Analytical Data
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基因名
FUBP1
- Application
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别名
FUBP1;Far upstream element-binding 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
Q96AE4
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表达区间
2-644aa
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氨基酸序列
ADYSTVPPP SSGSAGGGGG GGGGGGVNDA FKDALQRARQ IAAKIGGDAG TSLNSNDYGY GGQKRPLEDG DQPDAKKVAP QNDSFGTQLP PMHQQQSRSV MTEEYKVPDG MVGFIIGRGG EQISRIQQES GCKIQIAPDS GGLPERSCML TGTPESVQSA KRLLDQIVEK GRPAPGFHHG DGPGNAVQEI MIPASKAGLV IGKGGETIKQ LQERAGVKMV MIQDGPQNTG ADKPLRITGD PYKVQQAKEM VLELIRDQGG FREVRNEYGS RIGGNEGIDV PIPRFAVGIV IGRNGEMIKK IQNDAGVRIQ FKPDDGTTPE RIAQITGPPD RCQHAAEIIT DLLRSVQAGN PGGPGPGGRG RGRGQGNWNM GPPGGLQEFN FIVPTGKTGL IIGKGGETIK SISQQSGARI ELQRNPPPNA DPNMKLFTIR GTPQQIDYAR QLIEEKIGGP VNPLGPPVPH GPHGVPGPHG PPGPPGPGTP MGPYNPAPYN PGPPGPAPHG PPAPYAPQGW GNAYPHWQQQ APPDPAKAGT DPNSAAWAAY YAHYYQQQAQ PPPAAPAGAP TTTQTNGQGD QQNPAPAGQV DYTKAWEEYY KKMGQAVPAP TGAPPGGQPD YSAAWAEYYR QQAAYYAQTS PQGMPQHPPA PQGQ
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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
FUBP1, or far-upstream element binding protein 1, is a crucial RNA-binding protein that plays significant roles in regulating gene expression, RNA processing, and various cellular processes, including cell proliferation and differentiation. Research on FUBP1 has gained momentum due to its involvement in cancer biology, where it has been linked to the modulation of transcriptional networks affecting tumor growth and metastasis. Dysregulation of FUBP1 has been identified in several malignancies, indicating its potential as a biomarker for cancer diagnosis and prognosis. Moreover, FUBP1 is known to interact with various oncogenes and tumor suppressor genes, influencing their expression and activity. The recombinant protein studies of FUBP1 have been instrumental in elucidating its function and mechanism of action at the molecular level. By producing FUBP1 in recombinant systems, researchers can investigate its binding affinity to target RNA sequences, characterize its structural properties, and assess its role in post-transcriptional regulation. Understanding the biochemical pathways involving FUBP1 has the potential to uncover novel therapeutic targets, making it a significant focus in cancer research and molecular biology. Overall, the study of recombinant FUBP1 not only enhances our knowledge of its biological significance but also opens avenues for developing innovative strategies to combat cancer and other diseases associated with its dysregulation.
