RYR1 Antibody

Code CSB-PA020619XA01RB
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Product Details

Full Product Name
Rabbit anti-Oryctolagus cuniculus (Rabbit) RYR1 Polyclonal antibody
Uniprot No.
Target Names
RYR1
Alternative Names
RYR1 antibody; Ryanodine receptor 1 antibody; RYR-1 antibody; RyR1 antibody; Skeletal muscle calcium release channel antibody; Skeletal muscle ryanodine receptor antibody; Skeletal muscle-type ryanodine receptor antibody; Type 1 ryanodine receptor antibody
Raised in
Rabbit
Species Reactivity
Oryctolagus cuniculus (Rabbit)
Immunogen
Recombinant Oryctolagus cuniculus (Rabbit) RYR1 protein
Immunogen Species
Oryctolagus cuniculus (Rabbit)
Conjugate
Non-conjugated
Clonality
Polyclonal
Isotype
IgG
Purification Method
Antigen Affinity Purified
Concentration
It differs from different batches. Please contact us to confirm it.
Buffer
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Form
Liquid
Tested Applications
ELISA, WB (ensure identification of antigen)
Protocols
Troubleshooting and FAQs
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Value-added Deliverables
① 200ug * antigen (positive control);
② 1ml * Pre-immune serum (negative control);
Quality Guarantee
① Antibody purity can be guaranteed above 90% by SDS-PAGE detection;
② ELISA titer can be guaranteed 1: 64,000;
③ WB validation with antigen can be guaranteed positive;
Lead Time
Made-to-order (14-16 weeks)

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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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