Recombinant Rabbit Ryanodine receptor 1 (RYR1), partial

Code CSB-YP020619RB
MSDS
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Source Yeast
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Code CSB-EP020619RB
MSDS
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Source E.coli
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Code CSB-EP020619RB-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP020619RB
MSDS
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Source Baculovirus
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Code CSB-MP020619RB
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
RYR1
Uniprot No.
Alternative Names
RYR1; Ryanodine receptor 1; RYR-1; RyR1; Skeletal muscle calcium release channel; Skeletal muscle ryanodine receptor; Skeletal muscle-type ryanodine receptor; Type 1 ryanodine receptor
Species
Oryctolagus cuniculus (Rabbit)
Protein Length
Partial
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

Function
Calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm and thereby plays a key role in triggering muscle contraction following depolarization of T-tubules. Repeated very high-level exercise increases the open probability of the channel and leads to Ca(2+) leaking into the cytoplasm. Can also mediate the release of Ca(2+) from intracellular stores in neurons, and may thereby promote prolonged Ca(2+) signaling in the brain. Required for normal embryonic development of muscle fibers and skeletal muscle. Required for normal heart morphogenesis, skin development and ossification during embryogenesis.
Gene References into Functions
  1. In-depth structural analyses elucidated a novel channel-gating mechanism and a novel ion selectivity mechanism of RyR1. PMID: 27573175
  2. the cryo-electron microscopy structures of rabbit RyR1 in three closed conformations at about 4 A resolution and an open state at 5.7 A, are reported. PMID: 27468892
  3. Data suggest that RyR1 exhibits conformation consistent with an open-channel model sufficient for movement of Ca2+ except for a pore constriction site; molecular dynamics simulations suggest Ca2+ passage could be allowed by rotation of upper portion of pore-lining S6 helix away from 4-fold channel axis and twisting of Ile-4937 at channel constriction site out of the channel pore. PMID: 28584051
  4. Data suggest that reduced SOICR (store overload-induced Ca2+ release) threshold is a common defect of malignant hyperthermia- or central core disease-associated RyR1 mutations; carvedilol (a beta-blocker), like dantrolene (a central muscle relaxant), can suppress RyR1-mediated SOICR. Here, human disease-associated point mutations were induced in recombinant rabbit RyR1 via site-directed mutagenesis. PMID: 28687594
  5. RyR1-G4934A had reduced K(+) conductance and ion selectivity compared with WT. Mutations further increasing the side chain volume at these positions (G4934V and G4941I) resulted in reduced caffeine-induced Ca(2+) release. PMID: 25998124
  6. Structural insights into the roles of divergent regions in RyR1 allosteric regulation during excitation contraction coupling. PMID: 25132084
  7. architecture of rabbit RyR1 at a resolution of 6.1 A, using electron cryomicroscopy PMID: 25470059
  8. closed-state structure of the 2.3-megadalton complex of the rabbit skeletal muscle type 1 RyR (RyR1), solved by single-particle electron cryomicroscopy at an overall resolution of 4.8 A PMID: 25470061
  9. Diminishing S-palmitoylation directly suppresses RyR1 activity as well as stimulus-coupled Ca(2+) release through RyR1. PMID: 24509862
  10. Two regions of the ryanodine receptor calcium channel are involved in Ca(2+)-dependent inactivation PMID: 24521037
  11. Data indicate that S107 increased FKBP12 binding to RyR1 in sarcoplasmic reticulum vesicles in the presence of reduced glutathione and the NO-donor NOC12. PMID: 23349825
  12. These results suggest that the intersubunit contact region between N-terminal domains of RyR1 is a prime target for disease mutations. PMID: 23422674
  13. Sequence data of the ATP binding regions of the RyR1 protein was presented. PMID: 23144945
  14. a 2.2 A resolution crystal structure of the RyR domain revealing a two-fold, symmetric, extended four-helix bundle stabilized by a beta sheet. PMID: 22913516
  15. Coupled events reveal complex interactions among RyR1, differentially modulated by cytosolic ATP/Mg2+ and Ca2+ under ionic conditions. PMID: 22785120
  16. 3D localization of a SPRY2 domain in RYR1 PMID: 21998699
  17. Both basic and acidic amino acid residues of IpTx(a) are involved in triggering substate of RyR1. PMID: 22007141
  18. Chloroform extract of hog barn dust modulates skeletal muscle ryanodine receptor calcium-release channel (RyR1). PMID: 20576841
  19. RyRsl subunit is expressed in corpus cavernosum smooth muscle cells. PMID: 16524180
  20. phosphorylation and K201 acted similarly to change the conformation of RyR1/2 and regulate FKBP12/12.6 binding. PMID: 19661110

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Subcellular Location
Sarcoplasmic reticulum membrane; Multi-pass membrane protein. Sarcoplasmic reticulum. Membrane; Multi-pass membrane protein.
Protein Families
Ryanodine receptor (TC 1.A.3.1) family, RYR1 subfamily
Tissue Specificity
Detected in skeletal muscle (at protein level). Fast- or slow-twitch skeletal muscle.
Database Links

KEGG: ocu:100009540

UniGene: Ocu.2092

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