纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | SHB |
Uniprot No | Q15464-1 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 395-509aa |
氨基酸序列 | LGERVDPAVPLEKQIWYHGAISRGDAENLLRLCKECSYLVRNSQTSKHDYSLSLRSNQGFMHMKLAKTKEKYVLGQNSPPFDSVPEVIHYYTTRKLPIKGAEHLSLLYPVAVRTL |
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. |
以下是关于SHB重组蛋白的3篇示例参考文献(注:部分文献信息为模拟概括,供参考):
1. **文献名称**: "Functional Analysis of Recombinant SHB Adaptor Protein in Angiogenesis Signaling"
**作者**: Eriksson et al.
**摘要**: 本研究通过表达重组SHB蛋白,揭示了其在血管内皮生长因子(VEGF)信号通路中的作用,证明SHB通过调控PI3K/Akt通路影响血管生成。
2. **文献名称**: "Production and Characterization of Recombinant SHB for Structural Studies"
**作者**: Zhang Y, et al.
**摘要**: 报道了SHB重组蛋白在大肠杆菌中的高效表达与纯化方法,并利用X射线晶体学解析其SH2结构域的三维结构,为功能研究提供结构基础。
3. **文献名称**: "SHB Recombinant Protein Modulates Apoptosis in Breast Cancer Cells"
**作者**: Lee SJ, Kim H.
**摘要**: 通过体外实验发现,重组SHB蛋白可结合EGFR并影响下游凋亡相关蛋白表达,提示其在乳腺癌细胞存活中的调控作用。
4. **文献名称**: "Role of SHB in T-cell Receptor Signaling: Insights from Recombinant Protein Assays"
**作者**: Watanabe T, et al.
**摘要**: 利用重组SHB蛋白进行免疫共沉淀实验,证实其作为衔接分子参与T细胞受体信号转导,影响IL-2分泌和T细胞活化。
(注:以上文献为示例性质,实际引用时请以真实数据库检索结果为准。)
SHB (Src homology 2 domain-containing adaptor protein B) is a signaling adaptor protein involved in regulating diverse cellular processes, including proliferation, differentiation, apoptosis, and angiogenesis. It belongs to the SH2 domain-containing protein family, which mediates protein-protein interactions by binding phosphorylated tyrosine residues on target molecules. SHB contains an N-terminal phosphotyrosine-binding (PTB) domain, a central proline-rich region, and a C-terminal SH2 domain, enabling it to scaffold signaling complexes.
First identified in the 1990s, SHB gained attention for its role in receptor tyrosine kinase (RTK) signaling, particularly downstream of vascular endothelial growth factor receptor (VEGFR), platelet-derived growth factor receptor (PDGFR), and fibroblast growth factor receptor (FGFR). It interacts with phosphorylated receptors or docking proteins, recruiting effectors like PI3K, Grb2. and PLCγ to activate pathways such as MAPK/ERK and AKT, influencing cell survival and motility. SHB also regulates immune responses by modulating T-cell receptor signaling and cytokine production.
Recombinant SHB protein is produced using expression systems (e.g., E. coli, mammalian cells) for in vitro studies. Its purified form enables mechanistic exploration of signaling networks, protein interactions, and therapeutic targeting. Research links SHB dysregulation to cancer progression, cardiovascular disorders, and autoimmune diseases, making it a potential biomarker or drug target. For instance, SHB deletion in mice reveals vascular defects and impaired angiogenesis, underscoring its physiological relevance.
Overall, SHB serves as a critical node in cellular signaling, with recombinant tools advancing both basic research and translational applications in disease mechanisms and intervention strategies.
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