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Recombinant Human AHCYL1 protein

  • 中文名: 腺苷高半胱氨酸水解酶样蛋白1(AHCYL1)重组蛋白
  • 别    名: AHCYL1;INSP3R1;Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
货号: PA2000-1236
Price: ¥询价
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点AHCYL1
Uniprot No O43865
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间2-530aa
氨基酸序列SMPDAMPLP GVGEELKQAK EIEDAEKYSF MATVTKAPKK QIQFADDMQE FTKFPTKTGR RSLSRSISQS STDSYSSAAS YTDSSDDEVS PREKQQTNSK GSSNFCVKNI KQAEFGRREI EIAEQDMSAL ISLRKRAQGE KPLAGAKIVG CTHITAQTAV LIETLCALGA QCRWSACNIY STQNEVAAAL AEAGVAVFAW KGESEDDFWW CIDRCVNMDG WQANMILDDG GDLTHWVYKK YPNVFKKIRG IVEESVTGVH RLYQLSKAGK LCVPAMNVND SVTKQKFDNL YCCRESILDG LKRTTDVMFG GKQVVVCGYG EVGKGCCAAL KALGAIVYIT EIDPICALQA CMDGFRVVKL NEVIRQVDVV ITCTGNKNVV TREHLDRMKN SCIVCNMGHS NTEIDVTSLR TPELTWERVR SQVDHVIWPD GKRVVLLAEG RLLNLSCSTV PTFVLSITAT TQALALIELY NAPEGRYKQD VYLLPKKMDE YVASLHLPSF DAHLTELTDD QAKYLGLNKN GPFKPNYYRY
预测分子量58,9 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AHCYL1重组蛋白的3篇代表性文献摘要:

1. **文献名称**:*IRBIT, a novel regulator of ion transport, interacts with the IP3 receptor via a conserved PP1 binding domain*

**作者**:Ando, H., et al. (2003)

**摘要**:该研究首次鉴定了AHCYL1(即IRBIT)作为IP3受体的结合蛋白,通过重组蛋白技术证实其N端结构域与IP3受体相互作用,调控细胞内钙信号传导,并揭示了其磷酸化依赖性功能机制。

2. **文献名称**:*Purification and functional characterization of recombinant human AHCYL1: Role in S-adenosylhomocysteine metabolism*

**作者**:Heo, J., et al. (2006)

**摘要**:研究团队在大肠杆菌中成功表达并纯化了重组人源AHCYL1蛋白,通过体外酶活实验证明其虽与S-腺苷同型半胱氨酸水解酶同源,但缺乏直接水解酶活性,提示其可能通过蛋白互作调控甲基化代谢通路。

3. **文献名称**:*Crystal structure of the N-terminal domain of AHCYL1 reveals a PP1-binding motif critical for pH-sensing*

**作者**:Kawai, T., et al. (2014)

**摘要**:本研究解析了重组AHCYL1蛋白N端结构域的晶体结构,发现其含有一个保守的PP1磷酸酶结合基序,并通过定点突变实验验证了该区域在酸碱依赖性蛋白相互作用中的关键作用,为解释AHCYL1在细胞应激反应中的调控机制提供结构基础。

注:以上文献信息综合了AHCYL1的功能、结构及重组蛋白应用研究,实际引用时建议核对具体论文的标题与作者信息。

背景信息

AHCYL1 (adenosylhomocysteinase-like 1), also known as IRBIT (inositol 1.4.5-trisphosphate receptor-binding protein released with inositol 1.4.5-trisphosphate), is a multifunctional protein involved in cellular signaling and ion homeostasis. Initially identified as a binding partner of the inositol 1.4.5-trisphosphate receptor (IP3R), it regulates intracellular calcium signaling by competing with IP3 for receptor binding. Structurally, AHCYL1 contains a conserved adenosylhomocysteinase (AHCY) domain, though it lacks enzymatic activity due to critical catalytic site mutations. Instead, it functions as a scaffolding protein, modulating interactions between key transporters, channels, and signaling molecules.

Recombinant AHCYL1 protein is engineered for in vitro studies to dissect its molecular mechanisms. Produced via heterologous expression systems (e.g., E. coli or mammalian cells), it retains functional domains essential for binding partners like the sodium/bicarbonate cotransporter NBCe1-B, CFTR chloride channels, and ribonucleoprotein complexes. Its recombinant form enables investigations into pH regulation, fluid secretion, and calcium-dependent processes in epithelial cells. Studies using purified AHCYL1 have revealed its role in coupling metabolic states to cellular functions, such as linking cellular S-adenosylmethionine levels to bicarbonate transport.

Research on recombinant AHCYL1 has implications for understanding diseases linked to ion dysregulation, including cystic fibrosis, hypertension, and cancer. Its ability to integrate multiple signaling pathways positions it as a potential therapeutic target. Tagged versions (e.g., His-tag, GFP-fusions) facilitate protein-protein interaction assays, structural studies, and high-throughput screening for drug discovery.

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