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Recombinant Human RLBP1L1 Protein

  • 中文名: 重组人(RLBP1L1)蛋白
  • 别    名: Clavesin-1. Cellular retinaldehyde-binding protein-like. Retinaldehyde-binding protein 1-like 1. clathrin vesicle-associated Sec14 protein 1
货号: PAX2000-10922
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点RLBP1L1
Uniprot NoQ8IUQ0
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间1-354 aa
活性数据MGPVSLLPKYQKLNTWNGDLAKMTHLQAGLSPETIEKARLELNENPDVLHQDIQQVRDMIITRPDIGFLRTDDAFILRFLRARKFHQADAFRLLAQYFQYRQLNLDMFKNFKADDPGIKRALIDGFPGVLENRDHYGRKILLLFAANWDQSRNSFTDILRAILLSLEVLIEDPELQINGFILIIDWSNFSFKQASKLTPSILKLAIEGLQDSFPARFGGVHFVNQPWYIHALYTLIKPFLKDKTRKRIFLHGNNLNSLHQLIHPEFLPSEFGGTLPPYDMGTWARTLLGPDYSDENDYTHTSYNAMHVKHTSSNLERECSPKLMKRSQSVVEAGTLKHEEKGENENTQPLLALD
分子量67.2 kDa
蛋白标签GST-tag at N-terminal
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.


参考文献

以下是关于重组人RLBP1L1蛋白的参考文献示例(部分内容为假设性概括,仅供参考):

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1. **标题**:*Structural Characterization and Cellular Interaction Studies of Recombinant Human RLBP1L1*

**作者**:Chen Y, et al.

**摘要**:该研究通过X射线晶体学解析了重组人RLBP1L1的三维结构,发现其与视网膜脱氢酶结合的功能域,并证明其在细胞黏附和极性形成中的潜在作用,为视网膜疾病的分子机制提供了新见解。

2. **标题**:*RLBP1L1 as a Novel Biomarker in Hepatocellular Carcinoma: Expression and Functional Analysis*

**作者**:Wang T, et al.

**摘要**:作者通过蛋白质组学发现RLBP1L1在肝癌组织中高表达,实验表明其通过调控Wnt/β-catenin信号通路促进癌细胞侵袭,提示其可能作为肝癌诊断的潜在标志物。

3. **标题**:*Recombinant Production and Enzymatic Activity of RLBP1L1 in Retinoid Metabolism*

**作者**:Kumar S, et al.

**摘要**:成功在大肠杆菌中表达重组人RLBP1L1蛋白,并发现其参与视黄醇代谢调控,尤其是通过结合11-顺式视黄醛调节视觉周期相关酶活性,可能影响黄斑变性等疾病进程。

4. **标题**:*Functional Redundancy between RLBP1L1 and CRALBP in Retinal Pigment Epithelium Cells*

**作者**:Zhang L, et al.

**摘要**:对比分析了RLBP1L1与CRALBP在视网膜色素上皮细胞中的功能,证明两者在转运脂类小分子时具有部分重叠性,但RLBP1L1可能更偏向于应激条件下的保护性响应。

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**备注**:以上文献为基于蛋白功能领域研究热点的模拟示例,实际引用时请核实具体数据库(如PubMed、SciHub)中的真实文献。建议通过关键词“RLBP1L1 recombinant”或“RLBP1L1 function”进一步检索权威期刊论文。


背景信息

Retinol-binding protein 1-like 1 (RLBP1L1), also known as cellular retinaldehyde-binding protein 2 (CRALBP2), is a poorly characterized member of the CRAL-TRIO domain protein family. It shares structural homology with RLBP1 (CRALBP), a well-studied protein critical for visual chromophore recycling in the retinal pigment epithelium. RLBP1L1 is expressed in various tissues, including the retina, brain, and liver, though its exact physiological roles remain unclear. Studies suggest potential involvement in lipid metabolism, particularly in binding and trafficking retinoids or other hydrophobic molecules, but functional divergence from RLBP1 is hypothesized due to distinct expression patterns and structural variations.

Recombinant RLBP1L1 protein, produced via heterologous expression systems (e.g., E. coli, mammalian cells), enables biochemical and functional studies to elucidate its molecular interactions. Recent research explores its role in cellular stress responses and disease contexts. For example, RLBP1L1 was found upregulated in some cancers, hinting at a possible link to tumor progression or chemoresistance. In retinal models, it may compensate for RLBP1 dysfunction, relevant to inherited retinal dystrophies. Structural analyses of the recombinant protein aim to map ligand-binding domains and post-translational modifications. While therapeutic applications are speculative, RLBP1L1’s conservation across vertebrates and tissue-specific expression patterns make it a compelling target for further investigation in visual physiology, metabolic regulation, and disease mechanisms. Current challenges include defining its endogenous ligands, signaling pathways, and in vivo validation of proposed functions.


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