关键信息
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基因名
OCEL1
- 应用
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别名
OCEL1；Occludin/ELL domain-containing Protein 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
Q9H607
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表达区间
1-264aa
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氨基酸序列
MHNPDGSASP TADPGSELQT LGQAARRPPP PRAGHDAPRR TRPSARKPLS CFSRRPMPTR EPPKTRGSRG HLHTHPPGPG PPLQGLAPRG LKTSAPRPPC QPQPGPHKAK TKKIVFEDEL LSQALLGAKK PIGAIPKGHK PRPHPVPDYE LKYPPVSSER ERSRYVAVFQ DQYGEFLELQ HEVGCAQAKL RQLEALLSSL PPPQSQKEAQ VAARVWREFE MKRMDPGFLD KQARCHYLKG KLRHLKTQIQ KFDDQGDSEG SVYF
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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.
质检流程
相关产品
背景信息
OCEL1, a member of the OCEL family, has garnered significant attention in the field of molecular biology due to its intriguing role in cellular processes and potential therapeutic applications. Research into OCEL1's structure and function has revealed that this recombinant protein may play a crucial role in various signaling pathways, influencing cell growth, differentiation, and apoptosis. Its unique properties, including specific binding affinities and interactions with other biomolecules, make it a valuable target for understanding disease mechanisms, particularly in cancer and cardiovascular disorders. Advances in recombinant protein technology have facilitated the efficient production and purification of OCEL1, allowing researchers to explore its functional implications in greater detail. By employing techniques such as X-ray crystallography and mass spectrometry, scientists aim to elucidate the 3D structure of OCEL1 and its interaction with cellular partners. Additionally, studying the post-translational modifications of OCEL1 could provide insights into its regulatory mechanisms and biological activity. Overall, the investigation of OCEL1 as a recombinant protein not only enhances our understanding of its biological functions but also opens new avenues for developing targeted therapies and biotechnological applications, emphasizing the importance of this protein in current biomedical research.
