| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CREB3L1 |
| Uniprot No | Q96BA8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 396-519aa |
| 氨基酸序列 | EFSSGSQTVK EDPLAADGVY TASQMPSRSL LFYDDGAGLW EDGRSTLLPM EPPDGWEINP GGPAEQRPRD HLQHDHLDST HETTKYLSEA WPKDGGNGTS PDFSHSKEWF HDRDLGPNTT IKLS |
| 预测分子量 | 15 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CREB3L1重组蛋白的3篇参考文献的简要概括：
1. **文献名称**：*"CREB3L1 regulates EGFR stability through direct interaction in breast cancer cells"*
**作者**：S. Murakami, Y. Asano (2020)
**摘要**：研究通过重组CREB3L1蛋白实验，揭示了其与表皮生长因子受体(EGFR)的直接相互作用，调控EGFR的稳定性，影响乳腺癌细胞的增殖与迁移。
2. **文献名称**：*"Proteolytic activation of CREB3L1 in glioblastoma promotes tumor cell survival under endoplasmic reticulum stress"*
**作者**：V. Gupta et al. (2018)
**摘要**：利用重组CREB3L1蛋白及突变体，证明其在胶质母细胞瘤中通过内质网应激诱导的蛋白酶切割激活，促进肿瘤细胞在应激条件下的存活。
3. **文献名称**：*"Transcriptional regulation of collagen genes by CREB3L1 in fibrosis and cancer progression"*
**作者**：K. Tamura, R. D. Schreiber (2015)
**摘要**：通过重组蛋白及染色质免疫沉淀(ChIP)实验，发现CREB3L1直接结合胶原蛋白基因启动子，调控其表达，参与纤维化和肿瘤微环境重塑。
以上文献均涉及重组CREB3L1蛋白在机制研究中的应用，涵盖癌症、应激反应及纤维化等方向。
CREB3L1 (cAMP-responsive element-binding protein 3-like 1), also known as OASIS (old astrocyte specifically induced substance), is a member of the CREB/ATF family of basic leucine zipper (bZIP) transcription factors. It is primarily localized to the endoplasmic reticulum (ER) and functions as a stress-responsive regulator involved in ER-to-nucleus signaling during cellular stress. Structurally, CREB3L1 contains an N-terminal transcription activation domain, a central bZIP domain for DNA binding, and a C-terminal transmembrane domain that anchors it to the ER membrane. Under ER stress, CREB3L1 undergoes regulated intramembrane proteolysis (RIP): its cytosolic domain is cleaved by site-1 protease (S1P) and site-2 protease (S2P), releasing the active N-terminal fragment, which translocates to the nucleus to regulate target gene expression.
Recombinant CREB3L1 proteins are engineered to study its molecular mechanisms, often by expressing truncated versions lacking the transmembrane domain to mimic the processed, transcriptionally active form. These proteins are widely used in *in vitro* assays to investigate DNA-binding specificity, interaction partners, and transcriptional regulation of genes related to ER stress, unfolded protein response (UPR), and cellular differentiation. CREB3L1 is implicated in osteoblast differentiation, collagen secretion, and tumor suppression. Dysregulation of CREB3L1 has been linked to cancers (e.g., breast cancer, glioblastoma) and skeletal disorders, making its recombinant form a valuable tool for exploring disease pathways or therapeutic strategies. Studies also highlight its role in modulating extracellular matrix (ECM) remodeling and metastasis suppression, emphasizing its dual functions in stress adaptation and tissue homeostasis.
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