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Merck
모든 사진(1)

주요 문서

516852

Sigma-Aldrich

Pertussis Toxin, B Oligomer, Bordetella pertussis - Calbiochem

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About This Item

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양식

lyophilized

불순물

≤1% holotoxin (by CHO cell assay)

solubility

aqueous buffer: soluble
sterile distilled water: soluble

일반 설명

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.

생화학적/생리학적 작용

Cell surface receptors with oligosaccharide side chains

재구성

Following reconstitution, refrigerate (4°C). Stock solutions, prepared from high ionic strength buffers, are stable for up to 3 months at 4°C.

분석 메모

Four distinct bands by SDS-PAGE

시험 성적서(COA)

제품의 로트/배치 번호를 입력하여 시험 성적서(COA)을 검색하십시오. 로트 및 배치 번호는 제품 라벨에 있는 ‘로트’ 또는 ‘배치’라는 용어 뒤에서 찾을 수 있습니다.

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문서 라이브러리 방문

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 virology, 74(18), 8767-8770 (2000-08-23)
We have recently demonstrated that the binding subunit (B-oligomer) of pertussis toxin (PTX-B) deactivates CCR5 and inhibits entry of R5 human immunodeficiency virus type 1 (HIV-1) strains in activated primary T lymphocytes (M. Alfano et al., J. Exp. Med. 190:597-605
Y Sato et al.
Infection and immunity, 41(1), 313-320 (1983-07-01)
The role of the filamentous hemagglutinin (FHA) and the lymphocytosis-promoting factor hemagglutinin (LPF) in pertussis pathogenesis and immunity is the subject of active investigation. To be certain of their role as protective antigens, the hemagglutinins must be pure and free
D L Burns et al.
Infection and immunity, 55(1), 24-28 (1987-01-01)
The mechanism by which pertussis toxin induces morphological changes in Chinese hamster ovary cells was studied to determine whether the resulting clustered growth pattern is due to toxin-catalyzed ADP-ribosylation of a cellular substrate. While pertussis toxin was extremely potent in

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