Analytical Data
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Gene name
RYR3
- Application
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Alternative Names
RYR3；HBRR；Ryanodine receptor 3
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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
Q15413
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Expression Region
4636-4870aa
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AA Sequence
HYNNFFFAAHLLDIAMGFKTLRTILSSVTHNGKQLVLTVGLLAVVVYLYTVVAFNFFRKFYNKSEDDDEPDMKCDDMMTCYLFHMYVGVRAGGGIGDEIEDPAGDPYEMYRIVFDITFFFFVIVILLAIIQGLIIDAFGELRDQQEQVREDMETKCFICGIGNDYFDTTPHGFETHTLQEHNLANYLFFLMYLINKDETEHTGQESYVWKMYQERCWDFFPAGDCFRKQYEDQLG
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Molecular Weight
33.5 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
RYR3, or the ryanodine receptor type 3, is a crucial intracellular calcium release channel predominantly found in the brain and in certain other tissues. It plays a pivotal role in regulating calcium homeostasis, which is essential for various cellular processes including muscle contraction, neurotransmitter release, and gene expression. The study of RYR3 has gained significance due to its involvement in several physiological and pathological conditions such as neurodegenerative diseases, cardiac dysfunction, and muscle disorders. Despite its importance, the structural and functional characterization of RYR3 has lagged behind that of its counterparts RYR1 and RYR2, primarily due to challenges associated with obtaining sufficient amounts of functional protein for study. Recent advancements in recombinant protein technology have enabled researchers to express and purify RYR3 efficiently, paving the way for structural studies and functional assays. Understanding the biophysical properties and regulatory mechanisms of RYR3 could provide valuable insights into its role in health and disease, potentially leading to the development of targeted therapies for conditions linked to calcium dysregulation. Continuing research on RYR3 not only enhances our comprehension of calcium signaling but also contributes to a broader understanding of cardiac and neuronal physiology.
