Analytical Data
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Gene name
CHM
- Application
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Alternative Names
Choroideremia protein Rab escort protein 1 Short name:REP-1 TCD protein
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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
P24386
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Expression Region
1-653aa
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Molecular Weight
77.5 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
Related Products
Protein Description
The study of CHM recombinant proteins is rooted in the growing interest in understanding the molecular mechanisms underlying various genetic disorders and the development of targeted therapies. CHM, or Choroideremia, is a rare X-linked recessive genetic disease caused by mutations in the CHM gene, leading to progressive vision loss due to retinal degeneration. Research into the recombinant protein form of the CHM gene aims to explore its functional properties and potential therapeutic applications, as understanding the structure and function of this protein can provide insights into disease mechanisms. Additionally, the production of CHM recombinant proteins allows for the development of gene therapy approaches and protein replacement strategies that could potentially restore function in affected individuals. Recent advances in genetic engineering techniques enable the efficient expression and purification of these proteins, facilitating both in vitro and in vivo studies. Such research is critical not only for potentially developing effective treatments for Choroideremia but also for broader implications in the fields of ophthalmology and gene therapy, enhancing our overall understanding of retinal diseases and genetic disorders.
