| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EPB42 |
| Uniprot No | P16452 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-691aa |
| 氨基酸序列 | GQALGIKSC DFQAARNNEE HHTKALSSRR LFVRRGQPFT IILYFRAPVR AFLPALKKVA LTAQTGEQPS KINRTQATFP ISSLGDRKWW SAVVEERDAQ SWTISVTTPA DAVIGHYSLL LQVSGRKQLL LGQFTLLFNP WNREDAVFLK NEAQRMEYLL NQNGLIYLGT ADCIQAESWD FGQFEGDVID LSLRLLSKDK QVEKWSQPVH VARVLGALLH FLKEQRVLPT PQTQATQEGA LLNKRRGSVP ILRQWLTGRG RPVYDGQAWV LAAVACTVLR CLGIPARVVT TFASAQGTGG RLLIDEYYNE EGLQNGEGQR GRIWIFQTST ECWMTRPALP QGYDGWQILH PSAPNGGGVL GSCDLVPVRA VKEGTLGLTP AVSDLFAAIN ASCVVWKCCE DGTLELTDSN TKYVGNNIST KGVGSDRCED ITQNYKYPEG SLQEKEVLER VEKEKMEREK DNGIRPPSLE TASPLYLLLK APSSLPLRGD AQISVTLVNH SEQEKAVQLA IGVQAVHYNG VLAAKLWRKK LHLTLSANLE KIITIGLFFS NFERNPPENT FLRLTAMATH SESNLSCFAQ EDIAICRPHL AIKMPEKAEQ YQPLTASVSL QNSLDAPMED CVISILGRGL IHRERSYRFR SVWPENTMCA KFQFTPTHVG LQRLTVEVDC NMFQNLTNYK SVTVVAPELS A |
| 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EPB42重组蛋白的参考文献示例(注：部分信息为假设性示例，实际文献需通过学术数据库验证)：
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1. **"Cloning and Functional Expression of Human Erythrocyte Membrane Protein Band 4.2 (EPB42) in E. coli"**
*Authors: Kanno R., Inoue Y., et al.*
**摘要**：本研究首次报道了人源EPB42基因的克隆及在大肠杆菌中的重组表达。通过SDS-PAGE和Western blot验证了重组蛋白的分子量及抗原性，并发现其能够与红细胞膜中的锚蛋白(ankyrin)结合，提示其在维持细胞膜稳定性中的作用。
2. **"Structural and Functional Analysis of Recombinant EPB42 Mutants Linked to Hereditary Spherocytosis"**
*Authors: Lee S.E., Mohandas N., et al.*
**摘要**：通过构建EPB42常见致病突变体(如R175C)，在哺乳动物细胞中表达重组蛋白，发现突变导致其与带3蛋白(band 3)的相互作用减弱，破坏细胞膜机械稳定性，为溶血性贫血的分子机制提供了实验依据。
3. **"High-Throughput Screening of Small Molecules Targeting EPB42-Protein Interactions Using Recombinant Probes"**
*Authors: Wang R., Delaunay J., et al.*
**摘要**：利用昆虫细胞表达系统纯化EPB42重组蛋白，开发了基于荧光共振能量转移(FRET)的药物筛选平台，鉴定出多个可增强EPB42与锚蛋白结合的化合物，为潜在治疗策略奠定基础。
4. **"Reconstitution of EPB42-ankyrin Complex in Lipid Bilayers: Insights into Erythrocyte Membrane Organization"**
*Authors: Salomao M., An X., et al.*
**摘要**：通过体外重组EPB42与锚蛋白，结合脂质体重建实验，揭示了二者协同调控细胞膜弹性的分子机制，并证明EPB42缺陷会导致膜骨架网络异常。
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**注**：以上文献为示例性内容，实际研究中请通过PubMed、Google Scholar等平台以关键词“EPB42 recombinant protein”“erythrocyte membrane protein 4.2”等检索最新或经典文献。
The EPB42 gene encodes erythrocyte membrane protein Band 4.2. a crucial component of the red blood cell (RBC) cytoskeletal network. This 77 kDa protein binds to spectrin, actin, and transmembrane proteins like band 3. maintaining membrane stability and deformability essential for RBC circulation. Its deficiency, caused by genetic mutations, is associated with hereditary spherocytosis and hemolytic anemia, characterized by fragile, spherical RBCs with reduced lifespan.
Recombinant EPB42 protein is produced through heterologous expression systems (e.g., E. coli or mammalian cells) for structural and functional studies. Researchers utilize it to investigate protein-protein interactions within the RBC membrane complex, particularly its role in bridging the lipid bilayer and cytoskeleton. This has implications for understanding anemia mechanisms and developing diagnostic tools.
Structural analysis of recombinant EPB42 reveals multiple functional domains, including a calpain protease cleavage site and a conserved N-terminal region critical for spectrin binding. In vitro studies demonstrate its calcium-dependent interaction with band 3. suggesting regulatory roles in cellular signaling. Pharmaceutical applications include screening compounds that modulate RBC membrane stability and testing gene therapy vectors for EPB42-deficient anemias.
Recent advances employ cryo-EM and X-ray crystallography of recombinant EPB42 to resolve its 3D structure, providing insights into mutation-induced conformational changes. Such research bridges hematology and biophysics, offering potential therapeutic strategies for membrane-related blood disorders while advancing fundamental knowledge of cellular biomechanics.
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