Recombinant Human Myosin-Binding Protein C, Cardiac-Type (MYBPC3) Protein (His-SUMO)

Name: Recombinant Human Myosin-Binding Protein C, Cardiac-Type (MYBPC3) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-02554P
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 Myosin-Binding Protein C, Cardiac-Type (MYBPC3) Protein (His-SUMO) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q14896
Target Symbol	MYBPC3
Synonyms	C protein cardiac muscle isoform; C-protein; cardiac muscle isoform; Cardiac MyBP C; Cardiac MyBP-C; Cardiac myosin binding protein C ; cardiac-type; CMH4; FHC; MYBP C; MYBPC; MYBPC3; Myosin binding protein C cardiac; Myosin binding protein C cardiac-type; Myosin-binding protein C; myosin-binding protein C cardiac type; MYPC3_HUMAN
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MPEPGKKPVSAFSKKPRSVEVAAGSPAVFEAETERAGVKVRWQRGGSDISASNKYGLATEGTRHTLTVREVGPADQGSYAVIAGSSKVKFDLKVIEAEKAEPMLAPAPAPAEATGAPGEAPAPAAELGESAPSPKGSSSAALNGPTPGAPDDPIGLFVMRPQDGEVTVGGSITFSARVAGASLLKPPVVKWFKGKWVDLSSKVGQHLQLHDSYDRASKVYLFELHITDAQPAFTGSYRCEVSTKDKFDCSNFNLTVHEAMGTGDLDLLSAFRRTSLAGGGRRISDSHEDTGILDFSSLLKKRDSFRTPRDSKLEAPAEEDVWEILRQA
Expression Range	1-328aa
Protein Length	Partial
Mol. Weight	50.8kDa
Research Area	Others
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	Thick filament-associated protein located in the crossbridge region of vertebrate striated muscle a bands. In vitro it binds MHC, F-actin and native thin filaments, and modifies the activity of actin-activated myosin ATPase. It may modulate muscle contraction or may play a more structural role.
Protein Families	Immunoglobulin superfamily, MyBP family
Database References	HGNC: 7551 OMIM: 115197 KEGG: hsa:4607 STRING: 9606.ENSP00000442795 UniGene: PMID: 29386531 MYBPC3 does not seem to play a role in anthracycline induced cardiotoxicity. PMID: 29716714 Mutation in MYBPC3 was identified as Restrictive Cardiomyopathy - causing mutation. PMID: 27339502 pathogenic gene mutations in LMNA and MYBPC3 alter RNA splicing and may have a role in heart disease PMID: 28679633 MYBPC3 mutation carriers had a high frequency of ventricular arrhythmia and syncope. An absence of family history of sudden death (SD) and past history of syncope are useful prognostic factors in patients with hypertrophic cardiomyopathy. MYH7 and MYBPC3 mutations did not significantly influence prognosis compared to non-carriers. The patients with the MYBPC3 mutation should be closely followed for the possibility of SD. PMID: 27885498 Replacement Fibrosis was most abundantly present in the hearts with a MYBPC3 mutation that first presented with a Hypertrophic Cardiomyopathy. PMID: 28365402 Mutations in the gene MYBPC3 coding for cardiac myosin-binding protein-C (cMyBP-C), a multi-domain protein, are the most common cause of hypertrophic cardiomyopathy ..This molecular insight suggests that key HCM-causing mutations might significantly modify the native affinity required for the assembly of the domains in cMyBP-C, which is essential for normal cardiac function. PMID: 27267291 Five of the 19 patients (26.3%) had either a pathogenic variant or a likely pathogenic variant in MYBPC3 (n=1), MYH7 (n=1), RYR2 (n=2), or TNNT2 (n=1). All five variants were missense variants that have been reported previously in patients with channelopathies or cardiomyopathies PMID: 28202948 Double heterozygotes for mutations in DSP and MYBPC3 showed a variable clinical presentation of arrhythmogenic cardiomyopathy and hypertrophic cardiomyopathy. PMID: 28699631 Data provide evidence that MYBPC3 mutations constitute the preeminent cause of hypertrophic cardiomyopathy (HCM) and that they are phenotypically indistinguishable from HCM caused by MYH7 mutations. PMID: 29121657 In children and young adults, a 2-parameter 12-lead A-ECG score is retrospectively significantly more sensitive and specific than pooled, age-specific conventional ECG criteria for detecting MYBPC3-HCM and in distinguishing such patients from healthy controls, including endurance-trained athletes. PMID: 27061026 mutations associated with a reduced super-relaxed state in hypertrophic cardiomyopathy PMID: 28658286 Study showed that CACNB2 is a possible candidate hypertrophy-modifying gene contributing to disease variability of MYBPC3-associated familial hypertrophic cardiomyopathy PMID: 28614222 The authors demonstrate myosin tail (S2)-dependent functional regulation of actin-activated human beta-cardiac myosin ATPase. In addition, they show that both S2 and MyBP-C bind to S1 and that phosphorylation of either S1 or MyBP-C weakens these interactions. PMID: 28481356 Our study supports that mutations in MYH7 and MYBPC3 should be the first focus of moleculargenetic analysis in HCM, and that mutations in TNNT2 have a low prevalence in Brazilian population. All mutations detected were missense mutations, whereas two mutations in MYH7 had not been described before. PMID: 27737317 These findings point to the critical role of MYBPC3 during sarcomere assembly in cardiac myocyte differentiation and suggest developmental influences of MYBPC3 truncating mutations on the mature hypertrophic phenotype. PMID: 27620334 The p.Pro108Alafs*9 mutation is associated with HCM, high penetrance, and disease onset in middle age PMID: 28029522 Study shows lack of phenotypic differences between MYH7- and MYBPC3-associated hypertrophic cardiomyopathy when assessed by cardiac magnetic resonance imaging. PMID: 28193612 MYBPC3 and MYH7 were the most common mutated genes, accounting for 27% of the total Hypertrophic Cardiomyopathy patients and 83% of the putative mutations in the