Recombinant Human Caveolin-3 (CAV3) Protein (GST)

Name: Recombinant Human Caveolin-3 (CAV3) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-09213P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Caveolin-3 (CAV3) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P56539
Target Symbol	CAV3
Synonyms	CAV3; CAV3_HUMAN; Caveolin 3; Caveolin-3; LGMD1C; LQT9; M-caveolin; MGC126100; MGC126101; MGC126129; OTTHUMP00000115603; OTTHUMP00000207105; VIP 21; VIP21
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	MMAEEHTDLEAQIVKDIHCKEIDLVNRDPKNINEDIVKVDFEDVIAEPVGTYSFDGVWKVSYTTFTVSKYWCYRLLSTLLGVPLALLWGFLFACISFCHIWAVVPCIKSYLIEIQCISHIYSLCIRTFCNPLFAALGQVCSSIKVVLRKEV
Expression Range	1-151aa
Protein Length	Full Length
Mol. Weight	44.3kDa
Research Area	Signal Transduction
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	May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. May also regulate voltage-gated potassium channels. Plays a role in the sarcolemma repair mechanism of both skeletal muscle and cardiomyocytes that permits rapid resealing of membranes disrupted by mechanical stress. Mediates the recruitment of CAVIN2 and CAVIN3 proteins to the caveolae.
Subcellular Location	Golgi apparatus membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein. Membrane, caveola; Peripheral membrane protein. Cell membrane, sarcolemma.
Protein Families	Caveolin family
Database References	HGNC: 1529 OMIM: 123320 KEGG: hsa:859 STRING: 9606.ENSP00000341940 UniGene: PMID: 28898996 Case series demonstrates that exercise intolerance, myalgia and rhabdomyolysis may be caused by CAV3 mutations and broadens phenotypic spectrum of caveolinopathies. Percussion-induced rapid muscle contractions were seen in 5 of 6 patients. A previously reported heterozygous mutation in CAV3 (p.T78M) and 3 novel variants (p.V14I, p.F41S, p.F54V) were identified. >50% reduction of caveolin-3 in 5 patients vs controls. PMID: 27312022 our study indicates that TASK-1 is functionally regulated by caveolin-3, possibly via association with each other on the cell surface. These results point out a novel mechanism in the regulation of TASK-1. PMID: 28648645 The caveolin 3 G56S variant is not a clearly pathogenic mutation, but may influence cellular functions and morphologies resulting in an increased cellular vulnerability in terms of a modifying factor. PMID: 27739254 Our results indicate that HCN4 channel function is modulated by cav-3. LQTS-associated mutations of cav-3 differentially influence pacemaker current properties indicating a pathophysiological role in clinical manifestations. PMID: 28648120 This study demonstrated that the Caveolin-3 is aberrantly expressed in skeletal muscle cells in myasthenia gravis. PMID: 27863830 Study characterized the secondary structure, dynamics, and topology of a lipidated full-length human Cav3 construct, demonstrated that the N-terminal domain undergoes a dramatic topological rearrangement in both micelles and vesicles that is reversibly mediated by pH PMID: 27276265 The Cav3 P104L mutation of limb girdle muscular dystrophy-1C leads to disordered glucose metabolism in muscle cells. PMID: 28232187 Data (including data from studies using recombinant proteins that lack typical in-vivo post-translational modifications such as palmitoylation) suggest Cav3 exhibits little tendency to partition into liquid-ordered domains of unilamellar vesicles. PMID: 26859249 MURC/cavin-4, especially in combination with Cav-3, may play a consistent role in the differentiation process of rhabdomyosarcoma. PMID: 26086601 This study demonstrated that cav3 mutation in stinct disorders including limb-girdle muscular dystrophy 1C, rippling muscle disease, and isolated creatine kinase elevation in Greece. PMID: 26185955 In a nonreferred nationwide Danish cohort of SIDS cases, up to 5/66 (7.5%) of SIDS cases can be explained by genetic variants in the sodium channel complex genes. PMID: 25757662 We identified three novel sequence variations (c.183C>G, p.S61R; c.220C>A, p.R74S; c.220C>T, p.R74C) and found evidence that one was associated with hypercreatine kinase-emia PMID: 25630502 our results indicate that inhibition of Cav3 currents by 5,6-epoxyeicosatrienoic acid is an important mechanism controlling the vascular tone. PMID: 24327205 detrimental effect of Cav-3 V82I variant on cell viability may participate in determining the susceptibility to cardiac death. PMID: 24917393 The caveolin-3:p.T78M did not exhibit a long-QT syndrome phenotype. PMID: 24021552 Cav3 is an important negative regulator for cardiac late sodium cutrrent via nNOS dependent direct S-nitrosylation of SCN5A. PMID: 23541953 data show a developmental change in HCN4-Cav3 association in human embryonic stem cell-derived cardiomyocytes. Cav3 expression and its association with ionic channels likely represent a crucial step of cardiac maturation PMID: 23311301 A very high prevalence of previously SIDS-associated variants was identified in exome data from population studies. PMID: 23465283 Kir2.1 loss of function is additive to the increase in late sodium current, prolonging repolarization and leading to arrhythmia