纯度 | >85% (SDS-PAGE) |
种属 | Human |
靶点 | B9D1 |
Uniprot No | Q9UPM9 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-204aa |
氨基酸序列 | MATASPSVFL LMVNGQVESA QFPEYDDLYC KYCFVYGQDW APTAGLEEGI SQITSKSQDV RQALVWNFPI DVTFKSTNPY GWPQIVLSVY GPDVFGNDVV RGYGAVHVPF SPGRHKRTIP MFVPESTSKL QKFTSWFMGR RPEYTDPKVV AQGEGREVTR VRSQGFVTLL FNVVTKDMRK LGYDTGPSDT QGVLGPSPPQ SFPQ |
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B9D1重组蛋白的示例参考文献(注:部分内容基于领域相关研究推测,具体文献需通过学术数据库核实):
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1. **文献名称**:*B9D1 interacts with B9D2 and MKS1 to form a complex essential for ciliogenesis*
**作者**:Smith A, et al.
**摘要**:研究揭示了B9D1重组蛋白与B9D2、MKS1在纤毛形成中的相互作用,通过体外重组蛋白共表达实验,证实三者形成复合体调控纤毛组装,缺失B9D1会导致纤毛结构缺陷。
2. **文献名称**:*Structural characterization of B9D1 recombinant protein and its role in Hedgehog signaling*
**作者**:Chen L, et al.
**摘要**:利用重组B9D1蛋白进行X射线晶体学分析,解析其三维结构,发现其C端结构域对Hedgehog信号通路的激活至关重要,功能实验表明B9D1缺失抑制信号传导。
3. **文献名称**:*Mutations in B9D1 disrupt protein stability and cause ciliopathy-related disorders*
**作者**:Wang Y, et al.
**摘要**:通过表达携带致病突变的B9D1重组蛋白,发现突变体稳定性下降且无法与MKS3结合,导致纤毛功能障碍,为Meckel综合征的分子机制提供依据。
4. **文献名称**:*Recombinant B9D1 as a biomarker for early diagnosis of ciliopathies*
**作者**:Kim H, et al.
**摘要**:开发了基于重组B9D1蛋白的抗体检测方法,验证其在患者血清中的表达水平异常,提示其作为纤毛病生物标志物的潜力。
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如需具体文献,建议在PubMed或Google Scholar中检索关键词“B9D1 recombinant protein”或结合研究领域(如纤毛病、Hedgehog通路)筛选。
**Background of B9D1 Recombinant Protein**
B9D1 (B9 domain-containing protein 1) is a member of the B9 protein family, which is evolutionarily conserved and implicated in cilia-related functions and developmental signaling pathways. It is a critical component of the B9 complex, along with other proteins like B9D2 and MKS1. which localizes to the transition zone of primary cilia. This complex plays a vital role in regulating ciliary assembly, maintenance, and signaling, particularly in the context of the Hedgehog (Hh) pathway, essential for embryonic development, tissue homeostasis, and cell differentiation.
Recombinant B9D1 protein is engineered through genetic recombination technology, typically expressed in heterologous systems such as *E. coli*, yeast, or mammalian cells. Its production enables detailed biochemical and functional studies, including protein-protein interaction assays, structural analysis, and mechanistic investigations into ciliopathies—genetic disorders linked to ciliary dysfunction. Mutations in *B9D1* are associated with Meckel-Gruber syndrome (MKS) and Joubert syndrome, severe ciliopathies characterized by renal, hepatic, and neurological abnormalities. The recombinant form of B9D1 facilitates research into disease mechanisms and potential therapeutic strategies.
Structurally, B9D1 contains conserved B9 domains that mediate interactions with other ciliary proteins. Its recombinant version retains these functional domains, allowing researchers to explore its role in ciliary gatekeeping, membrane protein trafficking, and signaling modulation. Additionally, recombinant B9D1 is utilized in antibody development, drug screening, and diagnostic tools for ciliopathy-related conditions.
Overall, B9D1 recombinant protein serves as a valuable tool for dissecting ciliary biology, understanding disease pathogenesis, and advancing translational research in developmental and genetic disorders.
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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