Analytical Data
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Gene name
TNNI1
- Application
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Alternative Names
TNNI1；Troponin I. slow 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
P19237
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Expression Region
1-187aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MPEVERKPKI TASRKLLLKS LMLAKAKECW EQEHEEREAE KVRYLAERIP TLQTRGLSLS ALQDLCRELH AKVEVVDEER YDIEAKCLHN TREIKDLKLK VMDLRGKFKR PPLRRVRVSA DAMLRALLGS KHKVSMDLRA NLKSVKKEDT EKERPVEVGD WRKNVEAMSG MEGRKKMFDA AKSPTSQ
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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 TNNI1 (cardiac troponin I), a crucial regulatory protein in cardiac muscle contraction, has garnered significant interest due to its critical role in heart physiology and pathology. TNNI1 is a component of the troponin complex, which also includes troponin C and troponin T, and it regulates the muscle contraction process in response to calcium ion fluctuations. Research has shown that alterations in TNNI1 expression or mutations can lead to various cardiac diseases, including hypertrophic cardiomyopathy, dilated cardiomyopathy, and heart failure. Shedding light on TNNI1 through recombinant protein studies enables a deeper understanding of its structure-function relationships, its interactions with other cardiac proteins, and its role in the regulation of muscle contraction. Furthermore, the ability to produce recombinant TNNI1 in vitro allows for the development of targeted therapies and diagnostic tools, thus holding promise for improving outcomes in patients with heart disease. Thus, ongoing research into TNNI1 not only enhances our understanding of cardiac biology but also provides avenues for innovative therapeutic strategies to combat cardiovascular disorders.
