form
lyophilized
impurities
≤1% holotoxin (by CHO cell assay)
solubility
aqueous buffer: soluble, sterile distilled water: soluble
General description
The pentameric cell-binding component that is responsible for binding of the holotoxin to eukaryotic cell surfaces, facilitating entry of the A protomer into receptive cells. Reported to elicit direct cellular responses by binding to several cell surface receptors with oligosaccharide side chains. Also elicits a variety of physiological responses, such as mitogenesis in human T cells, enhancement of aggregation of human platelets, elevation of cytosolic Ca2+ levels, and neutralization of antibody response in mice. Reported to deactivate CCR5 and inhibit the entry of R5 HIV-1 in activated T lymphocytes. Also blocks post-entry step of HIV-1 replication.
Biochem/physiol Actions
Cell surface receptors with oligosaccharide side chains
Preparation Note
Following reconstitution, refrigerate (4°C). Stock solutions, prepared from high ionic strength buffers, are stable for up to 3 months at 4°C.
Analysis Note
Four distinct bands by SDS-PAGE
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E L Hewlett et al.
Infection and immunity, 40(3), 1198-1203 (1983-06-01)
Exposing Chinese hamster ovary cells in culture to pertussis toxin resulted in a novel clustered growth pattern. The specificity of the response for pertussis toxin was shown by neutralization of the activity with specific anti-toxin antibody, heat lability (80 degrees
M Tamura et al.
Biochemistry, 21(22), 5516-5522 (1982-10-26)
The subunit structure of islet-activating protein (IAP), pertussis toxin, has been analyzed to study a possibility that this protein is one of the A-B toxins [Gill, D. M. (1978) in Bacterial Toxins and Cell Membranes (Jeljaszewicz, J., & Wadstrom, T.
M Alfano et al.
Journal of immunology (Baltimore, Md. : 1950), 166(3), 1863-1870 (2001-02-13)
We have recently shown that the binding subunit of pertussis toxin (PTX-B) inhibits the entry and replication of macrophage-tropic (R5) HIV-1 strains in activated primary T lymphocytes. Furthermore, PTX-B suppressed the replication of T cell-tropic (X4) viruses at a postentry