Analytical Data
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Gene name
TPM3
- Application
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Alternative Names
NEM1; TRK; OK/SW-cl.5; TM-5; TM3; TM30; TM30nm; TPMsk3; Hscp30; Gamma-tropomyosin
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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 90% as determined by SDS-PAGE.
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Uniprot
P06753
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Expression Region
Met1~Ile285
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Molecular Weight
40kDa
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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
TPM3 (Tropomyosin 3) is a critical actin-binding protein that plays a significant role in muscle contraction, cell shape maintenance, and cellular motility. In recent years, research on TPM3 has intensified due to its involvement in various pathological conditions, including cancer, where its expression levels are often altered. The protein is known to contribute to the stability of the cytoskeleton, influencing the behavior of cancer cells and their metastatic potential. Moreover, mutations in the TPM3 gene have been linked to certain myopathies, highlighting the importance of understanding its structural and functional properties. The study of recombinant TPM3 proteins has become essential for elucidating the molecular mechanisms underlying these conditions, as it allows researchers to explore the specific interactions between TPM3 and actin filaments. By generating and characterizing recombinant forms of TPM3, scientists aim to investigate how different isoforms and mutations affect the protein's functions. This research not only contributes to a clearer understanding of TPM3's roles in health and disease but also holds potential for the development of therapeutic strategies targeting TPM3-related disorders. Overall, the investigation of TPM3 recombinant proteins is crucial for advancing our knowledge of cytoskeletal dynamics and its implications in various biomedical fields.
