Analytical Data
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Gene name
ERb
- Application
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Alternative Names
ERb;HER2;MLN19;NEU;Receptor tyrosine-Protein kinase erbB-2
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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
P04626
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Expression Region
720-976aa
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AA Sequence
LRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLEDVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKCWMIDSECRPRFRELVSEF
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Molecular Weight
36.6 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 ERb (Estrogen Receptor beta) recombinant proteins has gained significant attention in recent years due to their potential role in various biological processes and therapeutic applications. Estrogen receptors are critical mediators of estrogenic signaling, which influences reproductive and non-reproductive tissues. While ER alpha has been extensively studied, the less understood ERb exhibits distinct tissue distributions and functional roles. Research indicates that ERb is involved in regulating pathways related to cell proliferation, differentiation, and apoptosis, which are vital in conditions such as cancer, osteoporosis, and cardiovascular diseases. The development of recombinant proteins allows for the detailed investigation of ERb's structure-function relationships, binding affinities, and interactions with co-regulators. These studies not only provide insights into ERb's physiological roles but also open avenues for the design of selective modulators that can target specific signaling pathways. By using recombinant protein technology, researchers can produce ERb in manageable quantities, facilitating high-throughput screening for potential therapeutic compounds. Furthermore, understanding how ERb functions at the molecular level can lead to the development of novel strategies for treatment, especially in hormone-related disorders and cancers. Thus, the exploration of ERb recombinant proteins stands as a promising frontier in biomedical research, with implications for improving therapeutic options and patient outcomes.











