Analytical Data
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Gene name
OVA
- Application
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Alternative Names
OVA；Ccr11；Lccr；C-C chemokine receptor-like 2
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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
O00421
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Expression Region
1-344aa
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AA Sequence
MANYTLAPEDEYDVLIEGELESDEAEQCDKYDAQALSAQLVPSLCSAVFVIGVLDNLLVVLILVKYKGLKRVENIYLLNLAVSNLCFLLTLPFWAHAGGDPMCKILIGLYFVGLYSETFFNCLLTVQRYLVFLHKGNFFSARRRVPCGIITSVLAWVTAILATLPEFVVYKPQMEDQKYKCAFSRTPFLPADETFWKHFLTLKMNISVLVLPLFIFTFLYVQMRKTLRFREQRYSLFKLVFAIMVVFLLMWAPYNIAFFLSTFKEHFSLSDCKSSYNLDKSVHITKLIATTHCCINPLLYAFLDGTFSKYLCRCFHLRSNTPLQPRGQSAQGTSREEPDHSTEV
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Molecular Weight
39.5 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 OVA (ovalbumin) recombinant proteins has garnered significant interest in the fields of immunology and biotechnology due to their potential applications in vaccine development and allergen research. Ovalbumin, a major allergen found in egg whites, serves as a model protein for studying immune responses, particularly in the context of allergic reactions and tolerance induction. The recombinant version of OVA can be produced using various expression systems, including bacteria, yeast, and mammalian cells, allowing researchers to generate specific mutations or modifications that can enhance its immunogenic properties or alter its allergenic potential. This versatility enables the design of tailored proteins for therapeutic use, such as in allergy immunotherapy, where OVA can be used to sensitively assess immune responses in preclinical models. Moreover, understanding the structure-function relationship of OVA through recombinant techniques aids in deciphering the underlying mechanisms of immune recognition and activation. As such, the research into OVA recombinant proteins not only advances our fundamental knowledge of immunological processes but also holds promise for innovative approaches to treating allergies and designing novel vaccines, contributing to improved public health outcomes.
