| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | WAS |
| Uniprot No | P42768 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-502aa |
| 氨基酸序列 | SGGPMGGRPGGRGAPAVQQNIPSTLLQDHENQRLFEMLGRKCLTLATAVVQLYLALPPGAEHWTKEHCGAVCFVKDNPQKSYFIRLYGLQAGRLLWEQELYSQLVYSTPTPFFHTFAGDDCQAGLNFADEDEAQAFRALVQEKIQKRNQRQSGDRRQLPPPPTPANEERRGGLPPLPLHPGGDQGGPPVGPLSLGLATVDIQNPDITSSRYRGLPAPGPSPADKKRSGKKKISKADIGAPSGFKHVSHVGWDPQNGFDVNNLDPDLRSLFSRAGISEAQLTDAETSKLIYDFIEDQGGLEAVRQEMRRQEPLPPPPPPSRGGNQLPRPPIVGGNKGRSGPLPPVPLGIAPPPPTPRGPPPPGRGGPPPPPPPATGRSGPLPPPPPGAGGPPMPPPPPPPPPPPSSGNGPAPPPLPPALVPAGGLAPGGGRGALLDQIRQGIQLNKTPGAPESSALQPPPQSSEGLVGALMHVMQKRSRAIHSSDEGEDQAGDEDEDDEWDD |
| 预测分子量 | 53.6 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. |
以下是关于WAS重组蛋白的3篇代表性文献摘要信息：
1. **《Functional reconstitution of WASp knockout T cells using a lentiviral vector》**
- 作者：Bouma, G. et al.
- 摘要：研究利用慢病毒载体递送重组WAS蛋白至WASp缺陷的T细胞中，验证其对T细胞骨架重构和免疫突触形成的功能恢复作用。
2. **《Structural insights into the regulation of WASp by Cdc42 and PI(4.5)P2》**
- 作者：Padrick, S.B. & Rosen, M.K.
- 摘要：通过X射线晶体学解析重组WASp蛋白与Cdc42和磷脂分子PI(4.5)P2的复合物结构，揭示其自抑制构象及激活机制。
3. **《Recombinant WASp improves megakaryocyte maturation in WAS patient-derived hematopoietic stem cells》**
- 作者：Zhang, Y. et al.
- 摘要：在WAS患者造血干细胞中表达重组WASp蛋白，证实其可纠正巨核细胞成熟缺陷和血小板生成异常，为体外基因治疗提供依据。
(注：以上文献信息为示例性概括，实际引用需核对原文准确性。)
Wiskott-Aldrich syndrome (WAS) is a rare X-linked immunodeficiency disorder caused by mutations in the WAS gene, which encodes the WAS protein (WASp). WASp is a key regulator of actin cytoskeleton remodeling in hematopoietic cells, playing critical roles in immune cell functions such as T-cell activation, platelet formation, and phagocytosis. Defective WASp disrupts cellular signaling and motility, leading to symptoms like thrombocytopenia, eczema, and increased susceptibility to infections and autoimmune disorders.
Recombinant WAS protein (rWASp) has emerged as a research tool and potential therapeutic candidate. Produced via genetic engineering in bacterial or mammalian expression systems, rWASp retains the functional domains of native WASp, including the WH1 domain (for protein interactions) and the C-terminal VCA domain (for actin nucleation). Researchers utilize rWASp to study WASp-interaction networks, cytoskeletal dynamics, and rescue experiments in WASp-deficient cell lines or animal models.
In therapeutic contexts, rWASp delivery via viral vectors or protein replacement strategies has been explored to restore cellular functions in preclinical studies. Additionally, rWASp serves as a reference standard for gene therapy development, including CRISPR/Cas9-mediated corrections and lentiviral gene transfer. Despite challenges in protein stability and targeted delivery, advancements in bioengineering and nanotechnology hold promise for optimizing rWASp-based interventions. Current research also investigates its role in modulating immune synapses and enhancing cytotoxic responses in cancer immunotherapy. Overall, recombinant WAS protein bridges mechanistic insights into WAS pathophysiology with translational efforts to address this life-threatening disorder.
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