Analytical Data
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Gene name
ERa
- Application
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Alternative Names
ERa；HERA；GTPase Era. mitochondrial
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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
P03372
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Expression Region
10-595aa
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AA Sequence
SGMALLHQIQGNELEPLNRPQLKIPLERPLGEVYLDSSKPAVYNYPEGAAYEFNAAAAANAQVYGQTGLPYGPGSEAAAFGSNGLGGFPPLNSVSPSPLMLLHPPPQLSPFLQPHGQQVPYYLENEPSGYTVREAGPPAFYRPNSDNRRQGGRERLASTNDKGSMAMESAKETRYCAVCNDYASGYHYGVWSCEGCKAFFKRSIQGHNDYMCPATNQCTIDKNRRKSCQACRLRKCYEVGMMKGGIRKDRRGGRMLKHKRQRDDGEGRGEVGSAGDMRAANLWPSPLMIKRSKKNSLALSLTADQMVSALLDAEPPILYSEYDPTRPFSEASMMGLLTNLADRELVHMINWAKRVPGFVDLTLHDQVHLLECAWLEILMIGLVWRSMEHPGKLLFAPNLLLDRNQGKCVEGMVEIFDMLLATSSRFRMMNLQGEEFVCLKSIILLNSGVYTFLSSTLKSLEEKDHIHRVLDKITDTLIHLMAKAGLTLQQQHQRLAQLLLILSHIRHMSNKGMEHLYSMKCKNVVPLYDLLLEMLDAHRLHAPTSRGGASVEETDQSHLATAGSTSSHSLQKYYITGEAEGFPATV
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Molecular Weight
67.2 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
Related Products
Protein Description
The study of ERa (estrogen receptor alpha) recombinant proteins is a crucial area of research due to the pivotal role estrogen plays in various biological processes and its implications in disease, particularly in hormone-dependent cancers such as breast cancer. ERa, a type of nuclear hormone receptor, mediates the effects of estrogen by regulating gene expression, influencing cell proliferation, differentiation, and apoptosis. The recombinant production of ERa proteins allows for detailed structural and functional studies, facilitating the understanding of its signaling pathways, ligand binding characteristics, and interaction with other cellular components. Moreover, these proteins can be utilized in drug discovery efforts to identify potential therapeutic agents that can modulate ERa activity, with a focus on developing selective estrogen receptor modulators (SERMs) that can provide beneficial effects without the associated risks of traditional estrogen therapies. This research is further enriched by advancements in molecular biology techniques and protein engineering, which enable the creation of various ERa variants and the development of sophisticated assays to study their functions in vitro and in vivo. Ultimately, the insights gained from ERa recombinant protein studies are critical for advancing our knowledge of estrogen signaling and its broader implications in health and disease management.
