Pertussis Toxin (Islet-Activating Protein)

Catalog No : USB-215958
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Product name Pertussis Toxin (Islet-Activating Protein)
Catalog No USB-215958
Supplier’s Catalog No 215958
Supplier US Biologicals
Source antigen B. pertussis
Reactivity
Cross reactivity
Applications
Molecular weight
Storage 4°C Do Not Freeze
Other names
Grade
Purity
Form Supplied as a lyophilized powder. No preservative added. Reconstitute with sterile H2O or sterile buffer. Handle Gently. Do not vortex.
Reactivity life 12 months
Note For reserch purpose only
Purity
Description 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). Pertussis toxin is a multi-component protein composed of six non-covalently bound subunits ranging in molecular weight from ~9-28kD. 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 alpha subunits of G proteins of the class Gai, Gao or Gat. 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. Source: Pertussis Toxin from B. pertussis Biological Activity: The lowest concentration of toxin at which a positive response (clustered growth pattern) was obtained was 0.01ng/ml. The adenylate cyclase activity of this lot is 0.67picomole/min/ug in the presence of 1umolar calmodulin when assayed by the method of Wolff et al. Storage and Stability: Lyophilized powder may be stored at 4°C. Reconstitute with sterile ddH2O. Aliquot to avoid repeated freezing and thawing. Store at 4°C. Reconstituted product is stable for 6 months at 4°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.