to the cellular receptor on the surface of immune cells, translocation to the cell cytosol and creating cation-selective pores in the host cell membrane.

Adenylate cyclase toxin both suppresses and modulates the host immune system contributing to pathogenesis of B. pertussis.  This toxin is unusual in its ability to cross mammalian cell membranes and locate within the cytosol.  As a cell biology tool, adenylate cyclase has been used to deliver immunogenic epitopes, targeting antigen presenting cells.  ACT, product #188, and 188L are available from List Labs is an active enzyme, produced as a recombinant protein in E. coli.  These two adenylate cyclase products differ in that #188 is freeze dried and #188L is liquid.

A non-enzymatic, genetically detoxified ACT toxoid (CyaA-AC^–) has been produced. Although the catalytic activity in this toxoid is destroyed, it is still cell invasive and able to induce an immune response to co-administered pertussis antigens.  This toxoid has been shown to be capable of delivering vaccine antigens into the cytosol of major histocompatibility complex (MHC) class I antigen-presenting cells. CyaA-AC^– toxoid has been used as a tool to deliver antigens to T cells in anti-cancer immunotherapeutic vaccines.  Samples are available of the genetically detoxified CyaA-AC^– toxoid (Product #198L) and of an especially low endotoxin preparation of Adenylate Cyclase Toxin, Recombinant (Product #197L).

Bordetella pertussis virulence factors derived from native organisms and offered by List Labs, include Pertussis Toxin, Pertussis Toxin Subunits, Pertussis Toxin Mutant, Filamentous Hemagglutinin (FHA), Fimbriae 2/3, Pertactin (69 kDa protein), and B. pertussis Lipopolysaccharide (LPS).   More information about each of these products may be obtained through the links on the Pertussis Toxins and Virulence Factors.

This products is an adjuvant. For more information on this and other adjuvants from List Labs, read our blog.

This product is an adjuvant. For more information on this and other adjuvants from List Labs, read our blog.

This product is an adjuvant. For more information on this and other adjuvants from List Labs, read our blog.

List Labs’ HPT LPS is a highly potent lipopolysaccharide produced from E. coli O113. This endotoxin has been purified to eliminate residual intrinsic proteins and nucleic acids.  Potency of this product, in endotoxin units (EU), is determined to be at least 10 EU per ng LPS, or 10⁶ EU per mg LPS.

Endotoxins have been used to study the relationship between infection and the host innate immune system.  In humans, endotoxins have been shown to correlate with changes in cytokines, hormones and inflammatory makers, such as TNF, IL-6, cortisol, epinephrine, serum amyloid A and C-reactive protein.

This product is also an adjuvant. For more information on adjuvants from List Labs, read our blog.

This product is an adjuvant. For more information on adjuvants from List Labs, read our blog.

*This product is inactive

contact orders@listlabs.com for updates

This product is an adjuvant. For more information on adjuvants from List Labs, read our blog.

Limited Quantity Available

Limited inventory remaining, purchase what is needed from the same lot while it lasts.  Contact orders@listlabs.com if you have questions!

This product is an adjuvant. For more information on adjuvants from List Labs, read our blog.

Contact orders@listlabs.com if you have questions!

View citations for product # 100B

Read our Cholera related blog posts

(U.S. Patent #6,504,006)

Limited Quantity Available

Limited inventory remaining, purchase what is needed from the same lot while it lasts.  Contact orders@listlabs.com if you have questions!

(U.S. Patent #6,504,006)

GST-SV2c contains amino acids 454-579 of the human SV2c protein.  This region of the protein is known as the luminal domain loop, between transmembrane domains 7 and 8, and has been shown to be the location of botulinum neurotoxin type A (BoNT/A) binding.  Three posters demonstrating the functionality of the GST-SV2c fusion protein as a receptor for BoNT/A are available on this website (poster tab).  Recent data from our laboratory indicate improved specificity and reliable detection of as little as 1.25 pg BoNT/A when captured by the SV2c receptor. A full description of the optimized parameters will be available soon.

Product #133L is only available on a special order basis with a minimum quantity, please contact sales@listlabs.com for more information”

Liquid – must ship standard or priority overnight.

Liquid – must ship standard or priority overnight.

Liquid – must ship standard or priority overnight.

Liquid – must ship standard or priority overnight.

List Labs has designed a fluorescently labeled substrate for specific and quantitative detection of anthrax lethal factor in plasma.

More information can be found on our blog.

Limited Quantity Available

Limited inventory remaining, purchase what is needed from the same lot while it lasts.  Contact orders@listlabs.com if you have questions!

Liquid – must ship standard or priority overnight.

Limited Quantity Available

Limited inventory remaining, purchase what is needed from the same lot while it lasts.  Contact orders@listlabs.com if you have questions!