Analytical Data
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Gene name
TM1
- Application
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Alternative Names
Tropomyosin, fast isoform Short name: Tm-Penm-f
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Species
Penaeus monodon
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
A1KYZ2
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Expression Region
1-284aa
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Molecular Weight
48.8 kDa
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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
TM1, or Transmembrane protein 1, is a protein of significant interest in various fields of biomedical research, particularly in cell biology and neurobiology. Its unique structure and localization within the cellular membrane suggest key roles in signal transduction, cell communication, and possibly in the development of certain diseases. Elevated expression levels of TM1 have been observed in various cancers, indicating its potential as a biomarker for tumor progression and a target for therapeutic intervention. Researchers have been focusing on the functional characterization of TM1 through studies examining its interactions with other cellular proteins and its influence on cellular pathways. Additionally, advances in structural biology techniques, such as cryo-electron microscopy, have provided insights into the three-dimensional configuration of TM1, further elucidating its functional mechanisms. The study of TM1 is also instrumental in understanding the pathophysiology of neurodegenerative disorders, where its dysregulation may contribute to neuroinflammation and neuronal death. Overall, ongoing research on TM1 aims to provide a comprehensive understanding of its biological roles and therapeutic potential, ultimately contributing to the development of novel strategies for disease intervention.
