Analytical Data
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Gene name
RYR1
- Application
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Alternative Names
RYR1；RYDR；Ryanodine receptor 1
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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
P21817
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Expression Region
1-534aa
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AA Sequence
MGDAEGEDEVQFLRTDDEVVLQCSATVLKEQLKLCLAAEGFGNRLCFLEPTSNAQNVPPDLAICCFVLEQSLSVRALQEMLANTVEAGVESSQGGGHRTLLYGHAILLRHAHSRMYLSCLTTSRSMTDKLAFDVGLQEDATGEACWWTMHPASKQRSEGEKVRVGDDIILVSVSSERYLHLSTASGELQVDASFMQTLWNMNPICSRCEEGFVTGGHVLRLFHGHMDECLTISPADSDDQRRLVYYEGGAVCTHARSLWRLEPLRISWSGSHLRWGQPLRVRHVTTGQYLALTEDQGLVVVDASKAHTKATSFCFRISKEKLDVAPKRDVEGMGPPEIKYGESLCFVQHVASGLWLTYAAPDPKALRLGVLKKKAMLHQEGHMDDALSLTRCQQEESQAARMIHSTNGLYNQFIKSLDSFSGKPRGSGPPAGTALPIEGVILSLQDLIIYFEPPSEDLQHEEKQSKLRSLRNRQSLFQEEGMLSMVLNCIDRLNVYTTAAHFAEFAGEEAAESWKEIVNLLYELLASLIRGNRS
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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
RYR1, or Ryanodine Receptor 1, is a crucial calcium release channel primarily found in skeletal muscle, playing a vital role in excitation-contraction coupling. Mutations in the RYR1 gene are linked to several skeletal muscle disorders, such as malignant hyperthermia and centralcore disease, which can have severe clinical implications. Due to its significance in muscle physiology and pathology, the study of RYR1 recombinant protein has gained momentum in recent years. Recombinant RYR1 allows for in-depth investigations into its structural and functional properties, facilitating the understanding of its interaction with various ligands and regulatory proteins. Expression of RYR1 in heterologous systems is essential for generating sufficient quantities of functional protein, which can be used for biophysical studies, structural analysis via techniques like X-ray crystallography or cryo-electron microscopy, and pharmacological testing. Furthermore, the development of assays to screen for mutations that affect RYR1 function can aid in the identification of novel therapeutic approaches to mitigate the effects of associated diseases. Overall, research on RYR1 recombinant protein is integral to unraveling the complex mechanisms underlying muscle contraction and the pathophysiology of related muscle disorders, paving the way for potential clinical advancements.
