Analytical Data
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基因名
TPM2
- Application
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别名
AMCD1; DA1; TMSB; Arthrogryposis Multiplex Congenital,Distal,Type 1
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种属
Human
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表达系统
E. coli
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标签
N-His
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纯度
Greater than 95% as determined by SDS-PAGE.
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蛋白编号
P07951
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表达区间
Met1~Leu284
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分子量
42kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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
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.












