protein

ssPA Protein, E. coli (His)

HY-P76089

5 μg;10 μg;50 μg

40;70;200 USD

ssPA Protein, E. coli (His)

proteins

E. coli

5 μg;10 μg;50 μg

40;70;200 USD

The ssPA protein specifically forms an equimolar complex with RNA polymerase holoenzyme (RNAP), thereby distinguishing its interaction preference from the core enzyme. ssPA is primarily synthesized during amino acid starvation and accounts for more than 50% of the total protein produced under these conditions. ssPA Protein, E. coli (His) is the recombinant E. coli-derived ssPA protein, expressed by E. coli , with N-His labeled tag. The total length of ssPA Protein, E. coli (His) is 212 a.a., with molecular weight of ~25 kDa.

E.coli

The ssPA (stringent starvation protein A) forms an equimolar complex with the RNA polymerase holoenzyme (RNAP) but does not associate with the core enzyme. Synthesized predominantly during amino acid starvation, ssPA constitutes over 50% of the total protein synthesized under such conditions. Its role is crucial in orchestrating the transition from P1 early to P1 late gene expression, suggesting its involvement in regulating gene expression during specific cellular states. Remarkably, the functional interchangeability observed between Rnk and SspA with the Pseudomonas aeruginosa alginate regulatory gene algR2 underscores the regulatory versatility of ssPA-like proteins in bacterial systems.

Stringent starvation protein A; sspA; pog; ssp

Greater than 95% as determined by reducing SDS-PAGE

Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.

Room temperature in continental US; may vary elsewhere.