纯度 | >85%SDS-PAGE. |
种属 | Human |
靶点 | XPD |
Uniprot No | P18074 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-760aa |
氨基酸序列 | MKLNVDGLLV YFPYDYIYPE QFSYMRELKR TLDAKGHGVL EMPSGTGKTV SLLALIMAYQ RAYPLEVTKL IYCSRTVPEI EKVIEELRKL LNFYEKQEGE KLPFLGLALS SRKNLCIHPE VTPLRFGKDV DGKCHSLTAS YVRAQYQHDT SLPHCRFYEE FDAHGREVPL PAGIYNLDDL KALGRRQGWC PYFLARYSIL HANVVVYSYH YLLDPKIADL VSKELARKAV VVFDEAHNID NVCIDSMSVN LTRRTLDRCQ GNLETLQKTV LRIKETDEQR LRDEYRRLVE GLREASAARE TDAHLANPVL PDEVLQEAVP GSIRTAEHFL GFLRRLLEYV KWRLRVQHVV QESPPAFLSG LAQRVCIQRK PLRFCAERLR SLLHTLEITD LADFSPLTLL ANFATLVSTY AKGFTIIIEP FDDRTPTIAN PILHFSCMDA SLAIKPVFER FQSVIITSGT LSPLDIYPKI LDFHPVTMAT FTMTLARVCL CPMIIGRGND QVAISSKFET REDIAVIRNY GNLLLEMSAV VPDGIVAFFT SYQYMESTVA SWYEQGILEN IQRNKLLFIE TQDGAETSVA LEKYQEACEN GRGAILLSVA RGKVSEGIDF VHHYGRAVIM FGVPYVYTQS RILKARLEYL RDQFQIREND FLTFDAMRHA AQCVGRAIRG KTDYGLMVFA DKRFARGDKR GKLPRWIQEH LTDANLNLTV DEGVQVAKYF LRQMAQPFHR EDQLGLSLLS LEQLESEETL KRIEQIAQQL |
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XPD重组蛋白的3篇示例参考文献(内容为模拟概括,仅供参考):
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1. **文献名称**:*Structural Insights into the Mechanism of the XPD Helicase in DNA Repair*
**作者**:Fan L. et al.
**摘要**:本研究通过X射线晶体学解析了XPD重组蛋白的ATP结合结构域与DNA复合物的三维结构,揭示了其依赖ATP水解解开DNA双链的分子机制,并阐明了突变导致着色性干皮症(XP)的分子基础。
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2. **文献名称**:*Functional Analysis of XPD Mutations in Cancer Development*
**作者**:White M.F., Sanchez A.
**摘要**:通过体外重组表达XPD突变体蛋白,作者发现某些错义突变(如R683W)显著削弱其解旋酶活性,导致核苷酸切除修复(NER)功能缺陷,解释了此类突变与多种癌症易感性的关联。
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3. **文献名称**:*XPD Helicase Dynamics in Transcription-Coupled Repair*
**作者**:Coin F., Egly J.M.
**摘要**:利用重组人XPD蛋白与RNA聚合酶II的体外互作实验,证明XPD通过动态招募TFIIH复合体参与转录偶联修复(TCR),并揭示了其在维持基因组稳定性中的双重功能角色。
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(注:以上文献信息为示例性概括,实际引用请以真实文献为准。)
**Background of XPD Recombinant Protein**
XPD (xeroderma pigmentosum complementation group D), also known as ERCC2 (Excision Repair Cross-Complementation Group 2), is a critical ATP-dependent helicase enzyme encoded by the *ERCC2* gene in humans. It plays an essential role in nucleotide excision repair (NER), a DNA repair pathway that removes bulky DNA lesions caused by UV radiation, environmental carcinogens, and chemotherapeutic agents. Additionally, XPD is a core component of the transcription factor IIH (TFIIH) complex, which is involved in both DNA repair and RNA polymerase II-mediated transcription initiation.
Recombinant XPD protein is produced through genetic engineering techniques, typically by expressing the *ERCC2* gene in bacterial (e.g., *E. coli*) or eukaryotic systems (e.g., insect or mammalian cells). This allows large-scale production of purified, functional XPD protein for biochemical and structural studies. The recombinant form retains enzymatic activities, including helicase function and ATP hydrolysis, enabling researchers to investigate its role in DNA unwinding during NER, transcription-coupled repair, and transcription regulation.
Mutations in XPD are linked to severe genetic disorders such as xeroderma pigmentosum (XP), Cockayne syndrome (CS), and trichothiodystrophy (TTD), characterized by photosensitivity, neurodegeneration, and cancer predisposition. Studying recombinant XPD aids in understanding disease mechanisms, identifying mutation-specific functional defects, and developing targeted therapies. Furthermore, XPD's dual role in DNA repair and transcription makes it a valuable model for exploring crosstalk between these processes and its implications in aging, cancer, and genomic stability.
Overall, recombinant XPD protein serves as a vital tool for elucidating molecular mechanisms in DNA repair, transcription, and human disease.
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