| 纯度 | >95%SDS-PAGE. |
| 种属 | Mouse |
| 靶点 | CHODL |
| Uniprot No | Q9CXM0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-216aa |
| 氨基酸序列 | MIRIASLLLG AALLCAQGAF ARRVVSGQKV CFADVKHPCY KMAYFHELSS RVSFQEARLA CESEGGVLL SLENEAEQKL IESMLQNLTK PGTGISDGDF WIGLLRSGDG QTSGACPDLY QWSDGSSSQ FRNWYTDEPS CGSEKCVVMY HQPTANPGLG GPYLYQWNDD RCNMKHNYIC KYEPEIHPT EPAEKPYLTN QPEETHENVV VTEAGIIPN |
| 预测分子量 | 23 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CHODL重组蛋白的3篇构造示例文献(仅供参考，实际文献需通过学术数据库查询)：
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1. **标题**: *"Cloning and Functional Characterization of CHODL as a Novel C-Type Lectin in Cartilage Development"*
**作者**: Zhang L, et al.
**摘要**: 本研究成功克隆并表达了人源CHODL重组蛋白，证实其在软骨细胞分化中通过调控Wnt信号通路促进细胞黏附与增殖，为软骨发育机制提供了新见解。
2. **标题**: *"Structural Analysis of Recombinant CHODL Reveals Its Carbohydrate-Binding Specificity"*
**作者**: Tanaka K, et al.
**摘要**: 通过X射线晶体学解析CHODL重组蛋白的三维结构，发现其C端凝集素结构域特异性结合硫酸软骨素，揭示了其在细胞外基质相互作用中的潜在功能。
3. **标题**: *"CHODL Overexpression Attenuates Osteoarthritis Progression in a Mouse Model"*
**作者**: Chen R, et al.
**摘要**: 利用腺病毒载体表达重组CHODL蛋白，发现其在小鼠骨关节炎模型中抑制软骨降解和炎症因子释放，提示其作为治疗靶点的可能性。
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**注意**：以上文献为示例，实际研究中请通过PubMed、Web of Science或Google Scholar等平台检索真实文献(关键词：CHODL, recombinant protein, lectin, cartilage)。
**Background of CHODL Recombinant Protein**
CHODL (Chondrolectin) is a type I transmembrane protein belonging to the C-type lectin-like domain (CTLD) family, initially identified for its role in embryonic development and tissue differentiation. Structurally, it contains a conserved carbohydrate-recognition domain (CRD) that facilitates interactions with glycoproteins or glycolipids, though its specific ligands remain under investigation. CHODL is predominantly expressed in immune cells, including T lymphocytes and dendritic cells, suggesting a regulatory role in immune responses such as cell adhesion, signaling, and pathogen recognition.
The production of recombinant CHODL protein involves cloning its gene into expression systems (e.g., *E. coli*, yeast, or mammalian cells*) to generate purified, functional protein for research. Mammalian systems are often preferred to ensure proper post-translational modifications, such as glycosylation, critical for ligand-binding activity. Recombinant CHODL enables studies on its molecular interactions, structural dynamics, and downstream signaling pathways.
Research highlights CHODL's involvement in autoimmune diseases, cancer progression, and metabolic disorders. For instance, elevated CHODL levels correlate with poor prognosis in certain cancers, possibly by promoting angiogenesis or immune evasion. In metabolic contexts, it may influence lipid metabolism, linking it to atherosclerosis or obesity. Despite progress, challenges persist in elucidating its precise physiological roles and therapeutic potential. Recombinant CHODL remains a vital tool for unraveling these mechanisms and developing targeted therapies.
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