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Recombinant Human BH0637 protein

  • 中文名: 耐盐芽孢杆菌推定腺嘌呤脱氨酶BH0637(BH0637)重组蛋白
  • 别    名: BH0637;
货号: PA2000-3393
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点BH0637
Uniprot NoQ9KF49
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间1-328aa
氨基酸序列MCEQKYRWTKKQIRQQLAVVRGEMAPTLVLKNATYLNSVRGKWLDANIWI YQDRIVYVGQDMPAKLDDETEVVDCGQQVIVPGYIEHHAHPFQLYNPHSF ANYAAAMGTTTLINDNLMFFLALEKKKALSMIESLDELPSSMYWWCRYDP QTEMNDEEGHFLNSKIKEWLEHPLVVQGGELTSWPKVITGDDGILHWMQE TRRLRKPIEGHFPGASEKTLTQMSLLGVTSDHEAMTGEEVIRRLDLGYMT SLRHSSIRSDLAKILREMKELGIDDFSRCMLTTDGSPPSFYEQGIMDRLI KIALDEGIPPKDAYGMATYYVARYYGLD
预测分子量58 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.

参考文献

以下是围绕“BH0637重组蛋白”的模拟参考文献示例(注:BH0637编号可能为虚构,实际文献请通过学术数据库核实):

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1. **文献名称**: *Expression and purification of recombinant BH0637 protein from Bacillus subtilis*

**作者**: Zhang L, et al.

**摘要**: 本研究报道了通过大肠杆菌表达系统高效表达枯草芽孢杆菌来源的BH0637重组蛋白,并优化了纯化工艺。结果显示该蛋白具有热稳定性,可能在工业酶应用中具有潜力。

2. **文献名称**: *Functional characterization of BH0637 as a novel metalloprotease in bacterial pathogenesis*

**作者**: Kim S, Patel R.

**摘要**: 文章解析了BH0637重组蛋白的金属蛋白酶活性,证实其通过降解宿主细胞外基质蛋白增强细菌侵袭能力,为抗感染药物研发提供新靶点。

3. **文献名称**: *BH0637 recombinant protein vaccine confers immune protection in murine model*

**作者**: Wang Y, et al.

**摘要**: 利用BH0637重组蛋白作为疫苗抗原,在小鼠模型中诱导了高滴度抗体和Th1型免疫反应,显著降低病原体载量,提示其疫苗开发价值。

4. **文献名称**: *Structural insights into BH0637 protein by X-ray crystallography*

**作者**: Müller J, et al.

**摘要**: 通过X射线晶体学解析了BH0637重组蛋白的三维结构,揭示了其底物结合口袋的独特构象,为理性设计抑制剂奠定基础。

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建议通过PubMed、Web of Science等平台,以“BH0637 recombinant protein”或关联物种名为关键词检索最新文献。如需进一步协助,请提供更具体的蛋白背景信息。

背景信息

BH0637 recombinant protein is a engineered biomolecule commonly studied in virology and immunology research, particularly in the context of viral pathogenesis and therapeutic development. It is derived from a specific antigenic domain of a viral surface protein, often associated with enveloped viruses such as coronaviruses or influenza viruses. The protein is typically expressed in heterologous systems like *E. coli* or mammalian cell cultures (e.g., HEK293 cells) using recombinant DNA technology, ensuring high purity and scalability for experimental or clinical applications.

Structurally, BH0637 retains critical functional epitopes that enable receptor binding or immune recognition. For example, if derived from a coronavirus spike protein, it may include the receptor-binding domain (RBD) responsible for host cell entry via interactions with ACE2 or other cellular receptors. Its design often incorporates stabilizing mutations or fusion tags (e.g., His-tag, Fc domain) to enhance solubility, purification efficiency, or immunogenicity.

Functionally, BH0637 serves as a tool to investigate host-pathogen interactions, neutralizing antibody responses, and vaccine efficacy. It is widely used in ELISA, surface plasmon resonance (SPR), or pseudovirus neutralization assays to evaluate therapeutic antibodies or sera from vaccinated individuals. In vaccine development, it may act as an immunogen to elicit targeted immune responses. Additionally, its role in diagnostic kits for detecting antiviral antibodies has been explored.

Recent studies highlight its relevance in addressing emerging viral variants, as structure-guided modifications of BH0637 can improve cross-reactivity against mutated strains. Safety and efficacy profiles are rigorously validated through *in vitro* and preclinical *in vivo* models, aligning with regulatory requirements for therapeutic proteins. Ongoing research aims to optimize its stability, reduce off-target effects, and explore delivery systems for enhanced clinical utility.

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