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Recombinant Human tpl protein

  • 中文名: 丝裂原活化蛋白激酶激酶激酶8(tpl)重组蛋白
  • 别    名: tpl;COT;ESTF;Mitogen-activated protein kinase kinase kinase 8
货号: PA2000-4773
Price: ¥询价
数量:
大包装询价

产品详情

纯度>90%SDS-PAGE.
种属Human
靶点tpl
Uniprot NoQ9UKG9
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间1-612aa
氨基酸序列MENQLAKSTEERTFQYQDSLPSLPVPSLEESLKKYLESVKPFANQEEYKKTEEIVQKFQSGIGEKLHQKLLERAKGKRNWLEEWWLNVAYLDVRIPSQLNVNFAGPAAHFEHYWPPKEGTQLERGSITLWHNLNYWQLLRKEKVPVHKVGNTPLDMNQFRMLFSTCKVPGITRDSIMNYFRTESEGRSPNHIVVLCRGRAFVFDVIHEGCLVTPPELLRQLTYIHKKCHSEPDGPGIAALTSEERTRWAKAREYLIGLDPENLALLEKIQSSLLVYSMEDSSPHVTPEDYSEIIAAILIGDPTVRWGDKSYNLISFSNGVFGCNCDHAPFDAMIMVNISYYVDEKIFQNEGRWKGSEKVRDIPLPEELIFIVDEKVLNDINQAKAQYLREASDLQIAAYAFTSFGKKLTKNKMLHPDTFIQLALQLAYYRLHGHPGCCYETAMTRHFYHGRTETMRSCTVEAVRWCQSMQDPSVNLRERQQKMLQAFAKHNKMMKDCSAGKGFDRHLLGLLLIAKEEGLPVPELFTDPLFSKSGGGGNFVLSTSLVGYLRVQGVVVPMVHNGYGFFYHIRDDRFVVACSAWKSCPETDAEKLVQLTFCAFHDMIQLMNSTHL
预测分子量70,1 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

以下是关于TPL重组蛋白的3篇参考文献示例(注:部分内容为假设性概括,实际文献可能需要根据具体研究调整):

1. **文献名称**:*"Recombinant TPL-2 Kinase Expression in Escherichia coli: Purification and Functional Analysis"*

**作者**:Johnson R, et al.

**摘要**:研究利用大肠杆菌系统高效表达重组TPL-2激酶,通过亲和层析纯化获得活性蛋白,并验证其在MAPK信号通路中的催化功能,为靶向药物筛选提供工具。

2. **文献名称**:*"Role of Recombinant TPL Protein in Modulating TLR4-Mediated Inflammatory Responses"*

**作者**:Chen L, et al.

**摘要**:探讨重组TPL蛋白对TLR4信号通路的调控作用,发现其通过抑制MyD88依赖的NF-κB活化减轻脓毒症模型中的过度炎症反应。

3. **文献名称**:*"Development of a TPL-2 Recombinant Protein-Based Vaccine Adjuvant for Enhanced Cellular Immunity"*

**作者**:Martinez P, et al.

**摘要**:基于重组TPL-2蛋白设计新型疫苗佐剂,在小鼠实验中证实其可显著增强抗原特异性T细胞应答,提示其在感染性疾病疫苗中的应用潜力。

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**注意**:以上文献为示例,若需真实参考文献,建议通过PubMed或Google Scholar以关键词“TPL2 recombinant protein”“MAP3K8 expression”或“Cancer immunotherapy TPL-2”进行检索,并筛选近年高被引研究。

背景信息

**Background of TPL Recombinant Protein**

Recombinant TPL (Tyrosine Protein Lysase) is a genetically engineered protein derived from the integration of tyrosine-specific enzymatic domains into a stable, functional structure. Initially identified in bacterial systems for its role in post-translational modifications, TPL facilitates the attachment of tyrosine residues to target proteins, a process critical for modulating protein activity, stability, and interactions. The development of recombinant TPL leverages advancements in molecular cloning and expression systems, enabling large-scale production in host organisms like *E. coli* or yeast. This approach ensures high purity, consistency, and scalability, addressing limitations of native protein extraction.

The significance of TPL recombinant protein lies in its versatility across research and therapeutic applications. In biotechnology, it serves as a tool for site-specific protein labeling, aiding studies on protein dynamics and interactions. Therapeutically, TPL-based strategies are explored for targeted drug delivery and cancer treatment, leveraging its ability to modify tumor-associated proteins. Additionally, its role in synthesizing tyrosine-modified biologics enhances drug half-life and efficacy.

Recent advances in structural biology and computational design have optimized TPL’s catalytic efficiency and substrate specificity, broadening its utility. Challenges remain in minimizing immunogenicity and ensuring stability in vivo, yet ongoing engineering efforts, including fusion protein strategies and PEGylation, aim to refine its therapeutic potential. As a model system, TPL recombinant protein exemplifies the convergence of bioengineering and precision medicine, underscoring its growing importance in both industrial and academic settings.

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