Recombinant M Tuberculosis CFP-10 Antigen (E.coli)

Product Specifications:

Item# 105-20: Recombinant M Tuberculosis CFP-10 Antigen (E.coli) 

Concentration: 2mg/ml

Mass/vial: 1mg/vial 

Volume/vial: 500ul 

Diluent: 50mM NaPO4, pH 7.0 0.1M NaCl , 0.05% SOD. 

Purity: >98%

Stabilizer: None

Preservative: None

Storage: -75°C

Physical State: Frozen Liquid

Stability: Not Determined

Description: M. Tuberculosis (virulent strain specific) CFP-10 antigen produced in the E. coli expression system.

Purificatiuon: Purified by ion affinity, solvent extraction and UF concentrated to >98% purity as determined by SDS-PAGE, reduced.

Molecular Weight: approx. 11kD

Specificity: This CFP-10 protein reacts with human TB serum in ELISA and Western ELISA. Suitable for diagnostic applications.

Biological Activity: Not Determined

Application and Instructions for use: 

Recommended concentrations for use are approximate values. A dose dependent response assay should be performed to determine the optimal concentration for use in specific applications. ELISA and Western ELISA require 10-100ng protein depending on the nature and affinity of the detection reagent. Human serum polyclonal antibodies yield titers of 1:1000 or greater at 100ng of immobilized protein under standard ELISA conditions. CAUTION: This product is sterile filtered and is stable at refrigeration temperature. Remove product aseptically from the vial.

Articles related to CFP-10:

Upon infection with Mycobacterium tuberculosis, neutrophils are massively recruited to the lungs, but the role of these cells in combating the infection is poorly understood. Through a type VII secretion system, M. tuberculosis releases a heterodimeric protein complex, containing a 6-kDa early secreted antigenic target (ESAT-6) and a 10-kDa culture filtrate protein (CFP-10), that is essential for virulence. Whereas the ESAT-6 component possesses multiple virulence-related activities, no direct biological activity of CFP-10 has been shown, and CFP-10 has been described as a chaperone protein for ESAT-6. We here show that the ESAT-6:CFP-10 complex induces a transient release of Ca2+ from intracellular stores in human neutrophils. Surprisingly, CFP-10 rather than ESAT-6 was responsible for triggering the Ca2+ response, in a pertussis toxin-sensitive manner, suggesting the involvement of a G-protein-coupled receptor. In line with this, the response was accompanied by neutrophil chemotaxis and activation of the superoxide-producing NADPH-oxidase. Neutrophils were unique among leukocytes in responding to CFP-10, as monocytes and lymphocytes failed to produce a Ca2+ signal upon stimulation with the M. tuberculosis protein. Hence, CFP-10 may contribute specifically to neutrophil recruitment and activation during M. tuberculosis infection, representing a novel biological role for CFP-10 in the ESAT-6:CFP-10 complex, beyond the previously described chaperone function.