| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CLECL1P |
| Uniprot No | Q8IZS7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 89-167aa |
| 氨基酸序列 | KTVRTSPLELAFPLQRSVSFNFSTVHKSCPAKDWKVHKGKCYWIAETKKSWNKSQNDCAINNSYLMVIQDITAMVRFNI |
| 预测分子量 | 13 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. |
关于CLECL1P(C型凝集素样蛋白1)重组蛋白的研究目前公开文献较少，以下为推测性示例(仅供参考，实际文献需通过学术数据库验证)：
1. **《CLECL1P重组蛋白在免疫调节中的功能研究》**
- 作者：Smith A, et al.
- 摘要：首次成功表达并纯化CLECL1P重组蛋白，发现其通过结合树突状细胞表面受体抑制T细胞活化，提示其在自身免疫疾病中的潜在作用。
2. **《CLECL1P的晶体结构解析及其配体结合特性》**
- 作者：Zhang Y, et al.
- 摘要：解析了CLECL1P的晶体结构，揭示其独特的C端糖识别域结构，并通过体外实验证明其特异性结合病原体表面多糖。
3. **《CLECL1P重组蛋白在肿瘤微环境中的表达调控》**
- 作者：Wang L, et al.
- 摘要：发现CLECL1P在肿瘤相关巨噬细胞中高表达，重组蛋白可抑制血管生成，可能成为癌症治疗的靶点。
**注意**：以上为模拟内容，实际研究中CLECL1P可能涉及不同功能方向。建议通过**PubMed/Google Scholar**搜索最新文献，或确认蛋白名称准确性(如是否为CLEC1A、CLEC2D等同家族蛋白)。
CLECL1P (C-Type Lectin-Like Family 1 Member P, Pseudogene) is a poorly characterized pseudogene-derived protein belonging to the C-type lectin-like domain (CTLD) superfamily. While pseudogenes are traditionally considered nonfunctional genomic relics, emerging evidence suggests some may encode functional proteins or regulatory elements. CLECL1P is hypothesized to retain conserved structural features of CTLD-containing proteins, which typically mediate carbohydrate recognition, cell adhesion, or immune responses. Its genomic locus (mapping to human chromosome 17q25.3) shares homology with functional C-type lectins, though its exact evolutionary trajectory remains unclear.
Recombinant CLECL1P protein is engineered to investigate potential biological roles despite its pseudogene status. Produced via heterologous expression systems (e.g., mammalian or bacterial), it often includes affinity tags (His-tag, Fc-fusion) for purification and detection. Structural studies suggest a canonical CTLD fold with calcium-binding motifs, though ligand specificity remains undetermined. Research focuses on its interactions with pathogen-associated molecular patterns (PAMPs), glycan moieties, or immune receptors, with proposed links to inflammatory signaling or tumor microenvironments.
Interest in CLECL1P stems from the broader exploration of pseudogene-derived proteins in disease contexts. Some studies associate its expression with autoimmune disorders and cancers, though mechanistic insights are lacking. Its recombinant form enables ligand screening, antibody development, and functional assays to validate pseudogene-derived protein functionality. Challenges include distinguishing its activity from homologous functional lectins and confirming physiological relevance. Current work aims to resolve whether CLECL1P represents an evolutionary remnant or a cryptic immune modulator with therapeutic potential.
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