Analytical Data
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Gene name
TTN
- Application
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Alternative Names
CMD1G; CMH9; CMPD4; HMERF; LGMD2J; TMD; Cardiomyopathy,Dilated 1G(Autosomal Dominant)
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Species
Mouse
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
A2ASS6
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Expression Region
Thr34750~Ser34990
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Molecular Weight
33kDa
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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
TTN, or Titin, is a colossal protein that plays a crucial role in the structure and function of striated muscle tissues, being the largest known protein in the human body. Its intricate function is primarily linked to muscle contraction and elasticity, serving as a molecular spring that helps maintain the integrity of the muscle sarcomere during stretching and contraction. Research into TTN has gained momentum due to its involvement in myopathies and cardiomyopathies, with numerous mutations associated with these conditions. The complexity of TTN's structure, comprising over 38,000 amino acids, presents significant challenges for researchers, particularly in deciphering its diverse functional domains and their roles in muscle mechanics. Advances in recombinant protein technology have enabled the production of smaller fragments of TTN, allowing for a more detailed study of its functional properties. Furthermore, elucidating the molecular mechanisms behind TTN-related disorders can pave the way for potential therapeutic strategies, including gene therapy and precision medicine approaches. As the field continues to evolve, the investigation of TTN and its related proteins remains essential for developing a comprehensive understanding of muscle biology and pathology.
