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C8052 Cholera Toxin from Vibrio cholerae ~95% (SDS-PAGE), lyophilized powder, 1 × 105-1 × 106 units/mg protein Toxin consisting of an A subunit (27 kDa) surrounded by five B subunits (approximately 12 kDa each), which attach the toxin to ganglioside GM1 on the cell surface. The A subunit catalyzes ADP-ribosylation of the α-subunit of the stimulatory G protein (Gαs), reducing GTPase activity and activating the α-subunit. This activation of Gαs leads to an increase in the activity of adenylyl cyclase, resulting in increased levels of cAMP. Also ADP-ribosylates transducin in the eye rod outer segments, inactivating its GTPase activity. Cholera toxin has also been reported to ADP-ribosylate tubulin. Shown to be a potent mucosal vaccine adjuvant, inducing T helper cell type 2 responses by inhibiting the production of interleukin-12.
C8180 Cholera Toxin A Subunit from Vibrio cholerae lyophilized powder Catalyzes ADP-ribosylation of the α-subunit of G proteins, reducing GTPase activity and activating the α-subunit; also catalyzes ADP-ribosylation of cell membrane adenylyl cyclase
C9903 Cholera Toxin B subunit ≥95% (SDS-PAGE), lyophilized powder The cholera toxin B subunit is used for track tracing in neurological research, taking advantage of GM1 ganglioside binding and retrograde transport. Tissue culture cells treated with cholera toxin are not killed and tissues of animals do not become necrotic.
C167 Cholera Toxin B subunit solid The cholera toxin B subunit is used for track tracing in neurological research, taking advantage of GM1 ganglioside binding and retrograde transport. Tissue culture cells treated with cholera toxin are not killed and tissues of animals do not become necrotic.
C9972 Cholera Toxin B subunit biotin conjugate, lyophilized powder The cholera toxin B subunit is used for track tracing in neurological research, taking advantage of GM1 ganglioside binding and retrograde transport. Tissue culture cells treated with cholera toxin are not killed and tissues of animals do not become necrotic.
C1655 Cholera Toxin B subunit FITC conjugate, lyophilized powder The cholera toxin B subunit is used for track tracing in neurological research, taking advantage of GM1 ganglioside binding and retrograde transport. Tissue culture cells treated with cholera toxin are not killed and tissues of animals do not become necrotic.
C3977 Clostridium difficile Toxin A lyophilized powder Clostridium difficile Toxin A and B, cation-dependent UDP-glucose glucosyltransferases, are cellular toxins that inactivate Rho (and Rho family small GTPases) through monoglucosylation of these family members. Effects of this monoglucosylation include disregulation of the actin cytoskeleton, cell rounding, cytotoxicity, and altered cellular signaling. Rho proteins are monoglucosylated by Toxin A and B using UDP-glucose as a cosubstrate. Rho, Rac and Cdc42 are included in the Rho subfamilies targeted by both toxins. Low molecular mass GTP-binding proteins that are not modified by Toxin A and B include Ras, Rab, Arf, or Ran subfamilies as well as heterotrimeric G proteins.
SML1154 Clostridium difficile Toxin A ≥95% (SDS-PAGE) Clostridium difficile Toxin A and B, cation-dependent UDP-glucose glucosyltransferases, are cellular toxins that inactivate Rho (and Rho family small GTPases) through monoglucosylation of these family members. Effects of this monoglucosylation include disregulation of the actin cytoskeleton, cell rounding, cytotoxicity, and altered cellular signaling. Rho proteins are monoglucosylated by Toxin A and B using UDP-glucose as a cosubstrate. Rho, Rac and Cdc42 are included in the Rho subfamilies targeted by both toxins. Low molecular mass GTP-binding proteins that are not modified by Toxin A and B include Ras, Rab, Arf, or Ran subfamilies as well as heterotrimeric G proteins.
C4102 Clostridium difficile Toxin B lyophilized powder Clostridium difficile Toxin A and B, cation-dependent UDP-glucose glucosyltransferases, are cellular toxins that inactivate Rho (and Rho family small GTPases) through monoglucosylation of these family members. Effects of this monoglucosylation include disregulation of the actin cytoskeleton, cell rounding, cytotoxicity, and altered cellular signaling. Rho proteins are monoglucosylated by Toxin A and B using UDP-glucose as a cosubstrate. Rho, Rac and Cdc42 are included in the Rho subfamilies targeted by both toxins. Low molecular mass GTP-binding proteins that are not modified by Toxin A and B include Ras, Rab, Arf, or Ran subfamilies as well as heterotrimeric G proteins.
