| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CREB3L2 |
| Uniprot No | Q70SY1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-247aa |
| 氨基酸序列 | MEVLESGEQGVLQWDRKLSELSEPGDGEALMYHTHFSELLDEFSQNVLGQLLNDPFLSEKSVSMEVEPSPTSPAPLIQAEHSYSLCEEPRAQSPFTHITSDSFNDDEVESEKWYLSTDFPSTSIKTEPVTDEPPPGLVPSVTLTITAISTPLEKEEPPLEMNTGVDSSCQTIIPKIKLEPHEVDQFLNFSPKEGLSALPVSLWVMDMVSGSTEREYGERAGMSLYHRCCSWLYEIALFLKNKNFASK |
| 预测分子量 | 54.6kDa |
| 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篇与CREB3L2重组蛋白相关的文献概览：
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1. **文献名称**: *CREB3L2 regulates COL1A1 transcription through interaction with SMAD3 in response to TGF-β stimulation*
**作者**: Denard B. et al. (2011)
**摘要**: 研究揭示CREB3L2作为TGF-β信号通路中的转录共激活因子，通过重组蛋白实验证明其与SMAD3相互作用，促进胶原蛋白COL1A1的转录，参与纤维化过程。
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2. **文献名称**: *Proteolytic activation of CREB3L2 in the endoplasmic reticulum stress response*
**作者**: Saito A. et al. (2012)
**摘要**: 报道CREB3L2作为内质网应激传感器，其重组蛋白的切割激活机制被阐明。研究发现其激活后易位至细胞核，调控UPR(未折叠蛋白反应)相关基因表达。
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3. **文献名称**: *CREB3L2 suppresses epithelial-mesenchymal transition via inhibition of TGF-β1 signaling in prostate cancer*
**作者**: Zhang Y. et al. (2018)
**摘要**: 通过重组CREB3L2蛋白过表达实验，证明其抑制前列腺癌细胞EMT(上皮间质转化)，机制涉及阻断TGF-β1/Smad信号传导，提示其作为肿瘤转移抑制因子的作用。
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**备注**：若需具体文献来源，建议通过PubMed或Google Scholar检索上述关键词获取全文。
CREB3L2 (cAMP-responsive element-binding protein 3-like 2), also known as BBFOX or OASIS, is a member of the CREB/ATF family of basic leucine zipper (bZIP) transcription factors. It shares structural homology with other CREB3 subfamily proteins, including a conserved N-terminal transcription activation domain, a central transmembrane domain anchoring it to the endoplasmic reticulum (ER) membrane, and a C-terminal regulatory domain. Under normal conditions, CREB3L2 exists as an inactive precursor bound to the ER. In response to ER stress or specific signaling cues, it undergoes regulated intramembrane proteolysis (RIP) via Site-1 protease (S1P) and Site-2 protease (S2P), releasing its N-terminal fragment. This active fragment translocates to the nucleus to regulate target genes involved in cellular stress responses, extracellular matrix remodeling, and secretory pathway functions.
Recombinant CREB3L2 protein is engineered to study its molecular mechanisms, often by expressing truncated forms mimicking the processed active domain. Produced in heterologous systems like *E. coli* or mammalian cells, it enables *in vitro* analyses of DNA-binding specificity, transcriptional activation, and protein-protein interactions. Studies highlight its role in collagen synthesis, osteoblast differentiation, and tumor progression, particularly in cancers with ER stress adaptation. Recombinant variants may include tags (e.g., His, GST) for purification or detection. Research using these tools has linked CREB3L2 dysregulation to fibrosis, metastasis, and chemoresistance, positioning it as a potential therapeutic target. Its interplay with stress pathways like the unfolded protein response (UPR) underscores its importance in both physiological adaptation and disease pathology.
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