Analytical Data
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基因名
CASQ
- Application
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别名
PDIB1; CASQ1; Calsequestrin 1,Fast-Twitch,Skeletal Muscle; Calmitine; Calsequestrin, skeletal muscle isoform
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种属
Mouse
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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 90% as determined by SDS-PAGE.
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蛋白编号
O09165
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表达区间
Glu35~Glu249
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分子量
28.4kDa
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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
CASQ (Calsequestrin) is a calcium-binding protein predominantly found in the sarcoplasmic reticulum of muscle cells, playing a critical role in calcium storage and release during muscle contraction. Research into recombinant CASQ proteins has garnered significant attention due to their potential applications in understanding muscle physiology and pathology. CASQ is essential for maintaining calcium homeostasis within the sarcoplasmic reticulum, and its dysfunction is linked to various muscular disorders, including myopathies and heart diseases. The recombinant expression of CASQ allows scientists to study its structural and functional properties in detail, providing insights into its role in calcium signaling and muscle contraction mechanisms. By producing CASQ in heterologous systems, researchers can investigate its interaction with other proteins, its post-translational modifications, and its regulatory functions in muscle cells. These studies contribute to a better understanding of the molecular basis of muscle diseases, offering potential avenues for the development of therapeutic strategies aimed at restoring normal calcium handling in affected tissues. Moreover, the ability to produce CASQ as a recombinant protein paves the way for the development of novel biomaterials and biotechnological applications, where precise control of calcium ions is crucial for various bioengineering processes. Overall, researching recombinant CASQ proteins not only deepens our knowledge of muscle biology but also opens doors for innovative approaches in treating muscle-related conditions.