Toxin B is 100-1,000-fold more cytotoxic than toxin A in inducing rounding-up of cells and destruction of the actin cytoskeleton.
SML1153 Clostridium difficile Toxin B ≥95% (SDS-PAGE) Clostridium difficile Toxin A and B, cation-dependent UDP-glucose glucosyltransferases, are cellular toxins that inactivate Rho (and Rho family small GTPases) through monoglucosylation of these family members. Effects of this monoglucosylation include disregulation of the actin cytoskeleton, cell rounding, cytotoxicity, and altered cellular signaling. Rho proteins are monoglucosylated by Toxin A and B using UDP-glucose as a cosubstrate. Rho, Rac and Cdc42 are included in the Rho subfamilies targeted by both toxins. Low molecular mass GTP-binding proteins that are not modified by Toxin A and B include Ras, Rab, Arf, or Ran subfamilies as well as heterotrimeric G proteins.
Toxin B is 100-1,000-fold more cytotoxic than toxin A in inducing rounding-up of cells and destruction of the actin cytoskeleton.
D0564 Diphtheria Toxin from Corynebacterium diphtheriae lyophilized powder Inhibits protein synthesis by catalyzing ADP-ribosylation of eukaryotic aminoacyltransferase II.
D2189 [Glu52]-Diphtheria toxin from Corynebacterium diphtheriae lyophilized powder  
P5806 Pasteurella multocida toxin lyophilized powder  
P7208 Pertussis toxin from Bordetella pertussis lyophilized powder Pertussis toxin catalyzes the ADP-ribosylation of the α subunits of the heterotrimeric guanine nucleotide regulatory proteins Gi, Go, and Gt. This prevents the G protein heterotrimers from interacting with receptors, thus blocking their coupling and activation. Since the Gα subunits remain in their GDP-bound, inactive state, they are unable to inactivate adenylyl cyclase or open K+ channels.
P2980 Pertussis toxin from Bordetella pertussis buffered aqueous glycerol solution Pertussis toxin catalyzes the ADP-ribosylation of the α subunits of the heterotrimeric guanine nucleotide regulatory proteins Gi, Go, and Gt. This prevents the G protein heterotrimers from interacting with receptors, thus blocking their coupling and activation. Since the Gα subunits remain in their GDP-bound, inactive state, they are unable to inactivate adenylyl cyclase or open K+ channels.
P159 Pertussis toxin B oligomer solid Subunit of pertussis toxin responsible for binding to cell surfaces; stimulates both platelet aggregation and cytosolic Ca2+ level elevation, may also activate phospholipase C; isolated from B pertussis strain 165.
P0184 Pseudomonas exotoxin A from Pseudomonas aeruginosa lyophilized powder Shown to be toxic to animals and to cell lines, and to inhibit protein synthesis via ADP ribosylation of elongation factor 2.
SML0562 Shiga Toxin 1, B subunit recombinant, expressed in E. coli, ≥95% (SDS-PAGE) The Shiga toxins are a family of related protein toxins secreted by certain types of bacteria. Shiga toxin (Stx) is produced by Shigella dysenteriae, whereas the Shiga-like toxins, Stx1 and Stx2, with a few known isoforms, are secreted by specific strains of Escherichia coli named Shiga-toxin-producing E. coli (STEC) such as E. coli O157:H7, which causes bloody diarrhea and hemorrhagic colitis in humans, sometimes resulting in fatal systemic complications.

Stx1 is identical to Stx, while the Stx2 isoforms share less sequence similarity with Stx (~60%) and are immunologically distinct. In spite of the differences in their amino acid sequence, all Stx isoforms share the same overall toxin structure and mechanism of action.

Shiga toxins consist of two polypeptides: An A chain and a B chain non-covalently associated with an apparent stoichiometry of one A and five B chains, to form the holotoxin. The catalytic A subunit has a RNA N-glycosidase activity that inhibits eukaryotic protein synthesis. The B subunits form a pentamer that recognizes and binds to the functional cell-surface receptor globotriaosylceramide [Gb3; Gala(1-4)-Galb(1-4)-Glcb1-ceramide]. Gb3 is overexpressed in membranes of numerous tumor cells, therefore STxB binding to Gb3 receptors may be useful for cell-specific vectorization, labeling and imaging purposes.
