Recombinant Human GTF2H1 protein

中文名： 通用转录因子ⅡH肽1(GTF2H1)重组蛋白
别名： GTF2H1；XPCC；DNA repair protein complementing XP-C cells

货号: PA1000-9125

Price： ￥询价

20μg 50μg 100μg ＞100μg

数量：

大包装询价

产品详情

纯度	>90%SDS-PAGE.
种属	Human
靶点	GTF2H1
Uniprot No	P32780
内毒素	< 0.01EU/μg
表达宿主	E.coli
表达区间	1-548aa
氨基酸序列	MATSSEEVLL IVKKVRQKKQ DGALYLMAER IAWAPEGKDR FTISHMYADI KCQKISPEGK AKIQLQLVLH AGDTTNFHFS NESTAVKERD AVKDLLQQLL PKFKRKANKE LEEKNRMLQE DPVLFQLYKD LVVSQVISAE EFWANRLNVN ATDSSSTSNH KQDVGISAAF LADVRPQTDG CNGLRYNLTS DIIESIFRTY PAVKMKYAEN VPHNMTEKEF WTRFFQSHYF HRDRLNTGSK DLFAECAKID EKGLKTMVSL GVKNPLLDLT ALEDKPLDEG YGISSVPSAS NSKSIKENSN AAIIKRFNHH SAMVLAAGLR KQEAQNEQTS EPSNMDGNSG DADCFQPAVK RAKLQESIEY EDLGKNNSVK TIALNLKKSD RYYHGPTPIQ SLQYATSQDI INSFQSIRQE MEAYTPKLTQ VLSSSAASST ITALSPGGAL MQGGTQQAIN QMVPNDIQSE LKHLYVAVGE LLRHFWSCFP VNTPFLEEKV VKMKSNLERF QVTKLCPFQE KIRRQYLSTN LVSHIEEMLQ TAYNKLHTWQ SRRLMKKT
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.

参考文献

以下是关于GTF2H1重组蛋白的3篇参考文献示例(注：文献为示例，具体内容可能需要根据实际研究调整)：

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1. **文献名称**: *"Recombinant human GTF2H1 purification and functional characterization in transcription initiation"*

**作者**: Egly, J.M., et al.

**摘要**: 该研究通过重组表达系统纯化了人源GTF2H1蛋白，并验证其作为TFIIH复合体核心亚基的功能。实验表明，重组GTF2H1在体外转录体系中支持RNA聚合酶II的启动子逃逸，并参与DNA损伤修复中的核苷酸切除修复(NER)过程。

2. **文献名称**: *"Structural role of GTF2H1 in the assembly of the TFIIH complex revealed by cryo-EM"*

**作者**: Nogales, E., et al.

**摘要**: 利用冷冻电镜技术解析了包含重组GTF2H1的TFIIH全酶结构，揭示了GTF2H1在稳定TFIIH复合体构象中的关键作用，并阐明了其与XPB/XPD解旋酶亚基的相互作用机制。

3. **文献名称**: *"Functional analysis of disease-associated mutations in GTF2H1 using recombinant protein assays"*

**作者**: Coin, F., et al.

**摘要**: 通过重组GTF2H1蛋白构建了多种与遗传性疾病(如着色性干皮病)相关的突变体，发现特定突变会破坏TFIIH的ATP酶活性，从而影响转录和DNA修复功能。

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**备注**：以上文献为示例性质，实际引用时建议通过PubMed或Google Scholar以关键词“GTF2H1 recombinant protein”或“GTF2H1 purification”检索最新研究。

背景信息

**Background of GTF2H1 Recombinant Protein**

GTF2H1 (General Transcription Factor IIH Subunit 1) is a critical component of the TFIIH complex, a multifunctional protein assembly essential for transcription initiation by RNA polymerase II and nucleotide excision repair (NER) in eukaryotic cells. As part of TFIIH, GTF2H1 plays a structural and regulatory role, stabilizing interactions between core subunits like XPB (ERCC3) and XPD (ERCC2), which possess helicase activity. During transcription, TFIIH facilitates promoter unwinding and phosphorylation of RNA polymerase II, enabling transition to elongation. In DNA repair, it participates in lesion recognition and strand displacement during NER.

Recombinant GTF2H1 protein is produced via molecular cloning and expression in bacterial or eukaryotic systems, followed by purification to study its biochemical properties, interactions, and mechanisms. Its recombinant form retains functional domains, including a conserved cyclin-binding motif, enabling in vitro analysis of TFIIH assembly, transcription-coupled repair, and transcriptional regulation. Researchers utilize this tool to investigate mutations linked to diseases like xeroderma pigmentosum (XP) or Cockayne syndrome (CS), which arise from TFIIH dysfunction.

Studies involving GTF2H1 recombinant protein have advanced understanding of transcriptional dysregulation in cancers and neurodegenerative disorders. It also serves as a target for drug discovery, particularly for compounds modulating transcription or DNA repair pathways. Structural and functional insights from recombinant GTF2H1 continue to elucidate its dual role in gene expression and genome stability, highlighting its therapeutic potential in precision medicine.