Analytical Data
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Gene name
RP2
- Application
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Alternative Names
RP2；Protein XRP2
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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
O75695
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Expression Region
1-350aa
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AA Sequence
GCFFSKRRKADKESRPENEEERPKQYSWDQREKVDPKDYMFSGLKDETVGRLPGTVAGQQFLIQDCENCNIYIFDHSATVTIDDCTNCIIFLGPVKGSVFFRNCRDCKCTLACQQFRVRDCRKLEVFLCCATQPIIESSSNIKFGCFQWYYPELAFQFKDAGLSIFNNTWSNIHDFTPVSGELNWSLLPEDAVVQDYVPIPTTEELKAVRVSTEANRSIVPISRGQRQKSSDESCLVVLFAGDYTIANARKLIDEMVGKGFFLVQTKEVSMKAEDAQRVFREKAPDFLPLLNKGPVIALEFNGDGAVEVCQLIVNEIFNGTKMFVSESKETASGDVDSFYNFADIQMGI
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Molecular Weight
66.5 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
RP2, a crucial protein implicated in retinal degeneration, is associated with X-linked retinitis pigmentosa (XLRP), a genetic disorder leading to progressive vision loss. Mutations in the RP2 gene disrupt normal protein function, affecting photoreceptor cells in the retina. Due to the significant role RP2 plays in ciliary function and phototransduction pathways, understanding its molecular mechanisms is essential for developing targeted therapies. Research has focused on elucidating the structure and function of RP2, exploring its interactions with other proteins and cellular components. Advances in recombinant protein technology have enabled the production of RP2 variants for functional studies, elucidating the impact of specific mutations on protein stability and activity. Furthermore, studies utilizing animal models and cellular systems are providing insights into the pathophysiological consequences of RP2 deficiency, paving the way for potential gene therapy approaches. By understanding the intricate biology of RP2, researchers aim to unlock new opportunities for therapeutic interventions to mitigate the effects of XLRP and potentially restore vision in affected individuals.
