Analytical Data
-
Gene name
Troponin C/TNNC1
- Application
-
Alternative Names
(TN-C)
-
Species
Human
-
Source
Baculovirus
-
Tag
C- His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P63316
-
Expression Region
1-161aa
-
Molecular Weight
19.5 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
Troponin C (TNNC1) is a crucial calcium-binding protein that plays a significant role in cardiac and skeletal muscle contraction regulation. It is a component of the troponin complex, which also includes troponin I and troponin T, and is essential for the muscle's response to calcium ions during the excitation-contraction coupling process. Dysregulation or mutations in the TNNC1 gene can lead to various cardiac and muscular diseases, including hypertrophic cardiomyopathy and skeletal muscle disorders. The synthesis of recombinant Troponin C has garnered attention due to its potential applications in both research and clinical settings; it allows for the detailed study of calcium binding, protein-protein interactions, and the structural dynamics of muscle contractions. Moreover, recombinant TNNC1 can serve as a valuable tool in drug discovery and the development of therapeutic strategies aimed at mitigating the impact of troponin-related diseases. Understanding the functional properties and interactions of Troponin C through recombinant protein studies could also illuminate the fundamental mechanisms of muscle physiology and offer insights into novel treatment modalities for myopathies. As such, TNNC1 recombinant protein research represents a crossroad of biochemistry, genetics, and therapeutic innovation, highlighting the necessity of continued exploration into its structure-function relationships and potential biomedical applications.
