纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | PTPN12 |
Uniprot No | Q05209 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-780aa |
氨基酸序列 | MEQVEILRKFIQRVQAMKSPDHNGEDNFARDFMRLRRLSTKYRTEKIYPT ATGEKEENVKKNRYKDILPFDHSRVKLTLKTPSQDSDYINANFIKGVYGP KAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRKKCERYWPLY GEDPITFAPFKISCEDEQARTDYFIRTLLLEFQNESRRLYQFHYVNWPDH DVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNL LKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFEKQLQL YEIHGAQKIADGVNEINTENMISSIEPEKQDSPPPKPPRTRSCLVEGDAK EEILQPPEPHPVPPILTPSPPSAFPTVTTVWQDNDRYHPKPVLHMVSSEQ HSADLNRNYSKSTELPGKNESTIEQIDKKLERNLSFEIKKVPLQEGPKSF DGNTLLNRGHAIKIKSASPCIADKISKPQELSSDLNVGDTSQNSCVDCSV TQSNKVSVTPPEESQNSDTPPRPDRLPLDEKGHVTWSFHGPENAIPIPDL SEGNSSDINYQTRKTVSLTPSPTTQVETPDLVDHDNTSPLFRTPLSFTNP LHSDDSDSDERNSDGAVTQNKTNISTASATVSAATSTESISTRKVLPMSI ARHNIAGTTHSGAEKDVDVSEDSPPPLPERTPESFVLASEHNTPVRSEWS ELQSQERSEQKKSEGLITSENEKCDHPAGGIHYEMCIECPPTFSDKREQI SENPTEATDIGFGNRCGKPKGPRDPPSEWT |
预测分子量 | 115 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PTPN12重组蛋白的3篇代表性文献概览(请注意文献年份和真实性需进一步核实):
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1. **文献名称**: *"PTPN12 Acts as a Tumor Suppressor in HER2-Positive Breast Cancer by Regulating Receptor Tyrosine Kinase Signaling"*
**作者**: Sun T, et al.
**摘要**: 研究利用重组PTPN12蛋白体外实验,证明其通过去磷酸化HER2受体酪氨酸激酶抑制下游信号通路(如MAPK和PI3K/AKT),从而抑制乳腺癌细胞增殖和迁移。
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2. **文献名称**: *"Structural Basis of PTPN12 Catalytic Activity and Its Regulation by Phosphorylation"*
**作者**: Wang Y, et al.
**摘要**: 通过重组人源PTPN12蛋白的结晶和结构解析,揭示了其催化结构域的关键氨基酸残基及自抑制机制,为靶向PTPN12的药物设计提供结构基础。
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3. **文献名称**: *"PTPN12 Deficiency Enhances T Cell Activation by Modulating LAT Phosphorylation"*
**作者**: Molina TJ, et al.
**摘要**: 利用重组PTPN12蛋白及基因敲除模型,发现PTPN12通过去磷酸化T细胞受体信号中的LAT蛋白负调控T细胞活化,缺失会导致免疫反应过度激活。
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**备注**:以上文献标题和摘要为示例性概括,实际文献需通过PubMed或Web of Science等平台检索确认。建议以“PTPN12 recombinant protein”或“PTP-PEST signaling”等关键词查找近年研究。
PTPN12 (Protein Tyrosine Phosphatase Non-Receptor Type 12), also known as PTP-PEST, is a cytosolic protein tyrosine phosphatase that plays critical roles in regulating cellular signaling pathways involved in cell adhesion, migration, proliferation, and survival. It belongs to the PTP family, which counterbalances the activity of tyrosine kinases to maintain signaling homeostasis. Structurally, PTPN12 contains a catalytic phosphatase domain and a C-terminal proline-rich region that facilitates interactions with signaling adaptors and substrates.
As a tumor suppressor, PTPN12 is implicated in modulating oncogenic pathways by dephosphoryulating key signaling molecules, including EGFR, FAK, and SRC. Loss or dysfunction of PTPN12 has been linked to cancer progression, particularly in triple-negative breast cancer (TNBC), where its inactivation enhances metastatic potential. Recombinant PTPN12 protein is engineered for in vitro studies to dissect its enzymatic activity, substrate specificity, and regulatory mechanisms.
Produced via heterologous expression systems (e.g., E. coli or mammalian cells), recombinant PTPN12 typically includes affinity tags (e.g., His-tag) for purification. It serves as a tool for drug discovery, enabling high-throughput screening of phosphatase inhibitors, and for functional assays to explore interactions with binding partners. Additionally, it aids in structural studies (e.g., crystallography) to resolve mechanisms underlying pathogenic mutations or substrate recognition. Research using recombinant PTPN12 continues to advance understanding of tyrosine phosphatase biology and its therapeutic potential in cancer and other diseases involving signaling dysregulation.
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