Analytical Data
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Gene name
RPGR
- Application
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Alternative Names
/
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Species
Human
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Source
HEK293
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Tag
C- hFc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q92834
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Expression Region
54-367aa
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Molecular Weight
62.8
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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
The RPGR (Retinitis Pigmentosa GTPase Regulator) gene is crucial in the study of X-linked retinitis pigmentosa (XLRP), a leading cause of inherited blindness. Mutations in this gene disrupt the function of photoreceptor cells in the retina, leading to progressive vision loss. Understanding the structure and function of the RPGR protein is essential for developing potential gene therapies and treatment options for affected individuals. Researchers have been investigating how RPGR interacts with other proteins involved in phototransduction and retinal health. Recombinant RPGR proteins have been produced to elucidate their structure and functional properties. These studies involve various techniques, including X-ray crystallography and cryo-electron microscopy, to visualize the protein at molecular levels. Characterizing RPGR’s domains and identifying critical interaction sites can offer insights into the mechanisms underlying XLRP and pave the way for therapeutic interventions. Additionally, the creation of RPGR animal models has helped to mimic human disease, providing a platform for testing new treatments. The overarching goal of RPGR research is to better understand its role in vision preservation and develop innovative strategies to combat the debilitating effects of retinitis pigmentosa.
