Recombinant Treponema Membrane Protein A (Beta-Galactosidase) is a Treponema pallidum subsp. pallidum str. Nichols protein, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, ELISA, WB, Flow Cyt.
>95% SDS-PAGE
Escherichia coli
SDS-PAGE, ELISA, WB, Flow Cyt
No
Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application ELISA | Reactivity Reacts | Dilution info - | Notes - |
Application WB | Reactivity Reacts | Dilution info - | Notes - |
Application Flow Cyt | Reactivity Reacts | Dilution info - | Notes - |
Treponemal membrane protein A, Antigen TmpA, Membrane protein A, tmpA, TP_0768
Recombinant Treponema Membrane Protein A (Beta-Galactosidase) is a Treponema pallidum subsp. pallidum str. Nichols protein, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, ELISA, WB, Flow Cyt.
Treponemal membrane protein A, Antigen TmpA, Membrane protein A, tmpA, TP_0768
>95% SDS-PAGE
Escherichia coli
SDS-PAGE, ELISA, WB, Flow Cyt
No
No
Treponema pallidum subsp. pallidum str. Nichols
pH: 7.2 - 7.6
Constituents: 48% Urea, 0.316% Tris HCl, 0.078% 2-Mercaptoethanol
Liquid
To T.phagedenis TmpA.
Blue Ice
1-2 weeks
+4°C
-20°C
Upon delivery aliquot
Avoid freeze / thaw cycle
Reacts strongly with human T. pallidum positive serum.
Treponema Membrane Protein A also known as TmpA is an integral membrane protein identified in Treponema species such as Treponema pallidum which causes syphilis. This protein has a mass of approximately 42 kDa. It is expressed primarily in the outer membrane of these bacteria playing an important structural role. TmpA acts as a surface antigen detectable by the host immune system making it essential for pathogenesis and bacterial survival.
TmpA contributes significantly to the bacterial pathogen's ability to evade host immune responses. It is not part of a known protein complex but functions in interactions with host cell structures. This protein facilitates adhesion to host tissues which is critical for infection establishment. Furthermore TmpA assists in nutrient acquisition aiding the survival of Treponema within host environments.
TmpA contributes to infectious processes and immune evasion rather than traditional metabolic pathways. It involves in pathways significant for bacterial adhesion and immune response interference. TmpA's interactions may involve other bacterial proteins like TprK which plays a role in antigenic variation enhancing the bacteria's ability to avoid immune detection and ensuring persistent infection in the host.
TmpA is associated with syphilis a sexually transmitted disease caused by Treponema pallidum. The presence of TmpA is critical to the bacterium's pathogenicity contributing to tissue attachment and immune system evasion leading to disease progression. Moreover TmpA is associated with enhanced virulence and is considered a potential target for vaccine development against syphilis. Its connection with other Treponema proteins like TprF suggests a synergistic impact on disease mechanisms making it a relevant target for therapeutic intervention.
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