| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Sp1 |
| Uniprot No | P10645 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 19-457aa |
| 氨基酸序列 | LPVNSPMNKGDTEVMKCIVEVISDTLSKPSPMPVSQECFETLRGDERILSILRHQNLLKELQDLALQGAKERAHQQKKHSGFEDELSEVLENQSSQAELKEAVEEPSSKDVMEKREDSKEAEKSGEATDGARPQALPEPMQESKAEGNNQAPGEEEEEEEEATNTHPPASLPSQKYPGPQAEGDSEGLSQGLVDREKGLSAEPGWQAKREEEEEEEEEAEAGEEAVPEEEGPTVVLNPHPSLGYKEIRKGESRSEALAVDGAGKPGAEEAQDPEGKGEQEHSQQKEEEEEMAVVPQGLFRGGKSGELEQEEERLSKEWEDSKRWSKMDQLAKELTAEKRLEGQEEEEDNRDSSMKLSFRARAYGFRGPGPQLRRGWRPSSREDSLEAGLPLQVRGYPEEKKEEEGSANRRPEDQELESLSAIEAELEKVAHQLQALRRG |
| 预测分子量 | 50.9kDa |
| 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. |
以下是关于Sp1重组蛋白的3篇参考文献示例(注：文献为假设性示例，实际引用需核实)：
1. **《重组Sp1转录因子的功能表征及其DNA结合特性》**
- 作者：Kadonaga JT, et al.
- 摘要：研究通过大肠杆菌表达系统纯化重组Sp1蛋白，验证其与DNA启动子区GC框的特异性结合能力，并证明其在体外激活基因转录的作用。
2. **《Sp1锌指结构域的重组表达与突变分析》**
- 作者：Courey AJ, Tjian R
- 摘要：利用重组Sp1蛋白的锌指结构域突变体，揭示其第2、3锌指对DNA结合的关键作用，为Sp1功能调控机制提供结构基础。
3. **《重组Sp1与肿瘤抑制蛋白p53的协同调控机制》**
- 作者：Johnson PF, et al.
- 摘要：通过体外实验证明重组Sp1与p53蛋白在特定启动子区域形成复合物，协同增强肿瘤相关基因(如p21)的转录活性。
注：以上文献信息为示例，实际研究中请根据具体主题检索权威数据库(如PubMed)获取真实文献。
**Background of Sp1 Recombinant Protein**
Sp1 (Specificity Protein 1) is a transcription factor belonging to the SP/KLF family, first identified in 1983 for its role in binding GC-rich promoter regions to regulate gene expression. It plays a pivotal role in cellular processes such as cell growth, apoptosis, differentiation, and immune responses by modulating the transcription of target genes, including housekeeping genes, oncogenes, and tumor suppressors.
Structurally, Sp1 contains three C-terminal zinc finger domains (C2H2-type) that mediate DNA binding to GC-box motifs (5'-GGGCGG-3'), and N-terminal activation domains rich in glutamine and serine/threonine residues, which facilitate interactions with co-activators and the transcriptional machinery. Post-translational modifications (e.g., phosphorylation, glycosylation) further regulate its activity, linking Sp1 to signaling pathways like MAPK and PI3K/Akt.
Recombinant Sp1 protein is produced using expression systems (e.g., *E. coli*, mammalian cells*) engineered to express the human *SP1* gene. Purification often involves affinity tags (e.g., His-tag) for high yield and purity. This recombinant form retains DNA-binding and transcriptional activation capabilities, making it a critical tool *in vitro* for studying gene regulation mechanisms, protein-DNA/cofactor interactions, and epigenetic modulation.
In disease contexts, Sp1 is implicated in cancer (e.g., upregulated in tumors to drive proliferation), neurodegeneration (e.g., amyloid precursor protein regulation), and metabolic disorders. Its recombinant version aids in drug discovery, serving as a target for small molecules or biologics aiming to modulate pathological gene expression.
Overall, Sp1 recombinant protein bridges molecular research and therapeutic development, offering insights into transcriptional control and disease mechanisms.
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