| 纯度 | >95%SDS-PAGE. |
| 种属 | mouse |
| 靶点 | CRELD2 |
| Uniprot No | Q9CYA0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-350aa |
| 氨基酸序列 | MHLLLAAAFG LLLLLPPPGA VASRKPTMCQ RCRTLVDKFN QGMANTARKN FGGGNTAWEE KTLSKYEFSE IRLLEIMEGL CDSSDFECNQ LLEQQEEQLE AWWQTLKKEH PNLFEWFCVH TLKACCLPGT YGPDCQECQG GSERPCSGNG YCSGDGSRQG DGSCQCHTGY KGPLCIDCTD GFFSLQRNET HSICSACDES CKTCSGPSNK DCIQCEVGWA RVEDACVDVD ECAAETSPCS DGQYCENVNG SYTCEDCDST CVGCTGKGPA NCKECIAGYT KESGQCTDID ECSLEEKACK RKNENCYNVP GSFVCVCPEG FEETEDACVQ TAEGKVTEEN PTQPPSREDL |
| 预测分子量 | 38 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CRELD2重组蛋白的3篇参考文献示例(注：部分内容为模拟概括，具体文献需通过数据库核实)：
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1. **文献名称**: *"CRELD2 regulates endoplasmic reticulum stress signaling and cell survival"*
**作者**: Smith A, et al.
**摘要**: 研究揭示了CRELD2在内质网应激反应中的作用，通过重组蛋白表达实验证明其与BiP/GRP78的相互作用，调控未折叠蛋白反应通路，影响细胞凋亡与存活。
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2. **文献名称**: *"Recombinant CRELD2 protein modulates β-catenin signaling in cancer progression"*
**作者**: Tanaka K, et al.
**摘要**: 利用大肠杆菌系统表达并纯化CRELD2重组蛋白，发现其通过抑制Wnt/β-catenin信号通路抑制肿瘤细胞迁移，提示其可能作为癌症治疗的潜在靶点。
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3. **文献名称**: *"Structural and functional analysis of CRELD2 in cardiac development"*
**作者**: Johnson R, et al.
**摘要**: 通过重组CRELD2蛋白的晶体结构解析，发现其EGF样结构域对心脏发育关键受体(如Notch)的调控机制，为先天性心脏病研究提供分子基础。
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**注意事项**：
- 以上为模拟文献，实际研究中建议通过PubMed/Google Scholar以“CRELD2 recombinant protein”为关键词检索最新论文。
- CRELD2研究多集中于内质网应激、癌症及心脏疾病领域，重组蛋白技术常被用于互作或功能验证实验。
CRELD2 (Cysteine-Rich with EGF-Like Domains 2) is a member of the CRELD family of proteins, which are evolutionarily conserved and implicated in cell adhesion, signaling, and developmental processes. Originally identified through homology to CRELD1. a protein linked to cardiac malformations in humans, CRELD2 shares structural features such as N-terminal signal peptides, epidermal growth factor (EGF)-like domains, and conserved cysteine residues that likely facilitate disulfide bond formation. However, unlike CRELD1. its precise biological role remains less defined.
Recombinant CRELD2 refers to the protein produced via genetic engineering, typically expressed in heterologous systems like *E. coli* or mammalian cell lines (e.g., HEK293) to study its function. The recombinant form enables controlled investigation of CRELD2’s interactions and activities, overcoming challenges posed by its low endogenous expression. Purification often involves affinity tags (e.g., His-tag) followed by chromatographic methods, with quality verified by SDS-PAGE, Western blot, or mass spectrometry.
Emerging studies suggest CRELD2 plays roles in endoplasmic reticulum (ER) stress responses and the unfolded protein response (UPR), potentially acting as a chaperone or modulator of protein folding. It has been associated with pathological conditions, including cancer progression, neurodegenerative diseases, and cardiovascular disorders. For example, elevated CRELD2 levels correlate with tumor invasiveness in certain cancers, while its dysregulation may contribute to ER stress-related apoptosis in neurons.
Despite these insights, mechanistic details remain sparse. Recombinant CRELD2 tools are pivotal for structural studies (e.g., crystallography) and functional assays (e.g., binding partner screens). Challenges include optimizing soluble expression due to its cysteine-rich nature and resolving post-translational modification patterns in eukaryotic systems. Ongoing research aims to clarify CRELD2’s physiological relevance, signaling pathways, and therapeutic potential, positioning it as a target for diseases linked to ER dysfunction or developmental anomalies.
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