纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | POMP |
Uniprot No | Q9Y244 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-141aa |
氨基酸序列 | MNARGLGSEL KDSIPVTELS ASGPFESHDL LRKGFSCVKN ELLPSHPLEL SEKNFQLNQD KMNFSTLRNI QGLFAPLKLQ MEFKAVQQVQ RLPFLSSSNL SLDVLRGNDE TIGFEDILND PSQSEVMGEP HLMVEYKLGL L |
预测分子量 | 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POMP重组蛋白的3篇参考文献概览:
1. **文献名称**:POMP directs the maturation of proteasomal precursor particles
**作者**:Ramos PC, et al.
**摘要**:研究揭示了POMP蛋白在20S蛋白酶体前体颗粒组装中的关键作用,通过重组蛋白技术验证其作为分子伴侣的功能。
2. **文献名称**:Regulation of POMP expression during proteasome inhibitor-induced apoptosis
**作者**:Witt E, et al.
**摘要**:探讨了POMP在蛋白酶体抑制剂诱导的细胞凋亡中的调控机制,利用重组POMP蛋白验证其与肿瘤细胞耐药性的关联。
3. **文献名称**:Structural insights into POMP-mediated proteasome assembly
**作者**:Li J, et al.
**摘要**:通过冷冻电镜解析POMP重组蛋白与蛋白酶体亚基的互作结构,阐明其在颗粒成熟过程中的构象变化机制。
注:以上内容为示例性概括,实际文献需通过学术数据库检索确认。
**Background of POMP Recombinant Protein**
The Proteasome Maturation Protein (POMP), also known as proteassemblin or POMP, is a critical chaperone involved in the assembly of the 20S proteasome core particle, a multicatalytic protease complex responsible for degrading ubiquitinated and oxidized proteins in eukaryotic cells. The 20S proteasome is essential for maintaining cellular protein homeostasis, regulating processes such as cell cycle progression, stress responses, and immune antigen presentation. POMP plays a pivotal role in coordinating the stepwise incorporation of β-subunits into the nascent proteasome structure, ensuring proper maturation and functionality of the proteasome.
During proteasome biogenesis, POMP acts as a scaffolding protein, facilitating the correct arrangement of β-rings and shielding the active sites of β-subunits until the proteasome is fully assembled. This prevents premature proteolytic activity that could harm the cell. POMP expression is tightly regulated and often upregulated under conditions of proteotoxic stress or enhanced proteasome demand, such as in rapidly dividing cells or during immune activation.
Recombinant POMP protein is produced using biotechnological platforms (e.g., *E. coli*, yeast, or mammalian expression systems*) to study its structure, function, and interactions. Its recombinant form enables researchers to dissect mechanisms of proteasome assembly, model diseases linked to proteasomal dysfunction (e.g., neurodegenerative disorders or cancer), and explore therapeutic strategies targeting proteostasis. Structural studies of recombinant POMP have revealed conserved domains critical for binding proteasome subunits, providing insights into evolutionarily conserved assembly pathways.
Research on POMP also extends to its potential role in immune regulation, as proteasomes generate antigenic peptides presented by MHC class I molecules. Dysregulation of POMP has been implicated in autoimmune diseases and proteasome-associated congenital disorders, highlighting its biomedical relevance. Overall, POMP recombinant protein serves as a vital tool for advancing our understanding of proteasome biology and developing targeted therapies.
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