Analytical Data
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Gene name
MYBPC3
- Application
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Alternative Names
MYBPC3；Myosin-binding Protein C. cardiac-type
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q14896
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Expression Region
1-328aa
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AA Sequence
MPEPGKKPVSAFSKKPRSVEVAAGSPAVFEAETERAGVKVRWQRGGSDIS ASNKYGLATEGTRHTLTVREVGPADQGSYAVIAGSSKVKFDLKVIEAEKA EPMLAPAPAPAEATGAPGEAPAPAAELGESAPSPKGSSSAALNGPTPGAP DDPIGLFVMRPQDGEVTVGGSITFSARVAGASLLKPPVVKWFKGKWVDLS SKVGQHLQLHDSYDRASKVYLFELHITDAQPAFTGSYRCEVSTKDKFDCS NFNLTVHEAMGTGDLDLLSAFRRTSLAGGGRRISDSHEDTGILDFSSLLK KRDSFRTPRDSKLEAPAEEDVWEILRQA
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Molecular Weight
51 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
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Protein Description
MYBPC3 (Myosin Binding Protein C, Cardiac Type) is a critical protein involved in the regulation of cardiac muscle contraction. Mutations in the MYBPC3 gene are one of the most common causes of hereditary hypertrophic cardiomyopathy (HCM), a condition characterized by the thickening of the heart muscle, which can lead to heart failure and sudden cardiac death. The study of MYBPC3 recombinant proteins has gained prominence in recent years, primarily to understand the molecular mechanisms underlying HCM and to explore potential therapeutic avenues. By producing MYBPC3 in recombinant forms, researchers can investigate the functional impacts of specific mutations and assess their effects on cardiac muscle performance. This experimental approach enables the development of potential drug candidates and gene therapies aimed at correcting or compensating for the defective protein function. Additionally, examining MYBPC3 in a controlled laboratory setting facilitates the exploration of its interactions with other contractile proteins and provides insights into the structural and biochemical properties that are essential for normal cardiac function. As a result, research on MYBPC3 recombinant proteins not only contributes to the fundamental understanding of cardiac biology but also holds promise for innovative strategies to combat diseases associated with MYBPC3 dysfunction, paving the way for advancements in precision medicine for patients suffering from HCM.
