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Recombinant Human EBF2 protein

  • 中文名: 早期B-细胞因子2(EBF2)重组蛋白
  • 别    名: EBF2;COE2;Transcription factor COE2
货号: PA1000-8828
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点EBF2
Uniprot No Q9HAK2
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间1-575aa
氨基酸序列MFGIQDTLGR GPTLKEKSLG AEMDSVRSWV RNVGVVDANV AAQSGVALSR AHFEKQPPSN LRKSNFFHFV LALYDRQGQP VEIERTAFVD FVENDKEQGN EKTNNGTHYK LQLLYSNGVR TEQDLYVRLI DSVTKQPIAY EGQNKNPEMC RVLLTHEVMC SRCCEKKSCG NRNETPSDPV IIDRFFLKFF LKCNQNCLKT AGNPRDMRRF QVVLSTTVNV DGHVLAVSDN MFVHNNSKHG RRARRLDPSE ATPCIKAISP SEGWTTGGAM VIIIGDNFFD GLQVVFGTML VWSELITPHA IRVQTPPRHI PGVVEVTLSY KSKQFCKGAP GRFIYTALNE PTIDYGFQRL QKVIPRHPGD PERLAKEMLL KRAADLVEAL YGTPHNNQDI ILKRAADIAE ALYSVPRNPS QLPALSSSPA HSGMMGINSY GSQLGVSISE STQGNNQGYI RNTSSISPRG YSSSSTPQQS NYSTSSNSMN GYSNVPMANL GVPGSPGFLN GSPTGSPYGI MSSSPTVGSS STSSILPFSS SVFPAVKQKS AFAPVIRPQG SPSPACSSGN GNGFRAMTGL VVPPM
预测分子量kDa
蛋白标签His tag N-Terminus
缓冲液PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
稳定性 & 储存条件Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.
Reconstituted protein solution can be stored at 2-8°C for 2-7 days.
Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
复溶Always centrifuge tubes before opening.Do not mix by vortex or pipetting.
It is not recommended to reconstitute to a concentration less than 100μg/ml.
Dissolve the lyophilized protein in distilled water.
Please aliquot the reconstituted solution to minimize freeze-thaw cycles.

参考文献

以下是关于EBF2重组蛋白的3篇参考文献及其摘要概述:

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1. **文献名称**: *"Recombinant EBF2 Protein Production and Functional Characterization in Adipocyte Differentiation"*

**作者**: Smith J, Chen L, et al.

**摘要**: 本研究报道了在大肠杆菌系统中高效表达并纯化EBF2重组蛋白的方法。通过体外实验证明,该重组蛋白能够特异性结合脂肪细胞分化相关基因的启动子区域,并显著促进前脂肪细胞向成熟脂肪细胞的分化,揭示了EBF2在脂肪代谢调控中的关键作用。

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2. **文献名称**: *"Structural Insights into EBF2-DNA Interaction via Crystallographic Analysis of Recombinant Protein"*

**作者**: Wang Y, Kimura S, et al.

**摘要**: 研究者利用昆虫细胞表达系统制备了高纯度EBF2重组蛋白,并通过X射线晶体学解析了其DNA结合结构域的复合物结构。结果显示,EBF2通过特定的β-折叠构象与靶DNA序列结合,为理解其转录调控机制提供了结构基础。

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3. **文献名称**: *"EBF2 Recombinant Protein Modulates Neuronal Differentiation in vitro"*

**作者**: Rodriguez A, Gupta R, et al.

**摘要**: 该研究通过哺乳动物细胞表达系统生成功能性EBF2重组蛋白,并发现其在体外神经元分化模型中显著增强神经突生长和突触相关基因表达。实验表明EBF2可能通过激活Notch信号通路参与神经发育调控。

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**备注**:上述文献信息为模拟示例,实际引用时请根据具体研究通过学术数据库(如PubMed、Google Scholar)检索真实文献。

背景信息

**Background of Recombinant EBF2 Protein**

EBF2 (Early B-Cell Factor 2) is a transcription factor belonging to the Collier/Olf/EBF (COE) family, which plays critical roles in cell differentiation, tissue development, and metabolic regulation. Initially identified for its function in B-cell lineage specification, EBF2 is now recognized to participate in diverse biological processes, including adipogenesis, neuronal development, and bone metabolism. It binds to specific DNA sequences via a conserved DNA-binding domain, regulating the expression of target genes involved in cell fate determination and tissue homeostasis.

Recombinant EBF2 protein is engineered to enable functional studies and therapeutic exploration. Produced using heterologous expression systems (e.g., *E. coli* or mammalian cells), the protein is purified to retain its structural integrity and biochemical activity. Common constructs include full-length EBF2 or truncated variants encoding functional domains, such as the DNA-binding domain or dimerization domain. Affinity tags (e.g., His-tag, GST) are often incorporated to facilitate purification and detection.

Research applications of recombinant EBF2 span *in vitro* and *in vivo* models. It is used to investigate mechanisms of gene regulation, particularly in adipocyte differentiation and neuronal circuit formation. Dysregulation of EBF2 has been linked to metabolic disorders (e.g., obesity), neurodegenerative diseases, and cancer, making it a potential biomarker or therapeutic target. Additionally, recombinant EBF2 serves as a molecular tool in DNA-binding assays, protein interaction studies, and CRISPR/dCas9-based transcriptional activation systems.

Despite progress, challenges remain in optimizing its stability and delivery for clinical applications. Current studies focus on elucidating post-translational modifications and tissue-specific roles to advance its therapeutic potential.

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