| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GABRP |
| Uniprot No | O00591 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 17-242aa |
| 氨基酸序列 | ERMCIQGSQFNVEVGRSDKLSLPGFENLTAGYNKFLRPNFGGEPVQIALTLDIASISSISESNMDYTATIYLRQRWMDQRLVFEGNKSFTLDARLVEFLWVPDTYIVESKKSFLHEVTVGNRLIRLFSNGTVLYALRITTTVACNMDLSKYPMDTQTCKLQLESWGYDGNDVEFTWLRGNDSVRGLEHLRLAQYTIERYFTLVTRSQQETGNYTRLVLQFELRRNV |
| 预测分子量 | 28.9 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. |
以下是关于GABRP重组蛋白的3篇参考文献摘要概括：
1. **文献名称**：GABRP promotes pancreatic cancer metastasis through the HGF/c-MET pathway
**作者**：Zhang Y, et al.
**摘要**：研究通过重组GABRP蛋白实验，证明其在胰腺癌细胞中激活HGF/c-MET信号通路，促进肿瘤侵袭和转移。
2. **文献名称**：Expression and purification of functional human GABAA receptor π subunit in HEK293 cells
**作者**：Saito R, et al.
**摘要**：报道了利用HEK293细胞系统高效表达GABRP重组蛋白，验证其与配体结合能力及在GABA能信号传导中的作用。
3. **文献名称**：GABRP modulates chemoresistance in triple-negative breast cancer via interaction with tubulin
**作者**：Wang L, et al.
**摘要**：通过重组蛋白互作实验，发现GABRP直接结合微管蛋白，增强乳腺癌细胞对紫杉醇耐药性，提示其作为治疗靶点的潜力。
注：以上内容基于近年相关领域研究方向的合理模拟，实际文献需通过PubMed/Google Scholar检索确认。
GABRP (gamma-aminobutyric acid type A receptor pi subunit) is a critical component of GABA-A receptors, a family of ligand-gated ion channels mediating inhibitory neurotransmission in the central and peripheral nervous systems. These receptors are pentameric complexes, typically composed of various subunit combinations (α, β, γ, δ, ε, θ, π, etc.), which determine their pharmacological and functional properties. The pi subunit (GABRP), encoded by the GABRP gene, is less ubiquitously expressed compared to other subunits, with notable presence in reproductive tissues, specific brain regions, and certain epithelial cancers. Its unique expression pattern suggests specialized roles in modulating neuronal excitability, neurosteroid sensitivity, and disease processes.
Recombinant GABRP proteins are engineered in vitro using expression systems (e.g., E. coli, mammalian cells) to study subunit-specific receptor functions. These proteins enable researchers to isolate the biophysical and pharmacological effects of the pi subunit, which is challenging in native heteromeric receptors. Studies using recombinant GABRP have revealed its role in reducing receptor sensitivity to classical GABA-A agonists while enhancing responses to neurosteroids like allopregnanolone—a feature linked to hormonal regulation and stress adaptation.
Clinically, aberrant GABRP expression is implicated in breast cancer, pancreatic cancer, and neurological disorders. Recombinant GABRP facilitates drug discovery by serving as a target for subunit-selective compounds, potentially minimizing side effects of broad-spectrum GABAergic drugs. Additionally, it aids in structural studies (e.g., cryo-EM) to map neurosteroid binding sites and design therapies for epilepsy or postpartum mood disorders. The production of soluble, functional GABRP remains technically challenging due to its complex transmembrane structure, necessitating advanced protein engineering strategies.
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