Analytical Data
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Gene name
MYBPC3
- Application
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Alternative Names
C-protein, cardiac muscle isoform
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Species
Rat
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Source
Yeast
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P56741
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Expression Region
645-864aa
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Molecular Weight
26.1 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Myosin-binding protein C (MYBPC3) is a critical cardiac protein that plays a significant role in the regulation of cardiac muscle contraction and relaxation. Mutations in the MYBPC3 gene have been identified as a leading cause of familial hypertrophic cardiomyopathy (HCM), a genetic disorder characterized by the thickening of the heart muscle, which can lead to severe complications, including heart failure and sudden cardiac death. Understanding the structure and function of MYBPC3 is essential for elucidating the molecular mechanisms underlying HCM. Research on recombinant MYBPC3 proteins allows scientists to investigate the effects of specific mutations on protein function, interaction with other cardiac proteins, and overall impact on muscle contractility. Additionally, such studies enable the development of potential therapeutic strategies aimed at ameliorating the effects of MYBPC3 mutations. Advances in recombinant DNA technology have made it feasible to produce MYBPC3 proteins for structural and functional assays, facilitating a deeper understanding of this crucial protein's role in cardiac physiology. By obtaining precise insights into MYBPC3’s biology, researchers hope to identify biomarkers for early diagnosis and potential targets for gene therapy, offering hope for effective clinical interventions in patients affected by HCM.











