Analytical Data
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Gene name
Myocilin
- Application
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Alternative Names
Trabecular meshwork-induced glucocorticoid response protein
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Species
Mouse
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Source
Baculovirus
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O70624
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Expression Region
213-490aa
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Molecular Weight
35.2 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
Myocilin is a protein that plays a crucial role in ocular physiology and is primarily associated with the pathogenesis of glaucoma, a leading cause of irreversible blindness worldwide. The research surrounding myocilin has intensified due to its genetic mutations linked to primary open-angle glaucoma (POAG). These mutations often lead to abnormal protein folding and aggregation, resulting in increased intraocular pressure and degeneration of retinal ganglion cells. Recombinant myocilin proteins are essential for elucidating the molecular mechanisms underlying its function and the pathogenicity of the associated mutations. By producing myocilin in sufficient quantities through recombinant DNA technology, researchers can conduct in vitro studies to investigate its structure, biochemical properties, and interaction with other cellular components. Additionally, recombinant myocilin provides a platform for drug screening and the development of gene therapies aimed at correcting the underlying genetic defects. The growing understanding of myocilin's role in cellular homeostasis holds promise for novel therapeutic strategies to prevent or even treat glaucoma, thereby potentially reducing the burden of this prevalent ocular disease. Overall, the study of recombinant myocilin is pivotal in bridging the gap between basic research and clinical applications in the management of glaucoma.
