Analytical Data
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Gene name
Transcription termination factor Rho
- Application
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Alternative Names
OPN2; RP4; Opsin 2; Rod Pigment; Retinitis Pigmentosa 4; Visual Purple
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P08100
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Expression Region
Met1~Asn73
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Molecular Weight
14kDa
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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 transcription termination factor Rho is a vital protein in prokaryotic cells that plays a crucial role in terminating transcription initiated by RNA polymerase. Understanding Rho is essential as it helps regulate gene expression, influences antibiotic resistance, and sheds light on fundamental cellular processes. Rho operates as a hexameric RNA-dependent ATPase that binds to the nascent RNA transcript and translocates along it, ultimately dislodging the RNA polymerase when it encounters specific terminator sequences. Studying Rho's structure, function, and mechanistic pathways can reveal insights into transcription regulation and the potential for novel therapeutic strategies, especially in combating bacterial infections. Recombinant protein techniques allow for the production of Rho in a controlled laboratory setting, facilitating comprehensive biochemical and biophysical analyses. This research can contribute to the understanding of Rho's interactions with RNA and other cellular factors, and its role in transcription termination could lead to the development of targeted antibiotics that disrupt this process in pathogenic bacteria. Thus, the investigation of the Rho transcription termination factor not only enhances our comprehension of transcription mechanics but also holds significant implications for biotechnology and medicine.
