Analytical Data
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Gene name
OT
- Application
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Alternative Names
OT；OT；Oxytocin-neurophysin 1
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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
P01178
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Expression Region
1-125aa
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AA Sequence
MAGPSLACCLLGLLALTSACYIQNCPLGGKRAAPDLDVRKCLPCGPGGKGRCFGPNICCAEELGCFVGTAEALRCQEENYLPSPCQSGQKACGSGGRCAVLGLCCSPDGCHADPACDAEATFSQR
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Molecular Weight
12.7 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
The study of outer membrane transporter (OT) proteins has gained significant attention due to their crucial role in the cellular processes of gram-negative bacteria. These proteins are responsible for the transport of essential nutrients, metabolites, and drugs across the outer membrane, which acts as a permeability barrier. Understanding the structure and function of OT proteins is vital for several reasons: first, they are key to bacterial survival in hostile environments; second, they can contribute to antibiotic resistance by mediating the uptake or efflux of antimicrobial agents; and third, they serve as potential targets for drug development aimed at disrupting bacterial infections. The research on OT proteins encompasses various approaches, including structural biology, biochemistry, and genomics, which aim to elucidate their mechanisms of transport and interaction with substrates. Additionally, advances in techniques such as cryo-electron microscopy and X-ray crystallography have provided invaluable insights into their 3D structures, paving the way for the design of novel inhibitors. Given the rise of multidrug-resistant bacterial strains, the exploration of OT proteins is not only significant for basic science but also holds promise for improving therapeutic strategies against bacterial infections. Understanding these complex systems can ultimately contribute to the development of new antibiotics and enhance our ability to combat pathogenic bacteria effectively.
