Analytical Data
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Gene name
ROM1
- Application
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Alternative Names
ROM; ROSP1; TSPAN23; Rod Outer Segment Membrane Protein; Tetraspanin-23
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Species
Mouse
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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
P32958
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Expression Region
Arg85~Ala351
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Molecular Weight
33kDa
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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
ROM1 (Retinal Outer Segment Membrane Protein 1) is a critical protein predominantly expressed in the photoreceptor cells of the retina, playing an essential role in the integrity and function of photoreceptor outer segments. Research on ROM1 has gained prominence due to its involvement in photoreceptor cell structure and its implications in retinal diseases, including retinitis pigmentosa and other forms of inherited retinal dystrophies. Understanding the biochemical properties and function of ROM1 is vital, as mutations in the ROM1 gene can disrupt photoreceptor organization, leading to vision loss. Moreover, ROM1 exists as a homomeric and heteromeric complex with other membrane proteins, particularly peripherin-2, contributing to the formation of the disc membranes that are critical for capturing light stimuli. Investigations into the structure, function, and interactions of ROM1 at the molecular level are essential for uncovering the mechanisms underlying phototransduction and retinal health. Additionally, exploring the potential of ROM1 as a therapeutic target or biomarker for retinal diseases has become a focal point for researchers, aiming to develop innovative strategies for diagnosis and treatment of retinal degenerative conditions. As advancements in molecular biology techniques improve, the potential for creating model systems to better understand ROM1's role in health and disease continues to grow, offering promising avenues for future research and therapeutic interventions.
