Analytical Data
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Gene name
OPN1MW
- Application
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Alternative Names
(Green cone photoreceptor pigment)(Green-sensitive opsin)(GOP)
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Species
Human
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P04001
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Expression Region
1-364aa
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Molecular Weight
46.6 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
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Protein Description
OPN1MW, a member of the opsin protein family, is a key visual pigment found in the photoreceptor cells of some vertebrates, primarily those adapted to aquatic environments. It plays a crucial role in color vision and light detection, particularly under low-light conditions. Research on OPN1MW has gained significance due to its unique spectral properties that allow it to absorb light in the medium-wavelength range, contributing to the visual capabilities of species that inhabit dimly lit habitats. The study of this recombinant protein not only enhances our understanding of the molecular mechanisms underlying vision but also has implications for evolutionary biology, as it sheds light on the adaptive features of vision across different environments. Furthermore, elucidating the structure and function of OPN1MW through recombinant technologies holds potential applications in fields such as biotechnology and medicine, particularly in developing therapeutic strategies for vision disorders. Understanding the interactions between OPN1MW and other cellular components can uncover the foundational aspects of phototransduction pathways, ultimately enriching the broader field of sensory biology.
