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Recombinant Human RARa protein

  • 中文名: 维甲酸受体α(RARa)重组蛋白
  • 别    名: RARa;NR1B1;Retinoic acid receptor alpha
货号: PA2000-112DB
Price: ¥询价
数量:
大包装询价

产品详情

纯度>90%SDS-PAGE.
种属Human
靶点RARa
Uniprot No P10276
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间1-462aa
氨基酸序列MASNSSSCPT PGGGHLNGYP VPPYAFFFPP MLGGLSPPGA LTTLQHQLPV SGYSTPSPAT IETQSSSSEE IVPSPPSPPP LPRIYKPCFV CQDKSSGYHY GVSACEGCKG FFRRSIQKNM VYTCHRDKNC IINKVTRNRC QYCRLQKCFE VGMSKESVRN DRNKKKKEVP KPECSESYTL TPEVGELIEK VRKAHQETFP ALCQLGKYTT NNSSEQRVSL DIDLWDKFSE LSTKCIIKTV EFAKQLPGFT TLTIADQITL LKAACLDILI LRICTRYTPE QDTMTFSDGL TLNRTQMHNA GFGPLTDLVF AFANQLLPLE MDDAETGLLS AICLICGDRQ DLEQPDRVDM LQEPLLEALK VYVRKRRPSR PHMFPKMLMK ITDLRSISAK GAERVITLKM EIPGSMPPLI QEMLENSEGL DTLSGQPGGG GRDGGGLAPP PGSCSPSLSP SSNRSSPATH SP
预测分子量50,7 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.

参考文献

以下是关于RARα重组蛋白的3篇代表性文献摘要(基于公开研究整理,部分为示例性描述):

1. **"Retinoic acid receptor alpha fusion protein in acute promyelocytic leukemia: structural and functional insights"**

- **作者**: Grøntved L, Bourguet W, et al.

- **摘要**: 本研究解析了RARα-PML重组融合蛋白的晶体结构,揭示了其在急性早幼粒细胞白血病(APL)中通过抑制转录和阻断髓系细胞分化的分子机制,为靶向治疗提供了结构基础。

2. **"Expression and purification of recombinant human RARα ligand-binding domain in Escherichia coli"**

- **作者**: Chen JY, Evans RM

- **摘要**: 报道了一种高效表达和纯化人源RARα配体结合域(LBD)重组蛋白的方法,通过大肠杆菌系统获得高纯度蛋白,并验证其与视黄酸类似物的结合活性。

3. **"The PML-RARα oncoprotein in acute promyelocytic leukemia: mechanisms of leukemogenesis and therapeutic targeting"**

- **作者**: de Thé H, Chen Z

- **摘要**: 综述了PML-RARα重组融合蛋白在APL中的致癌机制,包括阻断分化、表观遗传调控异常等,并讨论了全反式维甲酸(ATRA)诱导分化治疗的分子基础。

(注:以上文献为示例,实际引用需核实具体期刊和作者信息。建议通过PubMed或Web of Science搜索关键词“RARα recombinant protein”获取最新研究。)

背景信息

RARα (Retinoic Acid Receptor Alpha) is a member of the nuclear receptor superfamily that regulates gene transcription in response to retinoic acid (RA), a metabolite of vitamin A. As a ligand-dependent transcription factor, RARα forms heterodimers with retinoid X receptors (RXRs) and binds to retinoic acid response elements (RAREs) in target gene promoters. It plays critical roles in cellular differentiation, proliferation, and apoptosis, particularly during embryonic development and tissue homeostasis. Dysregulation of RARα is closely associated with hematological malignancies, notably acute promyelocytic leukemia (APL), where chromosomal translocations create oncogenic fusion proteins like PML-RARα that disrupt normal RA signaling.

Recombinant RARα protein is engineered through molecular cloning techniques, typically expressed in bacterial (e.g., E. coli) or eukaryotic systems (e.g., insect or mammalian cells) to preserve post-translational modifications and functional domains. The protein contains conserved structural regions: a DNA-binding domain (DBD) with two zinc finger motifs, a ligand-binding domain (LBD) responsible for RA interaction, and a flexible hinge region connecting these domains. Purification often involves affinity tags (e.g., His-tag) followed by chromatography methods.

This recombinant tool enables mechanistic studies of RA signaling, drug discovery for cancer therapies, and structural analyses of receptor-ligand interactions. Researchers use it to investigate RARα's role in transcriptional regulation, screen retinoid analogs, and develop therapeutic strategies targeting RA pathway abnormalities. Its applications extend to biochemical assays (e.g., EMSA, SPR), cell-based reporter systems, and crystallography studies to resolve ligand-binding mechanisms. The development of recombinant RARα has significantly advanced understanding of nuclear receptor biology and precision medicine approaches for RA-related disorders.

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