Analytical Data
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Gene name
TTN
- Application
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Alternative Names
TTN；Titin
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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
Q8WZ42
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Expression Region
5398-5604aa
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AA Sequence
VFKCSVIGIPTPEVKWYKEYMCIEPDNIKYVISEEKGSHTLKIRNVCLSDSATYRCRAVNCVGEAICRGFLTMGDSEIFAVIAKKSKVTLSSLMEELVLKSNYTDSFFEFQVVEGPPRFIKGISDCYAPIGTAAYFQCLVRGSPRPTVYWYKDGKLVQGRRFTVEESGTGFHNLFITSLVKSDEGEYRCVATNKSGMAESFAALTLT
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Molecular Weight
26.5kDa
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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 (titin) is one of the largest known proteins and plays a crucial role in the structure and function of striated muscle fibers, contributing to their elasticity and stability. It serves as a molecular scaffold, connecting myofilaments and maintaining sarcomere integrity during muscle contraction. Research on TTN recombinant proteins has become increasingly relevant due to their importance in understanding muscle physiology and pathophysiology. Mutations in the TTN gene are linked to various muscular diseases, including dilated cardiomyopathy and skeletal myopathies, making it essential to investigate the functional implications of these variants. By producing recombinant TTN proteins, researchers aim to explore their biochemical properties, interaction dynamics, and the effects of specific mutations on muscle function. This line of inquiry not only enhances our understanding of TTN’s role in muscle mechanics but also aids in the development of therapeutic strategies for TTN-related diseases. Additionally, recombinant TTN proteins provide a valuable tool for investigating the mechanisms underlying muscle contraction and the potential for regenerative therapies, positioning TTN research at the forefront of both basic and applied muscle biology studies.
