| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | BARK |
| 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 | 29.6 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. |
以下是3篇与BARK(β肾上腺素能受体激酶，即GRK2)重组蛋白相关的经典文献摘要：
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1. **文献名称**: "Cloning, expression, and chromosomal localization of beta-adrenergic receptor kinase 2. A new member of the receptor kinase family."
**作者**: Benovic JL, et al.
**摘要**：该研究首次报道了BARK(GRK2)的基因克隆及在昆虫细胞中的重组表达，证实其能特异性磷酸化激活的β2肾上腺素受体，并分析了其染色体定位，为后续激酶功能研究奠定基础。
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2. **文献名称**: "Role of beta gamma subunits of G proteins in targeting the beta-adrenergic receptor kinase to membrane-bound receptors."
**作者**: Pitcher JA, et al.
**摘要**：通过重组BARK蛋白实验，揭示了G蛋白βγ亚基在激酶膜定位中的关键作用，阐明了BARK通过结合Gβγ被招募至细胞膜并磷酸化激活态受体的分子机制。
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3. **文献名称**: "Cardiac function in mice overexpressing the beta-adrenergic receptor kinase or a beta ARK inhibitor."
**作者**: Koch WJ, et al.
**摘要**：利用重组BARK及其抑制肽在转基因小鼠中的表达，证明BARK过表达会导致β肾上腺素受体脱敏和心功能受损，而抑制肽可逆转心衰模型的病理表型，提示其治疗潜力。
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如需具体应用或结构研究的文献，可进一步补充说明研究方向。
BARK (β-adrenergic receptor kinase), also known as GRK2 (G protein-coupled receptor kinase 2), is a serine/threonine kinase critical in regulating G protein-coupled receptor (GPCR) signaling. Discovered in the late 1980s, it phosphorylates agonist-activated β-adrenergic receptors (β-ARs), promoting their interaction with β-arrestin and subsequent receptor desensitization. This process prevents prolonged GPCR activation, maintaining cellular homeostasis. Structurally, BARK contains an N-terminal regulator of G protein signaling (RGS) domain, a central kinase domain, and a C-terminal pleckstrin homology (PH) domain that binds to Gβγ subunits, anchoring it to the plasma membrane upon receptor stimulation.
BARK's role extends beyond β-AR regulation, influencing numerous GPCRs involved in cardiovascular, neurological, and metabolic processes. Dysregulation of BARK/GRK2 is linked to pathologies like heart failure, hypertension, and insulin resistance. For instance, elevated GRK2 levels in heart failure impair β-AR signaling, reducing cardiac responsiveness to catecholamines. Conversely, GRK2 inhibition in preclinical models restores β-AR function and improves outcomes.
Recombinant BARK proteins are engineered using bacterial (e.g., E. coli) or eukaryotic expression systems for structural and functional studies. These proteins enable research into kinase activity, receptor interactions, and inhibitor screening. Tagged variants (e.g., His-tag, GST-fusion) facilitate purification and detection. Recombinant BARK has been pivotal in identifying small-molecule inhibitors (e.g., paroxetine) and elucidating mechanisms of GPCR cross-talk. Its applications span drug discovery, signal transduction studies, and therapeutic targeting for diseases associated with GPCR dysfunction. Ongoing research explores tissue-specific GRK2 modulation as a precision medicine strategy.
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