Recombinant Human Ryanodine Receptor 1 (RYR1) Protein (His)

Name: Recombinant Human Ryanodine Receptor 1 (RYR1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-04723P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Ryanodine Receptor 1 (RYR1) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P21817
Target Symbol	RYR1
Synonyms	CCO; Central core disease of muscle; MHS; MHS1; PPP1R137; Protein phosphatase 1 regulatory subunit 137; Ryanodine receptor 1; RYDR; RYR; RYR-1; RyR1; RYR1_HUMAN; sarcoplasmic reticulum calcium release channel; Skeletal muscle calcium release channel; Skeletal muscle ryanodine receptor; Skeletal muscle-type ryanodine receptor; SKRR; Type 1 ryanodine receptor
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	MGDAEGEDEVQFLRTDDEVVLQCSATVLKEQLKLCLAAEGFGNRLCFLEPTSNAQNVPPDLAICCFVLEQSLSVRALQEMLANTVEAGVESSQGGGHRTLLYGHAILLRHAHSRMYLSCLTTSRSMTDKLAFDVGLQEDATGEACWWTMHPASKQRSEGEKVRVGDDIILVSVSSERYLHLSTASGELQVDASFMQTLWNMNPICSRCEEGFVTGGHVLRLFHGHMDECLTISPADSDDQRRLVYYEGGAVCTHARSLWRLEPLRISWSGSHLRWGQPLRVRHVTTGQYLALTEDQGLVVVDASKAHTKATSFCFRISKEKLDVAPKRDVEGMGPPEIKYGESLCFVQHVASGLWLTYAAPDPKALRLGVLKKKAMLHQEGHMDDALSLTRCQQEESQAARMIHSTNGLYNQFIKSLDSFSGKPRGSGPPAGTALPIEGVILSLQDLIIYFEPPSEDLQHEEKQSKLRSLRNRQSLFQEEGMLSMVLNCIDRLNVYTTAAHFAEFAGEEAAESWKEIVNLLYELLASLIRGNRS
Expression Range	1-534aa
Protein Length	Partial
Mol. Weight	63.3kDa
Research Area	Transport
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target 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.
Subcellular Location	Sarcoplasmic reticulum membrane; Multi-pass membrane protein. Sarcoplasmic reticulum.
Protein Families	Ryanodine receptor (TC 1.A.3.1) family, RYR1 subfamily
Database References	HGNC: 10483 OMIM: 117000 KEGG: hsa:6261 STRING: 9606.ENSP00000352608 UniGene: PMID: 28403410 49 RYR1 variants were identified in 47 cases. In recessive cases, facial weakness, neonatal hypotonia, ophthalmoplegia/paresis, ptosis, and scapular winging were more frequently observed than in dominant/de novo cases. Variant mapping revealed patterns of clinical severity across RyR1 domains, including a structural plane of interest within the RyR1 cytosolic shell, in which 84% of variants affected the bridging solenoid. PMID: 30155738 Our FRET-based HTS detects RyR binding of accessory proteins calmodulin (CaM) or FKBP12.6...One compound increased FRET and inhibited RyR1, which was only significant at nM [Ca(2+)], and accentuated without CaM present. PMID: 27760856 Mutations in RYR1 should be considered as a significant cause of rhabdomyolysis and myalgia syndrome in patients with the characteristic combination of rhabdomyolysis, myalgia and cramps, creatine kinase elevation, no weakness and often muscle hypertrophy PMID: 29635721 The ryanodine receptor 1 (RyR1) is mainly expressed in the sarcoplasmic reticulum (SR) of skeletal muscle and is a calcium release channel which is coupled to the dihydropyridine receptor in the T-tubule of the sarcolemma. PMID: 27147545 in our series subarachnoid hemorrhage patients have an increased frequency of rare RYR1 variants PMID: 28750945 Findings signal a potential association between malignant hyperthermia (MH) susceptibility and exertional rhabdomyolysis (ER); the presence of MH-causative mutations and putative deleterious RYR1 variants in ER patients without a history of adverse anesthetic reactions suggests their possible increased risk for MH PMID: 28326467 Thus, RYR1 mutations may lead to prolonged bleeding by altering vascular smooth muscle cell function. The reversibility of the bleeding phenotype emphasizes the potential therapeutic value of dantrolene in the treatment of such bleeding disorders. PMID: 27382027 Results show that in disease-associated RYR1 mutations, there is increased gain and Ca(2+) sensitivity for activation in a site-specific manner which suggest that divergent CICR (Ca(2+) -induced Ca(2+) release) activity may cause various disease phenotypes by specific mutations. PMID: 27586648 the RYR1 SNP rs35364374 was not associated with Aneurysmal Subarachnoid Hemorrhage or its clinical squeal. PMID: 28087430 level of myotubes MTM1 mutations do not dramatically affect calcium homeostasis and calcium release mediated through the ryanodine receptor 1, though they do affect myotube size and nuclear content..mature muscles such as those obtained from patient muscle biopsies exhibit a significant decrease in expression of the ryanodine receptor 1, a decrease in muscle-specific microRNAs and a considerable up-regulation of HDAC4. PMID: 28007904 Allosteric mechanism of RyR1, including a key interaction between a peripheral domain and the Ca-binding EF hand domain PMID: 26492335 fetuses with lethal myopathy were compound heterozygous for a paternally inherited missense variant (c.2113G > A; p.Gly705Arg) and a novel maternally inherited truncating frameshift deletion (c.8843delC; p.Ser2948Cysfs*58) PMID: 27616680 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 results suggest that nine RyR1 mutants associated with skeletal muscle diseases were differently regulated by Ca(2+) and Mg(2+) Four malignant hyperthermia-associated RyR1 mutations in the S2-S3 loop conferred RyR2-type Ca(2+)- and Mg(2+)-dependent channel regulation PMID: 27558158 This review summarizes the progress in the structural determination of RyR by cryoEM and, bearing in mind the leap in resolution provided by the recent implementation of direct electron detection, analyzes the first near-atomic structures of RyR. PMID: 27671094 Data indicate that unlike ryanodine receptor RyRs, inositol 145-trisphosphate receptor IP3Rs are present and continually functional at early stages of cardiomyocyte differentiation. PMID: 27430888 This study reveled that One novel (p.L4578V) and heterozygous missense mutations in RYR1 were identified in 7 chines patients. PMID: 26799446 CaM and S100A1 can concurrently bind to and functionally modulate RyR1 and RyR2, but this does not involve direct competition at the RyR CaM binding site. PMID: 27226555 the RYR1 gene has previously been implicated in the pathogenesis of malignant hyperthermia, (1) this particular variant has only been reported in one other case of malignant hyperthermia PMID: 27555149 this is the first case of a patient with central core disease, carrying a RYR1 mutation in a Korean large family, who had concurrent familial hemophagocytic lymphohistiocytosis. PMID: 25521991 The results provide an intriguing perspective of involvement of misregulated RyR1 splicing in muscular disease. PMID: 26531141 Study describes the important role of RYR1 in skeletal muscle and as a susceptibility locus for malignant hyperthermia and other drug-induced myopathies. [review] PMID: 26709912 This study demonstrated that the RYR1 mutation p.Arg4737Trp associated with susceptibility to malignant hyperthermia. PMID: 26631338 Data show that the local Ca(2+) signals observed within 20 ms upon microinjection of Jurkat cells with nicotinic acid adenine dinucleotide phosphate (NAADP) were sensitive to type 1 ryanodine receptor (RyR1) knockdown. PMID: 26462735 A single nucleotide variant in the RYR1 gene is one of the responsible genes of idiopathic hyper CK-emia (persistent elevation of serum creatine kinase). PMID: 26119398 We report 2 siblings with congenital ptosis and scoliosis who were considered for ptosis surgery but were found to harbor underlying recessive RYR1 mutations. PMID: 26691049 Studies indicate that the ryanodine receptors (RyRs: RyR1, RyR2, RyR3) and inositol 1,4,5-trisphosphate receptors (IP3Rs: IP3R1, IP3R2, IP3R3) are the major Ca(2+) release channels (CRCs) on the endo/sarcoplasmic reticulum (ER/SR). PMID: 25966694 High-intensity interval training exercise