纯度 | >85%SDS-PAGE. |
种属 | Human |
靶点 | PIM2 |
Uniprot No | Q9P1W9 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-311aa |
氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSMLTKPLQGPPAPPGTPTPPPGGKDREA FEAEYRLGPLLGKGGFGTVFAGHRLTDRLQVAIKVIPRNRVLGWSPLSDS VTCPLEVALLWKVGAGGGHPGVIRLLDWFE TQEGFMLVLERPLPAQDLFDYITEKGPLGEGPSRCFFGQVVAAIQHCHSR GVVHRDIKDENILIDLRRGCAKLIDFGSGALLHDEPYTDFDGTRVYSPPE WISRHQYHALPATVWSLGILLYDMVCGDIPFERDQEILEAELHFPAHVSP DCCALIRRCLAPKPSSRPSLEEILLDPWMQTPAEDVPLNPSKGGPAPLAW SLLP |
预测分子量 | 37 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PIM2重组蛋白的模拟参考文献示例(注:内容为虚构,仅供格式参考):
1. **标题**: "Functional characterization of recombinant PIM2 kinase in cancer cell survival"
**作者**: Smith J, et al.
**摘要**: 本研究通过大肠杆菌系统表达并纯化PIM2重组蛋白,验证其激酶活性。体外实验表明,PIM2通过磷酸化BAD蛋白抑制肿瘤细胞凋亡,为靶向PIM2的抗癌药物开发提供依据。
2. **标题**: "Crystal structure analysis of human PIM2 kinase domain"
**作者**: Chen L, et al.
**摘要**: 解析PIM2激酶结构域的晶体结构(2.1Å),揭示其ATP结合口袋特征及底物识别机制,为设计选择性抑制剂奠定结构基础。
3. **标题**: "Optimization of PIM2 recombinant protein expression in mammalian systems"
**作者**: Gupta R, et al.
**摘要**: 比较昆虫细胞/HEK293系统中PIM2重组蛋白表达效率,发现哺乳动物系统可保留天然磷酸化修饰,适用于功能研究与高通量筛选。
4. **标题**: "PIM2-mediated signaling in hematopoietic malignancies: Insights from recombinant protein assays"
**作者**: Müller S, et al.
**摘要**: 利用重组PIM2蛋白建立体外激酶检测体系,证实其在白血病细胞中通过调控mTOR通路促进增殖,提示联合靶向治疗的潜在价值。
注:以上文献为示例性质,实际研究中建议通过PubMed/Web of Science等平台检索真实文献。
**Background of PIM2 Recombinant Protein**
PIM2 (Proviral Integration site 2) is a serine/threonine kinase belonging to the PIM kinase family, which includes three isoforms (PIM1. PIM2. PIM3) with overlapping functions in regulating cell proliferation, survival, and apoptosis. Originally identified as a proto-oncogene in murine leukemia virus-induced lymphomas, PIM2 has since been implicated in multiple human cancers, including hematologic malignancies (e.g., lymphoma, multiple myeloma) and solid tumors. Its overexpression is often linked to poor prognosis, resistance to chemotherapy, and dysregulation of key signaling pathways, such as PI3K/AKT/mTOR and JAK/STAT.
Recombinant PIM2 protein is engineered for research applications, typically produced in *E. coli* or mammalian expression systems to ensure proper folding and post-translational modifications. This purified protein retains enzymatic activity, enabling *in vitro* studies to investigate its kinase function, substrate interactions, and response to inhibitors. Researchers use it in kinase assays, drug screening, and structural studies to design targeted therapies.
Structurally, PIM2 lacks a regulatory domain, rendering it constitutively active and dependent on transcription for activity modulation. Its substrate repertoire includes proteins involved in cell cycle progression (e.g., CDC25A) and apoptosis (e.g., BAD), highlighting its role in promoting tumor survival.
The development of PIM2 recombinant protein has accelerated the study of its oncogenic mechanisms and its potential as a therapeutic target. Small-molecule inhibitors of PIM2 are under investigation, though challenges remain in achieving isoform selectivity and minimizing off-target effects. Additionally, PIM2's involvement in immune regulation and metabolic processes underscores its broader biological significance beyond cancer.
In summary, PIM2 recombinant protein serves as a critical tool for unraveling the kinase's pathological roles and advancing precision oncology strategies.
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