main sarcomeric genes. PMID: 27574918 MYBPC3 gene mutation is associated with Early-Onset Hypertrophic Cardiomyopathy. PMID: 27483260 The results showed that MYBPC3 25-bp deletion polymorphism was significantly associated with elevated risk of left ventricular dysfunction (LVD), while TTN 18 bp I/D, TNNT2 5 bp I/D and myospryn K2906N polymorphisms did not show any significant association with LVD. PMID: 27350668 we report a patient presenting with a complex phenotype consisting of severe, adult-onset, dilated cardiomyopathy, hearing loss and developmental delay, in which exome sequencing revealed two genetic variants that are inherited from a healthy mother: a variant, in MYBPC3, that is associated with hereditary cardiomyopathy. PMID: 27173948 5 out of 102 (4.9%) athletes carried mutations: a heterozygous MYH7 Glu935Lys mutation, a heterozygous MYBPC3 Arg160Trp mutation and another heterozygous MYBPC3 Thr1046Met mutation, all of which had been reported as HCM-associated mutations PMID: 26178432 the phosphorylation pattern of sMyBP-C is differentially regulated in response to age and disease, suggesting that phosphorylation plays important roles in these processes. PMID: 26287277 a significant role of MYBPC3 gene mutations in Hypertrophic cardiomyopathy(HCM) disease and can be used for pre-symptomatic diagnosis of at risk family members of affected individuals. PMID: 27348999 Atrial fibrillation occurred in 74 patients with hypertrophic cardiomyopathy (31%), but with no difference among genotype groups (31% in MYBPC3, 37% in MYH7 and 18% in other genotypes, p = 0.15). PMID: 26869393 The detection of MYBPC3 mutation, especially the PTC mutation and double-mutation, may serve as a molecular marker for clinical risk stratification of HCM. PMID: 26090888 Demonstrate that MYBPC3 gene mutations, revealed by next-generation sequencing, were associated with familial and sporadic restrictive cardiomyopathy phenotype in patients. PMID: 26163040 Data indicate that homozygous or compound heterozygous truncating pathogenic myosin binding protein C (MYBPC3) mutations cause severe neonatal cardiomyopathy with features of left ventricular noncompaction and septal defects. PMID: 25335496 Case Report: double cMyBP-C mutation in a patient with end-stage hypertrophic cardiomyopathy. PMID: 25971843 Mutations in the MYBPC3 and CASQ2 genes and six combinations between loci in the MYBPC3, MYH7 and CASQ2 genes were responsible for cardiomyopathy risk in a studied cohort. PMID: 25892673 Although females with MYBPC3 mutations showed later onset of hypertrophic cardiomyopathy, female patients were more symptomatic at diagnosis and had more frequent heart failure events once they had developed hypertrophy. PMID: 25123604 A founder MYBPC3 mutation results in HCM with a high risk of sudden death after the fourth decade of life PMID: 25740977 Mutations in MYBPC3 are associated with cardiomyopathy. [Review] PMID: 26358504 Characterization of the novel splicing mutations in cardiomyopathy genes MYBPC3 and TNNT2. PMID: 25849606 Gene-specific severity of cardiac abnormalities may underlie differences in disease onset and suggests that early initiation of metabolic treatment may be beneficial, in particular, in myosin heavy chain (MYH7) mutation carriers PMID: 24835277 These results show that the N-terminal region of MyBP-C stabilizes the ON state of thin filaments and the OFF state of thick filaments and lead to a novel hypothesis for the physiological role of MyBP-C in the regulation of cardiac contractility. PMID: 25512492 This review summarizes evidence that phosphorylation of MyBP-C is a key regulator of cardiac force and contraction. PMID: 25552695 at the cMyBP-C expression levels in hypertrophic cardiomyopathy patients, cross-bridge kinetics are preserved and that the depressed maximal force development is not explained by perturbation of cross-bridge kinetics PMID: 24186209 A founder MYBPC3 mutation that arose >550 years ago is the predominant cause of hypertrophic cardiomyopathy in Iceland. PMID: 25078086 These results demonstrate that MYBPC3 Val762Asp may be associated with unfavorable hypertrophic cardiomyopathy phenotypes PMID: 25281569 A review of MYBPC3 mutations associated with hypertrophic cardiomyopathy. PMID: 24337823 The structural features of the R502W mutation of myosin bindin protein C are described and discussed. PMID: 25058872 In this review, we will address what is known of cMyBP-C's role as a regulator of contraction as well as its role in HCM[review] PMID: 24240729 cMyBP-C is a key regulator of cardiac contractility. Although mutations in the gene encoding cMyBP-C are a leading cause of hypertrophic cardiomyopathy, little is known about the molecular mechanisms underlying the disease process[review] PMID: 24327208 Change in the ability of cMyBP-C to bind cardiac actin modified filaments might contribute to the development of disease. PMID: 24736382 G263X mutation of MYBPC3 was found in 7 patients with hypertrophic cardiomyopathy in Asturias, Spain. PMID: 23870641 Hypertrophic cardiomyopathy patients with MYBPC3 mutations have a specific miRNA expression profile. PMID: 24083979 N-terminal fragment of cardiac myosin-binding protein C (cMyBP-C) impairs myofilament function in human myocardium PMID: 24509847 cMyBP-C is released in the blood rapidly after cardiac damage and therefore has the potential to positively mark the onset of myocardial infarction. PMID: 24337456

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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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