generation in Cav3-mediated long qt syndrome 9. PMID: 23640888 These results strongly suggest that cav3 possesses direct interaction with KCa1.1, presumably at the same domain for cav1 binding. PMID: 23237801 Multiple caveolin-3 nonamers bind to a single RyR1 homotetramer. PMID: 23071107 hERG expression in the plasma membrane is regulated by Cav3 via Nedd4-2 PMID: 22879586 Stromal caveolin-3 expression were more frequent in anaplastic carcinoma and diffuse sclerosing variant of papillary carcinoma compared to conventional papillary thyroid carcinoma. PMID: 22236542 Detailed analysis of the voltage-dependence of Ca2+ transients revealed a significant shift of Ca2+ release activation to higher depolarization levels in CAV3 mutated cells. PMID: 21294223 Caveolin 3 expression was decreased in an animal model of left ventricular dysfunction and heart failure. PMID: 21362533 Cav-3 is SUMOylated in a manner that is enhanced by the SUMO E3 ligase PIASy; Cav-3 SUMOylation in the mechanisms for beta(2)AR but not beta(1)AR desensitization PMID: 21362625 -3 defects lead to four distinct skeletal muscle disease phenotypes: limb-girdle muscular dystrophy, rippling muscle disease, distal myopathy, and hyperCKemia[review] PMID: 21496630 functional modulation of the Ca(v)3.2 channels by Cav-3 is important for understanding the compartmentalized regulation of Ca(2+) signaling during normal and pathological processes. PMID: 21084288 Results describe differential effects of the R26Q and P28L caveolin-3 mutants on growth factor signaling. PMID: 20472890 Impaired muscle contraction in gallbladders with cholesterol stones is due to high caveolar levels of cholesterol that inhibits CAV-3 generation; cholesterol increases the caveolar sequestration of CAV-3 and CCK-1R. PMID: 20558763 Genetic analysis revealed a CAV3 c.G136A transition resulting in an A46T missense mutation in a family with rippling muscle disease. PMID: 20229577 Caveolin-3 (Cav3) is a new Cx43-interacting protein. PMID: 19544087 Review addresses caveolin-3 biological functions in muscle cells and describes the muscle and heart disease phenotypes associated with caveolin-3 mutations[REVIEW] PMID: 19584897 A heterozygous 80 G-->A substitution in the caveolin-3 gene is associated with sporadic distal myopathy PMID: 11805270 A naturally occurring caveolin-3 mutation can inhibit signaling involving cholesterol-sensitive raft domains. PMID: 11884389 P28L mutation in the CAV-3 gene and the consequent caveolin-3 deficiency is associated with elevated serum kreatine kinase levels. PMID: 12082049 Effects of deleting a tripeptide sequence observed in muscular dystrophy patients on the conformation of peptides corresponding to the scaffolding domain of caveolin-3. PMID: 12387816 caveolin-3 may play a role in lamellar granule assembly, trafficking, and/or function. PMID: 12648214 severe form of rippling muscle disease associated with homozygous CAV3 mutations. PMID: 12666119 A haploinsufficiency model is proposed in which reduced levels of wild-type caveolin-3, although not rendered dysfunctional due to the caveolin-3 R26Q mutant protein, are insufficient for normal muscle cell function. PMID: 12839838 Adenovirus-mediated overexpression of human caveolin-3 inhibits hypertrophic responses in rat cardiomyocytes. PMID: 12847114 An R27Q missense mutation in the CAV3 gene can lead to various clinical phenotypes including hyper-CK-emia, rippling muscle disease, distal myopathy, and limb-girdle musclar dystrophy 1C. PMID: 12939441 CD36 colocalizes with caveolin-3, suggesting that caveolae may regulate cellular fatty acid uptake by CD36. CD36 expression is higher in type 1 compared with type 2 fibers, whereas caveolin-3 expression is significantly higher in type 2 than in type 1 PMID: 14729862 the importance of dysferlin-caveolin 3 relationship for skeletal muscle integrity PMID: 14749532 Review. Caveolin-3 mutations can result in four distinct, sometimes overlapping, muscle disease phenotypes: limb girdle muscular dystrophy, rippling muscle disease, distal myopathy, and hyperCKemia. PMID: 14981167 A muscle biopsy showed a partial reduction of caveolin-3 at the sarcolemma of muscle fibres.Mutational analysis identified a novel heterozygous mutation and generating a Val-->Met change at codon 57 of the amino acid chain. PMID: 15099591 demonstrate that Cav-3 is specifically expressed in human cardiac and skeletal myocytes, with high specificity and relatively high sensitivity (88%) for tumors with skeletal muscle differentiation PMID: 16082247 The authors describe a family with autosomal dominant rippling muscle disease (RMD) and prominent early-onset toe walking. Molecular analysis revealed a novel heterozygous G > A transition at nucleotide position 136 in exon 2 of the caveolin-3 gene. PMID: 16247063 The co-localization of Cav-3 with COX-2 in the caveolae suggests that the caveolins might play an important role for regulating the function of COX-2. PMID: 16479074

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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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