Analytical Data
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基因名
STIP1
- Application
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别名
STIP1；Stress-induced-phosphoProtein 1
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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
P31948
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表达区间
1-543aa
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氨基酸序列
MEQVNELKEKGNKALSVGNIDDALQCYSEAIKLDPHNHVLYSNRSAAYAK KGDYQKAYEDGCKTVDLKPDWGKGYSRKAAALEFLNRFEEAKRTYEEGLK HEANNPQLKEGLQNMEARLAERKFMNPFNMPNLYQKLESDPRTRTLLSDP TYRELIEQLRNKPSDLGTKLQDPRIMTTLSVLLGVDLGSMDEEEEIATPP PPPPPKKETKPEPMEEDLPENKKQALKEKELGNDAYKKKDFDTALKHYDK AKELDPTNMTYITNQAAVYFEKGDYNKCRELCEKAIEVGRENREDYRQIA KAYARIGNSYFKEEKYKDAIHFYNKSLAEHRTPDVLKKCQQAEKILKEQE RLAYINPDLALEEKNKGNECFQKGDYPQAMKHYTEAIKRNPKDAKLYSNR AACYTKLLEFQLALKDCEECIQLEPTFIKGYTRKAAALEAMKDYTKAMDV YQKALDLDSSCKEAADGYQRCMMAQYNRHDSPEDVKRRAMADPEVQQIMS DPAMRLILEQMQKDPQALSEHLKNPVIAQKIQKLMDVGLIAIR
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分子量
63 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
STIP1 (Stress-Independent Partner 1), also known as HSP70-HSP90 organizing protein, plays a crucial role in the regulation of molecular chaperones, particularly HSP70 and HSP90, which are vital for protein folding, stabilization, and degradation. The study of STIP1 recombinant proteins has gained significant attention due to their involvement in various cellular processes and diseases, including cancer, neurodegenerative disorders, and stress responses. Researchers have been particularly interested in understanding STIP1's mechanism of action and its interactions with different client proteins within the cellular environment, as alterations in STIP1 function can influence disease progression and therapeutic outcomes. By generating recombinant STIP1 proteins, scientists aim to elucidate its structural properties, interactome, and the downstream effects of STIP1-mediated chaperone regulation. This research could pave the way for novel therapeutic strategies targeting STIP1 and related pathways, making it a potential biomarker or therapeutic target in various pathological conditions. The ongoing advancements in recombinant protein technology and structural biology techniques are expected to enhance our understanding of STIP1's biological significance, ultimately contributing to the development of innovative approaches to treat diseases associated with protein misfolding and stress responses.
