Analytical Data
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Gene name
oxyR
- Application
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Alternative Names
oxyR；Oxytocin receptor
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Species
E.coli
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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
P0ACQ4
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Expression Region
1-305aa
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AA Sequence
MNIRDLEYLVALAEHRHFRRAADSCHVSQPTLSGQIRKLEDELGVMLLERTSRKVLFTQAGMLLVDQARTVLREVKVLKEMASQQGETMSGPLHIGLIPTVGPYLLPHIIPMLHQTFPKLEMYLHEAQTHQLLAQLDSGKLDCVILALVKESEAFIEVPLFDEPMLLAIYEDHPWANRECVPMADLAGEKLLMLEDGHCLRDQAMGFCFEAGADEDTHFRATSLETLRNMVAAGSGITLLPALAVPPERKRDGVVYLPCIKPEPRRTIGLVYRPGSPLRSRYEQLAEAIRARMDGHFDKVLKQAV
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Molecular Weight
82.1 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
OxyR is a transcription factor in bacteria, particularly well-studied in Escherichia coli, that plays a crucial role in the oxidative stress response. Its primary function is to regulate the expression of genes involved in the defense against reactive oxygen species (ROS), which can cause significant cellular damage. Understanding the mechanisms of OxyR activation and regulation is essential, as oxidative stress is linked to various bacterial pathogenicity and resistance to antibiotics. Moreover, OxyR serves as a model for studying redox-sensitive transcription factors, providing insights into how cells adapt to fluctuating environmental conditions. The recombinant protein of OxyR has been expressed and purified in various systems for biochemical characterization and functional studies. Research on OxyR aims to elucidate its regulatory mechanisms, interaction with other cellular components, and potential applications in biotechnology, such as developing novel antimicrobial agents or improving bacterial strains for industrial purposes. The ongoing investigation into the structure and dynamics of OxyR, combined with advances in molecular biology techniques, opens new avenues for manipulating this protein's activity, ultimately contributing to a better understanding of stress responses in bacteria and their implications for health and disease.
