Analytical Data
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Gene name
Cardiac troponin I/Tnni3
- Application
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Alternative Names
(Cardiac troponin I)
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Species
Horse
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q5PYI0
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Expression Region
2-205aa
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Molecular Weight
30.8 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
Cardiac troponin I (cTnI) is a crucial regulatory protein in cardiac muscle contraction, serving as a key biomarker for myocardial injury and heart diseases. Elevated levels of cTnI in the bloodstream are indicative of conditions such as acute myocardial infarction and heart failure, making it a vital target for diagnostic and therapeutic applications. The gene encoding this protein, Tnni3, is specifically expressed in cardiac tissues, differentiating it from its skeletal muscle counterpart. Research into the recombinant expression of cTnI has gained momentum due to its potential in improving diagnostic assays, understanding pathophysiological mechanisms of cardiac diseases, and developing novel therapeutic strategies. Recombinant cTnI enables the production of large quantities of pure protein, facilitating in-depth studies on its structure-function relationships. Such studies are essential for elucidating the molecular pathways involved in cardiac contractility and identifying potential interventions for heart disease. Additionally, the ability to manipulate the cTnI structure through recombinant technology may lead to innovative treatment options, such as targeted gene therapy or protein-based approaches to enhance cardiac function in pathological states. Understanding the properties of cTnI at a molecular level also has implications for the development of new biomarkers that can provide more accurate and timely diagnosis, thereby improving patient outcomes. Overall, the recombination and study of cardiac troponin I represent a significant frontier in cardiovascular research, promising enhanced diagnostic capabilities and therapeutic advancements in the field of cardiology.
