Analytical Data
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Gene name
OXT
- Application
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Alternative Names
OXT；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
32-125aa
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AA Sequence
AAPDLDVRKCLPCGPGGKGRCFGPNICCAEELGCFVGTAEALRCQEENYLPSPCQSGQKACGSGGRCAVLGLCCSPDGCHADPACDAEATFSQR
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Molecular Weight
11.6 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
Related Products
Protein Description
Oxytocin (OXT) is a neuropeptide and hormone known for its important roles in social bonding, reproductive behaviors, and maternal-infant interactions. Recent research has focused on the recombinant production of oxytocin-like proteins due to their therapeutic potential in treating various psychiatric and physiological conditions, including autism spectrum disorders, anxiety, and postpartum depression. The ability to produce OXT recombinantly allows for large-scale generation of this peptide, overcoming limitations associated with traditional extraction methods from animal sources. Furthermore, recombinant OXT can be modified to enhance its stability and bioavailability or to develop analogs with improved efficacy or safety profiles. Studies have explored the structure-function relationship of OXT through site-directed mutagenesis and in vivo models, aiming to elucidate the mechanisms underlying its physiological effects. This growing body of research highlights the significance of recombinant OXT in both basic science and its potential application in clinical settings, opening the door for innovative therapies aimed at improving social and emotional well-being.
