| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CILP |
| Uniprot No | O75339 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 22-724aa |
| 氨基酸序列 | MASMTGGQQMGRGHHHHHHGNLYFQGGEFRQTMLTQSVRRVQPGKKNPSI FAKPADTLESPGEWTTWFNIDYPGGKGDYERLDAIRFYYGDRVCARPLRL EARTTDWTPAGSTGQVVHGSPREGFWCL NREQRPGQNCSNYTVRFLCPPGSLRRDTERIWSPWSPWSKCSAACGQTGV QTRTRICLAEMVSLCSEASEEGQHCMGQDCTACDLTCPMGQVNADCDACM CQDFMLHGAVSLPGGAPASGAAIYLLTKTPKLLTQTDSDGRFRIPGLCPD GKSILKITKVKFAPIVLTMPKTSLKAATIKAEFVRAETPYMVMNPETKAR RAGQSVSLCCKATGKPRPDKYFWYHNDTLLDPSLYKHESKLVLRKLQQHQ AGEYFCKAQSDAGAVKSKVAQLIVIASDETPCNPVPESYLIRLPHDCFQN ATNSFYYDVGRCPVKTCAGQQDNGIRCRDAVQNCCGISKTEEREIQCSGY TLPTKVAKECSCQRCTETRSIVRGRVSAADNGEPMRFGHVYMGNSRVSMT GYKGTFTLHVPQDTERLVLTFVDRLQKFVNTTKVLPFNKKGSAVFHEIKM LRRKKPITLEAMETNIIPLGEVVGEDPMAELEIPSRSFYRQNGEPYIGKV KASVTFLDPRNISTATAAQTDLNFINDEGDTFPLRTYGMFSVDFRDEVTS EPLNAGKVKVHLDSTQVKMPEHISTVKLWSLNPDTGLWEEEGDFKFENQR RNKR |
| 预测分子量 | 82 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CILP(软骨中间层蛋白)重组蛋白的示例文献(内容为假设性概括，建议通过学术数据库核实具体文献)：
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1. **文献名称**：*Recombinant expression and purification of human CILP in mammalian cells for functional studies*
**作者**：Tanaka K, et al.
**摘要**：研究利用哺乳动物表达系统成功表达并纯化具有生物活性的重组人CILP蛋白，验证其与Ⅱ型胶原的结合能力，为研究CILP在软骨代谢中的作用提供工具。
2. **文献名称**：*CILP inhibits TGF-β/Smad signaling via direct interaction with fibrillin-1 in osteoarthritis*
**作者**：Wang H, et al.
**摘要**：通过重组CILP蛋白体外实验，发现其通过结合原纤维蛋白1(fibrillin-1)抑制TGF-β/Smad信号通路，揭示了CILP在骨关节炎中促进软骨退化的机制。
3. **文献名称**：*Development of a CILP-based ELISA assay for early diagnosis of cartilage degeneration*
**作者**：Müller R, et al.
**摘要**：研究利用重组CILP蛋白作为抗原，开发了高灵敏度的ELISA检测方法，证实血清CILP水平与早期骨关节炎患者软骨损伤程度呈正相关。
4. **文献名称**：*Cryo-EM structure of the C-terminal domain of CILP reveals its role in extracellular matrix assembly*
**作者**：Chen L, et al.
**摘要**：通过冷冻电镜解析重组CILP蛋白C端结构域的三维结构，阐明其调控细胞外基质组装的关键区域，为靶向药物设计提供结构基础。
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**提示**：实际文献可通过PubMed、Web of Science等平台，以关键词“CILP recombinant protein”、“CILP AND osteoarthritis”检索获取。
CILP (Cartilage Intermediate Layer Protein) is a glycoprotein predominantly found in the extracellular matrix (ECM) of articular cartilage and intervertebral discs. Initially identified in the intermediate layer of cartilage, it exists as two isoforms (CILP1 and CILP2) encoded by separate genes. Structurally, CILP contains N-terminal hydrophobic domains, tandem leucine-rich repeats (LRRs), and a C-terminal zona pellucida (ZP) domain, which facilitate ECM interactions. Its expression is regulated by mechanical stress and inflammatory cytokines, linking it to cartilage homeostasis.
Functionally, CILP modulates growth factor signaling pathways, particularly TGF-β and IGF-1. CILP1 inhibits TGF-β activity by binding to latent TGF-β binding proteins, while CILP2 interacts with IGF-1 receptors, influencing chondrocyte metabolism. Dysregulation of CILP is implicated in degenerative joint diseases, including osteoarthritis (OA) and intervertebral disc degeneration (IDD), where elevated CILP levels correlate with ECM degradation and impaired tissue repair.
Recombinant CILP proteins, produced via bacterial or mammalian expression systems, are critical tools for studying these mechanisms. They enable structural analysis, ligand-receptor interaction studies, and high-throughput drug screening. In therapeutic contexts, recombinant CILP variants are explored for their potential to restore growth factor balance or serve as disease biomarkers. However, challenges remain in maintaining post-translational modifications essential for native functionality when using prokaryotic systems. Current research focuses on optimizing expression platforms and elucidating isoform-specific roles in tissue degeneration and regeneration.
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