Analytical Data
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Gene name
OBP2A
- Application
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Alternative Names
OBP2A；Odorant-binding Protein 2a
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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
Q9NY56
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Expression Region
16-170aa
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AA Sequence
LSFTLEEEDITGTWYVKAMVVDKDFPEDRRPRKVSPVKVTALGGGNLEATFTFMREDRCIQKKILMRKTEEPGKFSAYGGRKLIYLQELPGTDDYVFYSKDQRRGGLRYMGNLVGRNPNTNLEALEEFKKLVQHKGLSEEDIFMPLQTGSCVLEH
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Molecular Weight
30.8 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
OBP2A (Olfactory Binding Protein 2A) is a member of the odorant-binding protein family that plays a crucial role in the olfactory system by binding and transporting odorant molecules. Its expression is predominantly observed in non-sensory tissues, including various organs, which has led researchers to investigate its potential roles beyond olfaction, such as in cellular signaling, immune response, and tissue development. The study of OBP2A recombinant protein is particularly significant for several reasons: it enables a deeper understanding of olfactory mechanisms and provides insights into the molecular interactions involved in odor detection. Furthermore, the ability to produce OBP2A in recombinant form facilitates the exploration of its structure-function relationships, enabling researchers to identify key residues critical for its binding activity and potential therapeutic applications. As OBP2A may also interact with environmental toxins or pheromones, studying its properties could yield valuable information regarding its function in various ecological contexts. Overall, the research on OBP2A recombinant protein holds promise for advancing our comprehension of sensory biology, as well as its implications in health and disease.
