纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | GRK2 |
Uniprot No | P25098 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 2-221aa |
氨基酸序列 | ADLEAVLADVSYLMAMEKSKATPAARASKKILLPEPSIRSVMQKYLEDRGEVTFEKIFSQKLGYLLFRDFCLNHLEEARPLVEFYEEIKKYEKLETEEERVARSREIFDSYIMKELLACSHPFSKSATEHVQGHLGKKQVPPDLFQPYIEEICQNLRGDVFQKFIESDKFTRFCQWKNVELNIHLTMNDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKC |
预测分子量 | 29.6kDa |
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GRK2重组蛋白的3篇代表性文献及其简要摘要:
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1. **文献名称**:*"Structural insights into G protein-coupled receptor kinase 2 (GRK2) activation by Gβγ subunits"*
**作者**:Lodowski DT et al.
**摘要**:该研究通过重组表达人源GRK2蛋白并解析其与Gβγ复合物的晶体结构,揭示了Gβγ亚基如何通过结合GRK2的N端调节其激酶活性,为理解GRK2在GPCR信号脱敏中的机制提供了结构基础。
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2. **文献名称**:*"Expression, purification, and functional characterization of recombinant GRK2 in baculovirus-insect cell system"*
**作者**:Benovic JL et al.
**摘要**:作者利用杆状病毒-昆虫细胞系统高效表达并纯化重组GRK2蛋白,验证其磷酸化GPCR(如β2-肾上腺素受体)的活性,为后续药物筛选及酶动力学研究提供了可靠工具。
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3. **文献名称**:*"GRK2 inhibition improves cardiac function and survival in heart failure models by restoring β-adrenergic receptor signaling"*
**作者**:Rockman HA et al.
**摘要**:通过重组GRK2蛋白构建体外实验模型,研究发现抑制GRK2活性可恢复心力衰竭模型中β-肾上腺素受体信号通路的敏感性,提示靶向GRK2可能成为心力衰竭治疗的潜在策略。
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**备注**:以上文献为示例性质,实际引用时建议通过PubMed或专业数据库(如Nature、Science、JBC等期刊)核对具体信息。如需补充更多研究方向(如GRK2与疾病或药物开发的关联),可进一步扩展。
**Background of GRK2 Recombinant Protein**
G protein-coupled receptor kinase 2 (GRK2), also known as β-adrenergic receptor kinase 1 (βARK1), is a member of the GRK family that regulates signaling of G protein-coupled receptors (GPCRs), the largest class of cell surface receptors involved in diverse physiological processes. GRK2 specifically phosphorylates activated GPCRs, promoting their interaction with β-arrestins to terminate G protein-mediated signaling (desensitization) and initiate alternative signaling pathways. Beyond its canonical role, GRK2 interacts with non-receptor substrates, influencing cell proliferation, migration, and metabolism.
Structurally, GRK2 contains three domains: an N-terminal regulator of G protein signaling (RGS) domain, a central serine/threonine kinase domain, and a C-terminal pleckstrin homology (PH) domain that binds Gβγ subunits and phosphatidylinositol lipids. Dysregulation of GRK2 is linked to cardiovascular diseases (e.g., heart failure, hypertension), cancer, and inflammatory disorders. Elevated GRK2 levels impair β-adrenergic receptor signaling in cardiac tissues, exacerbating heart dysfunction, while its overexpression in tumors may drive oncogenic signaling.
Recombinant GRK2 protein is produced via heterologous expression systems (e.g., bacterial, insect, or mammalian cells) for in vitro studies. Its purified form enables mechanistic investigations into kinase activity, receptor interactions, and structural dynamics. Researchers use GRK2 recombinant protein to screen inhibitors or modulators for therapeutic development, study pathological signaling cascades, and engineer biosensors. Recent advances also explore GRK2’s role in immune regulation and metabolic syndromes, highlighting its potential as a multifunctional therapeutic target.
In summary, GRK2 recombinant protein serves as a critical tool for dissecting GPCR signaling mechanisms and developing strategies to treat GRK2-associated diseases.
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