SML0655 Shiga toxin 1, B subunit, HIS-tagged recombinant, expressed in E. coli, ≥95% (SDS-PAGE) The Shiga toxins are a family of related protein toxins secreted by certain types of bacteria. Shiga toxin (Stx) is produced by Shigella dysenteriae; whereas, the Shiga-like toxins, Stx1 and Stx2, with a few known isoforms, are secreted by specific strains of Escherichia coli named Shiga-toxin-producing E. coli (STEC), such as E. coli O157:H7, which causes bloody diarrhea and hemorrhagic colitis in humans, sometimes resulting in fatal systemic complications.

Stx1 is identical to Stx, while the Stx2 isoforms share less sequence similarity with Stx (∼60%) and are immunologically distinct. In spite of the differences in their amino acid sequence, all Stx isoforms share the same overall toxin structure and mechanism of action.

Shiga toxins consists of two polypeptides. An A chain and a B chain non-covalently associate with an apparent stoichiometry of one A and five B chains to form the holotoxin. The catalytic A subunit has
RNA N-glycosidase activity that inhibits eukaryotic protein synthesis. The B subunits form a pentamer, which recognizes and binds to the functional cell-surface receptor globotriaosylceramide [Gb3; Gala(1-4)-Galb(1-4)-Glcb1-ceramide]. Gb3 is overexpressed in membranes of numerous tumor cells, therefore STxB binding to Gb3 receptors may be useful for cell-specific vectorization, labeling, and imaging purposes.
S0149 Streptolysin O from Streptococcus pyogenes γ-irradiated Thiol-activated toxin that permeabilizes animal cell membranes. The protein binds as a monomer to membrane cholesterol and subsequently polymerizes into large arc- and ring-shaped structures surrounding pores of >12 nm.
S1014 Streptonigrin from Streptomyces flocculus ≥98% Streptonigrin (SN) is an aminoquinone antitumour antibiotic. Its antineoplastic activity requires reductive activation by Xanthine-converting enzymes. It induces apoptosis by a mechanism involving NF-κB. DNA cleavage reaction and chromosome damage by SN are influenced by the nature of the metal ion present and dependent on the production of free radicals. Its antibiotic activity is iron-activated.
T5319 Tetanolysin from Clostridium tetani Cholesterol-binding toxin used to permeabilize cellular membranes to enhance the entry of macromolecules into the interior of the cell. Pores induced reported to be in the range of 20-50 nm.
T3194 Tetanus toxin from Clostridium tetani Binds to polysialogangliosides acceptors on surface of all peripheral presynaptic nerve terminals. Internalized by receptor-mediated endocytosis and carried to spinal cord and brain by transsynaptic retrograde transport. Blocks the release of glycine from inhibitory interneurons of the spinal cord. Cleaves synaptobrevin (VAMP-2), and blocks synaptic vesicle exocytosis in vivo.
T3694 Tetanus toxin C fragment from Clostridium tetani Tetanus toxin is a neurotoxin that comprises of a heavy and a light chain linked by disulfide bridges. This neurotoxin enters the cytoplasm and releases the light chain component that subsequently inhibits the release of neurotransmitters2. Studies have reported that the fragment C of tetanus toxin retains most of the determinants that interact with thyroid membranes, gangliosides and neural membranes3.
T3819 Tetanus toxin C-fragment−FITC from Clostridium tetani C terminal portion conjugated to fluorescein isothiocyanate is taken up by persynaptic nerve terminals and exhibits transsynaptic retrograde transport in central neurons similar to that of tetanus toxin. It is used to map neuronal connections and to target proteins to neurons
Tetanus toxin is a neurotoxin that comprises of a heavy and a light chain linked by disulfide bridges. This neurotoxin enters the cytoplasm and releases the light chain component that subsequently inhibits the release of neurotransmitters3. Studies have reported that the fragment C of tetanus toxin retains most of the determinants that interact with thyroid membranes, gangliosides and neural membranes4.
T5662 Toxic shock syndrome toxin-1 from Staphylococcus aureus Superantigen for T-lymphocytes.