Analytical Data
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基因名
CCS
- Application
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别名
CCS；Copper chaperone for superoxide dismutase
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
O14618
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表达区间
1-274aa
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氨基酸序列
MGSSHHHHHHSSGLVPRGSHMASDSGNQGTLCTLEFAVQMTCQSCVDAVR KSLQGVAGVQDVEVHLEDQMVLVHTTLPSQEVQALLEGTGRQAVLKGMGS GQLQNLGAAVAILGGPGTVQGVVRFLQLTPERCLIEGTIDGLEPGLHGLH VHQYGDLTNNCNSCGNHFNPDGASHGGPQDSDRHRGDLGNVRADADGRAI FRMEDEQLKVWDVIGRSLIIDEGEDDLGRGGHPLSKITGNSGERLACGII ARSAGLFQNPKQICSCDGLTIWEERGRPIAGKGRKESAQPPAHL
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分子量
31 kDa
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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
Related Products
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Protein Description
The study of CCS (Copper Chaperone for Superoxide Dismutase) recombinant proteins is pivotal in understanding the intricate mechanisms of copper homeostasis and oxidative stress response in cells. CCS plays a crucial role in delivering copper ions to the enzyme superoxide dismutase (SOD1), which is essential for the conversion of harmful superoxide radicals into less toxic compounds. The misfolding or malfunction of SOD1 is associated with neurodegenerative diseases such as Amyotrophic Lateral Sclerosis (ALS). Therefore, researching CCS recombinant proteins not only elucidates the fundamental biological processes involved in metal ion chaperoning but also helps in exploring potential therapeutic avenues for diseases linked to copper dysregulation. The production of recombinant CCS proteins enables detailed structural and functional studies, which can reveal how CCS interacts with SOD1 and other cellular components. Additionally, insights gained from this research can inform drug development strategies aimed at enhancing the delivery of copper to SOD1, potentially mitigating oxidative stress and improving cellular health. Overall, the investigation of CCS and its recombinant forms is a significant step toward uncovering new biological pathways that could lead to innovative treatments for various disorders linked to oxidative damage and metal ion imbalances.
