| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CITED2 |
| Uniprot No | Q99967 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-270aa |
| 氨基酸序列 | MADHMMAMNH GRFPDGTNGL HHHPAHRMGM GQFPSPHHHQ QQQPQHAFNA LMGEHIHYGA GNMNATSGIR HAMGPGTVNG GHPPSALAPA ARFNNSQFMG PPVASQGGSL PASMQLQKLN NQYFNHHPYP HNHYMPDLHP AAGHQMNGTN QHFRDCNPKH SGGSSTPGGS GGSSTPGGSG SSSGGGAGSS NSGGGSGSGN MPASVAHVPA AMLPPNVIDT DFIDEEVLMS LVIEMGLDRI KELPELWLGQ NEFDFMTDFV CKQQPSRVSC |
| 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3篇关于CITED2重组蛋白的关键文献及其摘要概括：
1. **文献名称**: "Molecular mechanisms of CITED2 function in the developing heart"
**作者**: Bamforth SD et al.
**摘要**: 本研究通过基因敲除小鼠模型，发现CITED2缺失导致心脏发育异常及肾上腺缺陷，揭示了CITED2作为转录共激活因子在胚胎心脏形态发生中的关键作用，并通过重组蛋白实验证明其与TFAP2转录因子的互作机制。
2. **文献名称**: "Regulation of HIF-1alpha function by CITED2 in hypoxic signaling"
**作者**: Sørensen PH et al.
**摘要**: 文章阐明了CITED2通过竞争性结合p300/CBP共激活因子，抑制HIF-1α介导的低氧应答通路。利用重组CITED2蛋白进行体外结合实验，证实其通过CH1结构域阻断HIF-1与p300的相互作用，从而调控血管生成相关基因表达。
3. **文献名称**: "CITED2 deficiency disrupts transcriptional control of embryonic angiogenesis"
**作者**: Dunwoodie SL et al.
**摘要**: 该研究结合转基因小鼠与细胞模型，发现CITED2通过调控VEGF和TGF-β信号通路参与血管生成。重组CITED2蛋白的过表达实验显示其可逆转内皮细胞迁移缺陷，证明其在胚胎血管系统发育中的直接调控功能。
*注：若需更近期文献，建议检索PubMed等数据库，关键词"CITED2 recombinant protein"或结合具体研究领域(如癌症、干细胞)。*
CITED2 (CBP/p300-interacting transactivator with glutamic acid/aspartic acid-rich carboxyl-terminal domain 2) is a multifunctional transcriptional regulator involved in diverse cellular processes, including hypoxia response, embryonic development, and cell differentiation. As a member of the CITED family, it lacks intrinsic DNA-binding capacity but modulates gene expression by serving as a transcriptional cofactor. Its primary mechanism involves competitive binding to the histone acetyltransferase (HAT) domain of p300/CBP, thereby regulating the accessibility of these coactivators to other transcription factors like HIF-1α (hypoxia-inducible factor 1-alpha). This interaction fine-tunes hypoxia-responsive gene networks and influences angiogenesis, energy metabolism, and cellular adaptation to low oxygen conditions.
Recombinant CITED2 protein is engineered through molecular cloning techniques, typically expressed in bacterial (e.g., E. coli) or mammalian systems to ensure proper post-translational modifications. The purified protein retains functional domains critical for its biological activity, including the conserved CR2 domain responsible for p300/CBP interaction. Researchers utilize recombinant CITED2 to investigate its role in developmental pathways, particularly heart formation and neural crest cell migration, where it interacts with TFAP2 transcription factors. Its involvement in TGF-β/Smad and Wnt/β-catenin signaling cascades has also been demonstrated, linking it to cancer progression and fibrosis.
In disease models, CITED2 dysregulation correlates with cardiovascular anomalies, renal pathologies, and tumor metastasis. Recombinant forms enable mechanistic studies of its dual regulatory functions—both enhancing and repressing specific transcriptional programs depending on cellular context. Current applications extend to drug discovery platforms targeting transcriptional coactivator systems and regenerative medicine approaches exploring its role in stem cell maintenance. The protein’s ability to cross-regulate HIF-1α and estrogen receptor pathways positions it as a potential therapeutic node for ischemia-related disorders and hormone-responsive cancers.
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