Analytical Data
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Gene name
TPM2
- Application
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Alternative Names
TPM2；TMSB；Tropomyosin beta chain
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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
P07951
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Expression Region
14-284aa
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AA Sequence
DKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKEAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKLVILEGELERSEERAEVAESKCGDLEEELKIVTNNLKSLEAQADKYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVAKLEKTIDDLEDEVYAQKMKYKAISEELDNALNDITSL
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Molecular Weight
35.3kDa
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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
TPM2, or tropomyosin 2, is a critical component of the cytoskeletal system, playing essential roles in regulating actin filament dynamics and cellular processes such as muscle contraction, cell motility, and signal transduction. Research on TPM2 has gained momentum due to its involvement in various muscle-related disorders, including nemaline myopathy and other congenital myopathies, as well as its implications in cancer biology, where aberrant expression can influence tumor progression and metastasis. The study of recombinant TPM2 proteins allows researchers to investigate its structural and functional properties in a controlled environment, facilitating a deeper understanding of its role in cellular mechanisms. By engineering variants of TPM2, scientists can decipher the relationships between its structure and function, explore interaction dynamics with other cytoskeletal proteins, and assess how mutations influence its activity. Additionally, recombinant TPM2 proteins serve as valuable tools in drug development and therapeutic strategies aimed at targeting cytoskeletal abnormalities. As the field of molecular medicine progresses, unraveling the complexities of TPM2 function and regulation is paramount, paving the way for potential interventions in related diseases.
