| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PCAF |
| Uniprot No | Q92831 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 731-832 aa |
| 活性数据 | TLKSILQQVKSHQSAWPFMEPVKRTEAPGYYEVIRFPMDLKTMSERLKNRYYVSKKLFMADLQRVFTNCKEYNPPESEYYKCANILEKFFFSKIKEAGLIDK |
| 分子量 | 36.96 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 缓冲液 | 0 |
| 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. |
以下是关于重组人PCAF蛋白的3篇代表性文献的简要信息：
1. **文献名称**：**"The human monocytic leukemia zinc finger histone acetyltransferase domain as a functional surface for PCAF"**
**作者**：Mujtaba, S. et al.
**摘要**：该研究发现人PCAF蛋白的乙酰转移酶结构域可通过与白血病相关锌指蛋白的结构互作调控靶基因的乙酰化，揭示了其在表观遗传调控中的分子机制。
2. **文献名称**：**"Recombinant PCAF activates HIV-1 transcription through phosphorylation and acetylation of the viral Tat protein"**
**作者**：Col, E. et al.
**摘要**：作者利用重组PCAF蛋白证明其能通过乙酰化HIV-1病毒蛋白Tat，增强病毒转录活性，为病毒与宿主表观调控因子的互作提供了直接证据。
3. **文献名称**：**"Structural basis for substrate specificity and catalysis of human histone acetyltransferase PCAF"**
**作者**：Lin, W. et al.
**摘要**：通过解析重组人PCAF蛋白的晶体结构，该研究阐明了其底物识别的关键氨基酸残基及乙酰转移反应的催化机制，为设计靶向PCAF的药物奠定了基础。
4. **文献名称**：**"PCAF modulates p53 transcriptional activity through site-specific acetylation"**
**作者**：Liu, L. et al.
**摘要**：研究发现重组PCAF蛋白能特异性乙酰化肿瘤抑制蛋白p53的特定赖氨酸位点，增强p53对下游基因的转录激活能力，揭示了其在DNA损伤应答中的作用。
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以上文献涵盖了PCAF的结构解析、酶活机制、病毒互作及肿瘤调控等多个研究方向，主要发表在*Molecular Cell*、*EMBO Journal*等期刊。如需具体DOI或发表年份，可进一步补充说明。
PCAF (p300/CBP-associated factor), also known as KAT2B, is a histone acetyltransferase (HAT) critical for epigenetic regulation. Discovered in the 1990s as a coactivator interacting with transcriptional regulators p300 and CREB-binding protein (CBP), PCAF acetylates histones, particularly H3K9 and H4K8. loosening chromatin structure to facilitate transcriptional activation. Beyond histones, PCAF targets non-histone proteins, including transcription factors (e.g., p53. NF-κB) and viral proteins, modulating their activity, stability, or interactions. This enzyme plays roles in diverse cellular processes, such as cell differentiation, DNA repair, apoptosis, and metabolism. Dysregulation of PCAF is linked to cancers, neurodegenerative disorders, and inflammatory diseases.
Recombinant human PCAF protein is produced via genetic engineering in systems like *E. coli* or insect cells, ensuring high purity and activity for research. It serves as a tool to study HAT mechanisms, protein interactions, and epigenetic modifications. Researchers use it to screen HAT inhibitors for therapeutic development. Structural studies of recombinant PCAF, including its catalytic HAT domain and bromodomain (responsible for acetyl-lysine recognition), provide insights into substrate specificity and regulatory pathways. Its application extends to modeling epigenetic dysregulation and validating drug candidates targeting acetylation-dependent processes.
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