Analytical Data
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Gene name
ATP2B2
- Application
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Alternative Names
PMCA2; Plasma Membrane Ca2+ Pump 2; Plasma Membrane Calcium-Transporting ATPase 2
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Species
Mouse
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9R0K7
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Expression Region
Ala417~Ile830
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Molecular Weight
76kDa
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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
ATP2B2, also known as the plasma membrane calcium ATPase type 2B, is a crucial enzyme that plays a significant role in maintaining calcium homeostasis in cells by extruding calcium ions from the cytoplasm to the extracellular space. It is highly expressed in various tissues, particularly in the brain, heart, and skeletal muscle. Dysregulation of ATP2B2 has been implicated in several pathological conditions, including cardiovascular diseases, neurodegenerative disorders, and certain cancers. Understanding the function and regulation of ATP2B2 is essential for elucidating its physiological roles and potential therapeutic targets. Recent advances in recombinant protein technology have enabled the expression and purification of ATP2B2, facilitating studies on its structure-function relationships, interaction partners, and the mechanisms of its regulation. This research not only enhances our knowledge of ATP2B2's physiological role but also provides insights into its contributions to disease mechanisms, paving the way for the development of novel therapeutic interventions that target calcium signaling pathways. As scientists continue to explore the nuances of ATP2B2 function, the understanding of its potential as a biomarker or therapeutic target in disease contexts becomes increasingly valuable, underscoring its significance in cellular physiology and pathology.











