Analytical Data
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Gene name
TPM2
- Application
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Alternative Names
AMCD1; DA1; TMSB; Arthrogryposis Multiplex Congenital,Distal,Type 1
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P07951
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Expression Region
Met1~Leu284
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Molecular Weight
42kDa
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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 member of the tropomyosin family of proteins, which play critical roles in the regulation of actin filament dynamics and stability in cells. Research into TPM2 has gained momentum due to its essential function in muscle contraction, cell motility, and cytoskeletal organization. Mutations in the TPM2 gene have been linked to various myopathies and other muscle-related disorders, highlighting its importance in human health. The production of recombinant TPM2 proteins has become a valuable tool for studying its structure-function relationships and interactions with other proteins in the actin cytoskeleton. By generating recombinant forms of TPM2, researchers can explore the protein's biophysical properties, elucidate mechanisms of muscle function, and identify potential therapeutic targets for muscle diseases. Furthermore, the production of these proteins in model systems enables detailed biochemical assays, including binding studies and structural analysis, ultimately contributing to a deeper understanding of TPM2's role in both normal physiology and disease states. As investigations into TPM2 continue, it holds the potential for significant insights that could inform the development of novel treatments for myopathies and improve our grasp of muscle biology.
