Analytical Data
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Gene name
MYBPC1
- Application
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Alternative Names
MYBPCC; MYBPCS; C-protein, skeletal muscle slow isoform
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Species
Mouse
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Source
E. coli
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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
Q6P6L5
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Expression Region
Met1~Leu277
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Molecular Weight
40kDa
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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
MYBPC1 (Myosin Binding Protein C, cardiac type) is a critical protein in cardiac muscle function, playing a vital role in the structure and regulation of the sarcomere, the fundamental unit of muscle contraction. Mutations in the MYBPC1 gene have been associated with various cardiomyopathies, which can lead to heart failure and other cardiovascular diseases. Given the importance of MYBPC1 in cardiac health, researchers have focused on the recombinant production of MYBPC1 protein to study its structural and functional properties in detail. The expression of MYBPC1 as a recombinant protein enables the investigation of its interactions with other sarcomeric proteins and the elucidation of its role in cardiac mechanics at a molecular level. Moreover, understanding the protein's structure-function relationships can provide insights into the pathophysiological mechanisms underlying MYBPC1-related diseases. This research is crucial for developing targeted therapeutic strategies aimed at mitigating the effects of MYBPC1 mutations in patients with cardiomyopathy, ultimately contributing to the advancement of cardiovascular medicine and improving patient outcomes.











