Analytical Data
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Gene name
acrR
- Application
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Alternative Names
acrR；ybaH；HTH-type transcriptional regulator AcrR
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P0ACS9
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Expression Region
1-215aa
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AA Sequence
MARKTKQEAQ ETRQHILDVA LRLFSQQGVS STSLGEIAKA AGVTRGAIYW HFKDKSDLFS EIWELSESNI GELELEYQAK FPGDPLSVLR EILIHVLEST VTEERRRLLM EIIFHKCEFV GEMAVVQQAQ RNLCLESYDR IEQTLKHCIE AKMLPADLMT RRAAIIMRGY ISGLMENWLF APQSFDLKKE ARDYVAILLE MYLLCPTLRN PATNE
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Molecular Weight
24.7 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
AcrR is a transcriptional regulator belonging to the MarR family, playing a crucial role in the expression of acrAB-tolC efflux pump in Escherichia coli. This efflux pump is essential for bacterial resistance to a wide range of antibiotics and toxic compounds, making AcrR an important target for understanding mechanisms of antibiotic resistance. In recent years, increasing rates of antibiotic resistance have raised significant concerns in clinical settings, necessitating a deeper understanding of the underlying molecular mechanisms. The study of AcrR, particularly through the characterization of its recombinant protein, is aimed at elucidating its regulatory role and interactions with DNA and effector molecules. By employing techniques such as site-directed mutagenesis and crystallography, researchers can identify key residues and conformational changes that influence AcrR's activity. This can pave the way for the development of novel antibacterial agents that target AcrR or disrupt its regulatory pathway, ultimately enhancing the efficacy of existing antibiotics and combating the growing threat of multidrug-resistant bacterial infections. Understanding AcrR's function and structure is thus integral to the broader fight against antibiotic resistance and the optimization of therapeutic strategies.
