Analytical Data
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Gene name
rpoH
- Application
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Alternative Names
Heat shock regulatory protein F33.4 (RNA polymerase sigma-32 factor) (fam) (hin) (htpR)
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Species
Escherichia coli
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P0AGB3
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Expression Region
1-284aa
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Molecular Weight
39.9 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
The study of RpoH, a key heat shock sigma factor in bacteria, arises from its critical role in responding to stress conditions, particularly elevated temperatures. RpoH, also known as sigma 32, orchestrates the expression of numerous heat shock proteins (HSPs), which are essential for protein folding, repair, and degradation under stress. Understanding RpoH's function is crucial as it contributes to bacterial survival, virulence, and adaptation in various environments, including pathogenic settings. Research has revealed that RpoH is regulated through multiple mechanisms, including degradation by the FtsH protease and sequestration by chaperones such as DnaK, which ensures a controlled response to stress. Investigating RpoH's biochemical properties and the pathways that regulate its activity can provide insights into the broader mechanisms of bacterial adaptation and stress resilience. Additionally, this knowledge can inform the development of new antimicrobial strategies aimed at disrupting RpoH function, thereby providing a potential target for therapeutic interventions against pathogenic bacteria that rely on this sigma factor for survival in hostile conditions. As such, the recombinant expression and characterization of RpoH protein not only advance fundamental microbiological research but also hold promise for applied biomedical applications.
