ALEXIS Biochemicals: Pertussis Toxin

ALX-630-003

Revised 18-Mar-08

Pertussis Toxin
SYNONYMS	Islet-Activating Protein PTX Holotoxin
PRODUCT LINE	Natural Products / Antibiotics
PRODUCT CATEGORY	Neurotoxins

Ordering Information

Product Numbers:	Format:	Size:	Unit Price:	Quantity:	Add To Cart
ALX-630-003-C050		50 µg	220.00 USD

Product Specification

CAS NUMBER:	70323-44-3
RTECS:	XW5883750
SOURCE/HOST:	Isolated from Bordetella pertussis.
CONCENTRATION:	0.1mg/ml after reconsitution. Determined by a modification of the method of Bradford using BSA as the standard.
PURITY:	Migrates as 5 distinct bands (S1 subunit: A Protomer (Prod. No. ALX-630-080); S2-S5 subunits: B Protomer (Prod. No. ALX-630-081)).
APPEARANCE:	Lyophilized.
PURITY DETAIL:	Described by Tamura et al., when run on SDS-PAGE prepared according to a modification of the method of Laemmli.
RECONSTITUTION:	Reconstitute with 500µl distilled water to get a solution in 0.01M sodium phosphate buffer, pH 7.0, containing 0.05M NaCl. The resulting suspension should be made uniform by gentle mixing prior to use. Do not sterile filter, as this will result in loss of material. For long term storage, reconstitute in a buffer of higher ionic strength, i.e. sterile 0.1M sodium phosphate, pH 7.0, containing 0.5M NaCl.
SHIPPING:	AMBIENT
LONG TERM STORAGE:	+4°C
HANDLING:	Do not freeze. Aseptically packed, sealed under vacuum.
HAZARD:	TOXIC.

Product Description

Major protein toxin produced by virulent strains of Bordetella pertussis. The purified protein consists of five dissimilar subunits: S-1 (MW 28kDa), S-2 (MW 23kDa), S-3 (MW 22kDa), S-4 (MW 11.7kDa) and S-5 (MW 9.3kDa), in a molar ratio of 1:1:1:2:1. S-1 (A protomer) is responsible for the enzymatic activity of the toxin. Together, S-2, S-3, S-4 and S-5 comprise the B oligomer, responsible for binding the toxin to the cell surface.

Product Specific Literature References

Subunit structure of islet-activating protein, pertussis toxin, in conformity with the A-B model: M. Tamura, et al.; Biochemistry 21, 5516 (1982) Abstract
Induction of a novel morphological response in Chinese hamster ovary cells by pertussis toxin: E.L. Hewlett, et al.; Infect. Immun. 40, 1198 (1983) Abstract
Structure-activity analysis of the activation of pertussis toxin: H.R. Kaslow, et al.; Biochemistry 26, 123 (1987) Abstract
Pertussis toxin and target eukaryotic cells: binding, entry, and activation: H. R. Kaslow & D. L. Burns; FASEB J. 6, 2684 (1992), (Review) Abstract
A proposed mechanism of ADP-ribosylation catalyzed by the pertussis toxin S1 subunit: C. Locht & R. Antoine; Biochimie 77, 333 (1995) Abstract

General Information

BACKGROUND/TECHNICAL INFORMATION

CHO Cell Assay: When examined in a CHO cell assay as described by Hewlett et al., the lowest concentration of toxin at which a positive response (clustered growth pattern) was obtained was XXng/ml.
Adenylate Cyclase Assay: The adenylate cyclase activity of this lot is XXpmol/min/µg in the presence of 1µM calmodulin when assayed by the method of Wolff et al.
Please note: Product is not activated. If used with an intact cell system, the cells will activate the toxin. If used in a cell-free system activation may be achieved by the methods, of Kaslow et al.

General Literature References

Cleavage of structural proteins during the assembly of the head of bacteriophage T4: U.K. Laemmli; Nature 227, 680 (1970) Abstract
A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding: M.M. Bradford; Anal. Biochem. 72, 248 (1976) Abstract
Calmodulin activates prokaryotic adenylate cyclase: J. Wolff, et al.; PNAS 77, 3841 (1980) Abstract

Further Categories Containing This Product:

Adenylyl Cyclase Activators • ADP Ribosylation Factor [ARF] / Related Products

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