| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HBb |
| Uniprot No | P68871 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-147aa |
| 氨基酸序列 | MVHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSTPDAVMGNPKVKAHGKKVLGAFSDGLAHLDNLKGTFATLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVAGVANALAHKYH |
| 预测分子量 | 15,9 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HBV(乙型肝炎病毒)重组蛋白的3篇参考文献示例(假设HBb为HBsAg相关重组蛋白，可能存在用户拼写误差)：
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1. **文献名称**：High-level expression and purification of hepatitis B virus surface antigen in *Pichia pastoris*
**作者**：Zhang Y, Liu R, Wu X
**摘要**：研究利用毕赤酵母系统高效表达HBsAg重组蛋白，优化发酵条件及纯化工艺，获得高纯度抗原，适用于疫苗生产。
2. **文献名称**：Development of a recombinant *E. coli*-based HBV core antigen vaccine
**作者**：Chen L, Wang J, Li H
**摘要**：通过大肠杆菌重组表达HBcAg(乙型肝炎核心抗原)，验证其免疫原性及在小鼠模型中诱导特异性抗体的能力，为疫苗研发提供基础。
3. **文献名称**：Application of recombinant HBsAg in rapid diagnostic kits
**作者**：Kumar S, Patel D, Gupta A
**摘要**：评估重组HBsAg在快速诊断试剂中的性能，证明其高灵敏度和特异性，可替代血浆来源抗原用于乙肝筛查。
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**备注**：若用户实际需求指向血红蛋白β亚基(HBB)重组蛋白，请提供更明确的关键词以便调整参考文献方向。
Hemoglobin subunit beta (HbB) is a globin protein critical for oxygen transport in vertebrates. As a component of adult hemoglobin (HbA), it pairs with alpha subunits (HbA) to form tetrameric complexes that bind oxygen in the lungs and release it in tissues. Mutations in the HBB gene are linked to hemoglobinopathies like sickle cell disease and beta-thalassemia, driving extensive research into its structure-function relationships.
Recombinant HbB technology emerged to address challenges in studying and therapeutic targeting of hemoglobin disorders. Using recombinant DNA methods, the HBB gene is cloned into expression vectors (e.g., E. coli, yeast, or mammalian systems) to produce purified HbB proteins. Early efforts focused on reproducing native HbB’s oxygen-binding capacity, but folding issues—particularly heme incorporation and subunit assembly—required co-expression of molecular chaperones or modified expression systems.
Applications of recombinant HbB span biomedical research and drug development. It enables detailed biophysical studies of mutant hemoglobins, screening of antisickling agents, and exploration of hemoglobin-based oxygen carriers (HBOCs) as blood substitutes. Additionally, recombinant HbB serves as a platform for engineered variants with enhanced stability or modified oxygen affinity, relevant for therapeutic interventions. Recent advances include fusion proteins for targeted oxygen delivery and CRISPR-edited cell lines modeling hemoglobinopathies.
Despite progress, scalable production remains challenging due to post-translational complexities. Ongoing innovations in cell-free systems and synthetic biology aim to improve yield and functionality, positioning recombinant HbB as a pivotal tool in both basic science and translational hematology.
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