induces a ROS-dependent RyR1 fragmentation in muscles of recreationally active subjects, and the resulting changes in muscle fiber Ca(2+)-handling trigger muscular adaptations PMID: 26575622 This study demonistrated that RYR1 mutation releated to Centronuclear myopathy. PMID: 25957634 Phenotype-genotype correlation analysis in 4 families and review of available reports on association of the p.Tyr3933Cys allele with malignant hyperthermia (MH) as well as congenital core myopathies indicates an allelic association with MH susceptibility PMID: 25958340 unlike RyR1 normal WT RyR2 does not bind dantrolene in spite of the fact that the RyR1 dantrolene-binding site (residues 590-609) is conserved in RyR2 PMID: 26009179 investigated spectrum of RYR-1 related disorders in a retrospective cohort study. 61 different mutations were detected, of which 24 were novel. Some mutations are present in both dominant (MHS) and recessive modes (congenital myopathy) of inheritance PMID: 25960145 SPRY2 domain forms two antiparallel beta sheets establishing a core, and four additional modules of which several are required for proper folding PMID: 25370123 Large deletions in the RYR1 gene have been reported in only two cases. Report underlines the broadening spectrum in myopathologic disorders and highlights the concept of 'RYR1-associated/related core myopathies'. PMID: 25747005 Mutations of p.Arg2508 in RYR1 were linked to malignant hyperthermia. PMID: 26381711 RYR1 mutations have to be considered in patients presenting with fever-induced rhabdomyolysis, particularly if recurrent, even without a personal or familial history of MHS. PMID: 25081049 Study reports a homozygous RYR1 null mutation and expand the range of RYR1-related phenotypes to include early lethal foetal akinesia deformation sequence/lethal multiple pterygium syndrome PMID: 25476234 The RyR2-H29D mutation is associated with a clinical phenotype of short-coupled PMVT at rest PMID: 25463374 the authors identified three pathogenic and four novel RYR1 variants, with a further five RYR1 variants previously reported in association with Malignant Hyperthermia PMID: 25658027 RYR1-related myopathy is one of the most frequent causes of congenital myopathy. PMID: 24706162 Patients with one RYR1 mutation displayed significantly higher contractures in the in vitro contracture test than patients without RYR1 mutations PMID: 25047158 R2452W ryanodine receptor variant is associated with malignant hyperthermia. PMID: 25086907 Calcium-dependent energetics of calmodulin domain interactions with regulatory regions of the RYR1 has been characterized. PMID: 25145833 RYR1 causative mutations were identified in six persons. Trends indicated higher mutation identification in those with more definitive clinical episodes of malignant hyperthermia and stronger in vitro contracture test responses. PMID: 25735680 we sequenced the ryanodine receptor 1 (RYR1) gene in 47 patients with DMD searching for malignant hyperthermia causative mutations in the skeletal muscle RYR1 gene PMID: 24557023 Aberrant splicing of RYR1 may alter intracellular Ca(2+) signalling in myotonic dystrophy 1 and 2 myotubes. The differing dysregulation of intracellular Ca(2+) handling in DM1 and DM2 may explain their distinct sarcolemmal hyperexcitabilities. PMID: 23888875 RYR1 missense mutations were identified in 85% of patients with central core disease and were found to cluster in exons 100-102. PMID: 24561095 Ryr1-3 genes all show evvects of positive and purifying selection, as well as correlated evolution with dihydropyridine receptor. PMID: 24254650 R2355W can be included in the list of causative mutations for malignant hyperthermia. V2354M might be a causative mutation. PMID: 24361844

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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