Analytical Data
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Gene name
TNNI2
- Application
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Alternative Names
TNNI2；Troponin I. fast skeletal muscle
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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
P48788
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Expression Region
1-182aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGDEEKRNRAITARRQHLKSVMLQIAATEL EKEESRREAEKQNYLAEHCPPLHIPGSMSEVQELCKQLHAKIDAAEEEKY DMEVRVQKTSKELEDMNQKLFDLRGKFKRPPLRRVRMSADAMLKALLGSK HKVCMDLRANLKQVKKEDTEKERDLRDVGDWRKNIEEKSGMEGRKKMFES ES
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Molecular Weight
24 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
The study of TNNI2, or troponin I type 2, has gained significant traction due to its critical role in cardiac and skeletal muscle contraction regulation. TNNI2 is a key component of the troponin complex, which, together with tropomyosin, regulates the interaction between actin and myosin in muscle fibers. Mutations or dysregulations in TNNI2 have been associated with various myopathies and cardiac diseases, emphasizing the importance of understanding its structure and function. The recombinant production of TNNI2 allows researchers to study its properties in detail, providing insights into muscle physiology and pathophysiology. Furthermore, recombinant TNNI2 can be used to investigate the effects of specific mutations on protein function, aiding in the identification of therapeutic targets for muscle-related disorders. This research not only enhances our comprehension of muscle contraction mechanics but also has potential implications for developing treatments for conditions linked to TNNI2 mutations, such as familial hypertrophic cardiomyopathy and other myopathies. As such, the investigation of TNNI2 recombinant protein represents a vital area of research with broad biomedical applications.
