Analytical Data
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Gene name
TPM1
- Application
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Alternative Names
TPM1；C15orf13；Tropomyosin alpha-1 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
P09493
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Expression Region
1-284aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMDAIKKKMQMLKLDKENALDRAEQAEADKK AAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATD AEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVI ESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAE ERAELSEGQVRQLEEQLRIMDQTLKALMAAEDKYSQKEDRYEEEIKVLSD KLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHALND MTSM
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Molecular Weight
35 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
TPM1 (tropomyosin 1) is a key actin-binding protein that plays a vital role in the regulation of muscle contraction and cellular processes in various tissues. It is a member of the tropomyosin family, which consists of distinct isoforms that are expressed in non-muscle and muscle cells. Research into TPM1 has gained significance due to its involvement in cardiac and skeletal muscle function, as well as its contribution to the structural stability of the cytoskeleton. Mutations in the TPM1 gene have been linked to various myopathies and inherited cardiomyopathies, highlighting its importance in muscle pathology. The recombinant protein of TPM1 is often produced for research purposes to study its biochemical properties and interactions with other proteins, such as actin and myosin. Understanding the mechanisms of TPM1 function could provide insights into muscle disorders and lead to potential therapeutic strategies. Moreover, studying the structure and dynamics of TPM1 through recombinant protein techniques allows for a deeper exploration of tropomyosin's role in cellular signaling and mechanical properties. As a result, ongoing research aims not only to elucidate the molecular underpinnings of muscle function but also to develop targeted interventions for muscle-related diseases that arise from TPM1 dysfunction.
