纯度 | > 95 % SDS-PAGE. |
种属 | Human |
靶点 | CD4 |
Uniprot No | P01730 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 26-396aa |
氨基酸序列 | KKVVLGKKGD TVELTCTASQ KKSIQFHWKN SNQIKILGNQ GSFLTKGPSK LNDRADSRRS LWDQGNFPLI IKNLKIEDSD TYICEVEDQK EEVQLLVFGL TANSDTHLLQ GQSLTLTLES PPGSSPSVQC RSPRGKNIQG GKTLSVSQLE LQDSGTWTCT VLQNQKKVEF KIDIVVLAFQ KASSIVYKKE GEQVEFSFPL AFTVEKLTGS GELWWQAERA SSSKSWITFD LKNKEVSVKR VTQDPKLQMG KKLPLHLTLP QALPQYAGSG NLTLALEAKT GKLHQEVNLV VMRATQLQKN LTCEVWGPTS PKLMLSLKLE NKEAKVSKRE KAVWVLNPEA GMWQCLLSDS GQVLLESNIK VLPTWSTPVQ P |
预测分子量 | 41 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3篇与CD4重组蛋白相关的模拟参考文献(注:文献信息为示例性构建,实际引用时请核实真实文献):
1. **文献名称**: "Recombinant Soluble CD4 Protein Blocks HIV-1 Infection in vitro"
**作者**: Smith A, et al.
**摘要**: 研究报道了重组可溶性CD4蛋白在体外实验中抑制HIV-1病毒进入宿主细胞的机制,证实其通过与病毒包膜蛋白gp120结合阻断病毒与细胞表面CD4受体的相互作用。
2. **文献名称**: "Structural Analysis of CD4 Recombinant Protein for Immunotherapy Development"
**作者**: Lee B, et al.
**摘要**: 通过X射线晶体学解析了重组CD4蛋白的三维结构,揭示了其与MHC-II分子及T细胞受体的结合位点,为基于CD4的免疫治疗药物设计提供了结构基础。
3. **文献名称**: "Engineered CD4 Fusion Proteins Enhance Anti-Tumor Immune Response"
**作者**: Zhang C, et al.
**摘要**: 开发了一种重组CD4-抗体融合蛋白,通过靶向肿瘤微环境中的抗原呈递细胞,增强T细胞活化,在小鼠模型中显著抑制肿瘤生长并延长生存期。
如需真实文献,建议通过PubMed或Google Scholar检索关键词如"recombinant CD4 protein"、"soluble CD4 immunotherapy"等,并筛选近年高影响力期刊论文。
**Background of CD4 Recombinant Protein**
CD4 is a glycoprotein expressed primarily on the surface of helper T cells, regulatory T cells, and certain dendritic cells. As a key co-receptor for T-cell receptor (TCR) signaling, it interacts with major histocompatibility complex class II (MHC II) molecules on antigen-presenting cells, stabilizing TCR-antigen binding and enhancing immune activation. Structurally, CD4 comprises four extracellular immunoglobulin-like domains (D1-D4), a transmembrane region, and a cytoplasmic tail involved in intracellular signaling.
The CD4 protein gained significant attention due to its role in HIV infection. HIV-1 envelope glycoprotein gp120 binds to CD4 as the initial step of viral entry, making CD4 a critical target for therapeutic interventions. Recombinant CD4 proteins, engineered through genetic modification and produced in systems like mammalian or bacterial cells, mimic the extracellular domains of native CD4. These proteins are designed to block HIV entry by competitively binding gp120. preventing viral attachment to host cells.
In the 1980s–1990s, recombinant soluble CD4 (sCD4) was explored as an HIV therapy but showed limited efficacy due to low potency and short half-life. However, advancements led to engineered variants, such as CD4-IgG fusion proteins (e.g., PRO 542) or CD4-based CAR-T cells, which improved antiviral activity. Beyond HIV, recombinant CD4 proteins serve as tools to study T-cell activation mechanisms, autoimmune diseases, and immune evasion strategies of pathogens.
Challenges remain in optimizing stability, affinity, and delivery methods. Current research focuses on bispecific constructs, combination therapies, and structural modifications to enhance clinical utility. Overall, recombinant CD4 proteins continue to bridge foundational immunology with translational applications in infectious diseases and immunotherapy.
在生物科技领域,蛋白研发与生产是前沿探索的关键支撑。艾普蒂作为行业内的创新者,凭借自身卓越的研发实力,每年能成功研发 1000 多种全新蛋白,在重组蛋白领域不断突破。 在重组蛋白生产过程中,艾普蒂积累了丰富且成熟的经验。从结构复杂的跨膜蛋白,到具有特定催化功能的酶、参与信号传导的激酶,再到用于免疫研究的病毒抗原,艾普蒂都能实现高效且稳定的生产。 这一成就离不开艾普蒂强大的技术平台。我们构建了多元化的重组蛋白表达系统,昆虫细胞、哺乳动物细胞以及原核蛋白表达系统协同运作。不同的表达系统各有优势,能够满足不同客户对重组蛋白的活性、产量、成本等多样化的需求,从而提供高品质、低成本的活性重组蛋白。 艾普蒂提供的不只是产品,更是从源头到终端的一站式解决方案。从最初的基因合成,精准地构建出符合要求的基因序列,到载体构建,为蛋白表达创造适宜的环境,再到蛋白质表达和纯化,每一个环节都严格把控。我们充分尊重客户的个性化需求,在表达 / 纯化标签的选择、表达宿主的确定等方面,为客户量身定制专属方案。 同时,艾普蒂还配备了多种纯化体系,能够应对不同特性蛋白的纯化需求。这种灵活性和专业性,极大地提高了蛋白表达和纯化的成功率,让客户的研究项目得以顺利推进,在生物科技的探索道路上助力每一位科研工作者迈向成功。
艾普蒂生物自主研发并建立综合性重组蛋白生产和抗体开发技术平台,包括: 哺乳动物细胞表达平台:利用哺乳动物细胞精准修饰蛋白,产出与天然蛋白相似的重组蛋白,用于药物研发、细胞治疗等。 杂交瘤开发平台:通过细胞融合筛选出稳定分泌单克隆抗体的杂交瘤细胞株,优化后的技术让抗体亲和力与特异性更高,应用于疾病诊断、免疫治疗等领域。 单 B 细胞筛选平台:FACS 用荧光标记和流式细胞仪快速分选特定 B 细胞;Beacon® 基于微流控技术,单细胞水平捕获、分析 B 细胞,挖掘抗体多样性,缩短开发周期。 凭借这些平台,艾普蒂生物为客户提供优质试剂和专业 CRO 技术服务,推动生物科技发展。
艾普蒂生物在重组蛋白和天然蛋白开发领域经验十分丰富,拥有超过 2 万种重组蛋白的开发案例。在四大重组蛋白表达平台的运用上,艾普蒂生物不仅经验老到,还积累了详实的成功案例。针对客户的工业化生产需求,我们能够定制并优化实验方案。通过小试探索、工艺放大以及条件优化等环节,对重组蛋白基因序列进行优化,全面探索多种条件,精准找出最契合客户需求的生产方法。 此外,公司还配备了自有下游验证平台,可对重组蛋白展开系统的质量检测与性能测试,涵盖蛋白互作检测、活性验证、内毒素验证等,全方位保障产品质量。 卡梅德生物同样重视蛋白工艺开发,确保生产出的蛋白质具备所需的纯度、稳定性与生物活性,这对于保障药物的安全性和有效性起着关键作用 ,与艾普蒂生物共同推动着行业的发展。
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