Analytical Data
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Gene name
RYR2
- Application
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Alternative Names
RYR2；Ryanodine receptor 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
Q92736
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Expression Region
全长
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AA Sequence
full
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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
RYR2, or Ryanodine Receptor 2, is a crucial calcium release channel located in the sarcoplasmic reticulum of cardiac muscle cells, playing a vital role in the regulation of intracellular calcium levels and, consequently, cardiac contraction. Mutations in the RYR2 gene have been implicated in various cardiac conditions, including catecholaminergic polymorphic ventricular tachycardia (CPVT) and arrhythmias, highlighting its importance in cardiovascular health. Research on RYR2 recombinant proteins focuses on understanding the structural and functional characteristics of the receptor, particularly how specific mutations affect its calcium handling capabilities. This knowledge is essential for developing targeted therapies and interventions for patients with RYR2-associated cardiac disorders. By studying the recombinant RYR2 protein, scientists aim to unravel the molecular mechanisms underlying calcium signaling in heart cells, which may lead to novel pharmacological strategies to modulate RYR2 function and improve heart contractility in disease states. Overall, the study of RYR2 recombinant proteins represents a critical intersection of molecular biology and cardiology, with significant implications for advancing therapeutic approaches in treating cardiac dysregulation.
