LFn-Linker-Cys (Anthrax Lethal Factor Mutant (LFn-Linker-Cys))

Lethal factor (LF) residues 1-254, followed by a short linker and a C-terminal Cysteine. This Cys provides a target for chemical conjugation of dyes, polypeptides, etc., through maleimide or iodoacetyl groups. The conjugated material will be internalized to the cytosol in the same way as LF or EF, provided the material has properties conducive to passage through the PA channel. LFn has the native N-terminus of AGG.

Anthrax toxin is a three-protein exotoxin secreted by virulent strains of the bacterium, Bacillus anthracis, the causative agent of anthrax. Anthrax toxin is composed of a cell-binding protein, known as protective antigen (PA), and two enzyme components, called edema factor (EF) and lethal factor (LF). Anthrax is caused by B. anthracis, a spore-forming, Gram positive, rod-shaped bacterium. The lethality of the disease is caused by the bacterium's two principal virulence factors: the polyglutamic acid capsule, which is anti-phagocytic, and the tripartite protein toxin, called anthrax toxin.

From the laboratory of Stephen H. Leppla, PhD, National Institute of Allergy and Infectious Diseases/NIH.

Catalog Number Product DataSheet Size AVAILABILITY Price Qty
ENH015-LT
LFn-Linker-Cys (Anthrax Lethal Factor Mutant (LFn-Linker-Cys))
100ug (1.25mg/mL) In stock
Regular Price:$306.00
On Sale:

In order to purchase this product, we require a Letter of Assurance form to be completed. Download form here: PDF Kerafast Letter of Assurance

Specifications

Product Type: Protein
Name: AGG-LFn-NLSLEELKD-GGGGSC
Alternative Name(s): LFn-Linker-Cys
Source: Expressed in avirulent engineered B. anthracisstrain BH460
Format: Purified protein (liquid)
Purity: Q-Sepharose Ion Exchange Chromatography
Buffer: 5 mM HEPES pH 7.5 and 0.5 mM EDTA, 0.25 mM DTT
Concentration: 1.25mg/mL
Storage: -80C
Shipped: Dry ice

Provider
From the laboratory of Stephen H. Leppla, PhD, National Institute of Allergy and Infectious Diseases/NIH.
References
  1. Leppla SH. Production and purification of anthrax toxin. Methods Enzymol. 1988;165:103-16.

If you publish research with this product, please let us know so we can cite your paper.

Loading...