纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | KLHL12 |
Uniprot No | Q53G59 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-568aa |
氨基酸序列 | MASMTGGQQMGRGEFMGGIMAPKDIMTNTHAKSILNSMNSLRKSNTLCDV TLRVEQKDFPAHRIVLAACSDYFCAMFTSELSEKGKPYVDIQGLTASTME ILLDFVYTETVHVTVENVQELLPAACLLQLKGVKQACCEFLESQLDPSNC LGIRDFAETHNCVDLMQAAEVFSQKHFPEVVQHEEFILLSQGEVEKLIKC DEIQVDSEEPVFEAVINWVKHAKKEREESLPNLLQYVRMPLLTPRYITDV IDAEPFIRCSLQCRDLVDEAKKFHLRPELRSQMQGPRTRARLGANEVLLV VGGFGSQQSPIDVVEKYDPKTQEWSFLPSITRKRRYVASVSLHDRIYVIG GYDGRSRLSSVECLDYTADEDGVWYSVAPMNVRRGLAGATTLGDMIYVSG GFDGSRRHTSMERYDPNIDQWSMLGDMQTAREGAGLVVASGVIYCLGGYD GLNILNSVEKYDPHTGHWTNVTPMATKRSGAGVALLNDHIYVVGGFDGTA HLSSVEAYNIRTDSWTTVTSMTTPRCYVGATVLRGRLYAIAGYDGNSLLS SIECYDPIIDSWEVVTSMGTQRCDAGVCVLREK |
预测分子量 | 63 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KLHL12重组蛋白的示例参考文献(内容为模拟,实际文献需通过学术数据库查询):
---
1. **文献名称**:*KLHL12 mediates the assembly of Cullin 3 ubiquitin ligase complexes*
**作者**:Angers S. et al.
**摘要**:研究揭示了KLHL12作为接头蛋白在Cullin 3泛素连接酶复合物组装中的作用,通过重组蛋白实验证明其通过BTB结构域与Cullin 3结合,并参与底物识别和泛素化调控。
2. **文献名称**:*Structural basis for KLHL12 recognition of specific substrates in Wnt signaling*
**作者**:Chen Y. et al.
**摘要**:利用KLHL12重组蛋白进行晶体结构分析,阐明了其Kelch重复结构域如何特异性结合Wnt信号通路相关蛋白(如Dishevelled),从而调控β-catenin的稳定性。
3. **文献名称**:*KLHL12 regulates COPII coat dynamics and cargo secretion at ER-Golgi junctions*
**作者**:Jin L. et al.
**摘要**:通过体外重组蛋白实验发现,KLHL12通过泛素化修饰COPII组分Sec31.影响内质网-高尔基体运输过程中的囊泡形成和货物分泌。
4. **文献名称**:*KLHL12-dependent ubiquitination degrades the G protein-coupled receptor PAC1*
**作者**:Xu J. et al.
**摘要**:研究利用KLHL12重组蛋白及敲除模型,证实其通过Cullin 3复合物介导PAC1受体的泛素化降解,揭示了其在GPCR代谢调控中的新功能。
---
**注意**:以上为模拟文献,实际引用请通过PubMed、Web of Science或Google Scholar检索关键词(如“KLHL12 recombinant protein”“KLHL12 ubiquitin ligase”)。
KLHL12 (Kelch-like protein 12) is a member of the BTB-Kelch protein family, characterized by its conserved N-terminal BTB (Bric-a-brac, Tramtrack, and Broad Complex) domain and C-terminal Kelch repeat motifs. These structural features enable KLHL12 to act as a substrate-specific adaptor for Cullin3 (CUL3)-based E3 ubiquitin ligase complexes, facilitating the targeted ubiquitination and subsequent degradation of proteins via the proteasome. KLHL12 plays critical roles in regulating cellular processes such as protein homeostasis, signal transduction, and stress responses.
A key function of KLHL12 is its involvement in the Wnt/β-catenin signaling pathway, where it promotes the ubiquitination of Dishevelled (Dvl), a central mediator of Wnt signaling. This regulatory mechanism impacts embryonic development, tissue homeostasis, and cancer progression. Additionally, KLHL12 interacts with the corticotropin-releasing hormone receptor 1 (CRHR1), influencing G protein-coupled receptor (GPCR) trafficking and adrenal glucocorticoid synthesis. Dysregulation of KLHL12 has been linked to endocrine disorders, including Cushing’s syndrome, and malignancies such as hepatocellular carcinoma.
Recombinant KLHL12 protein, typically produced in *E. coli* or mammalian expression systems, retains its structural integrity and biochemical activity. Researchers utilize it to study ubiquitination mechanisms, screen for small-molecule modulators, and explore therapeutic strategies targeting KLHL12-associated pathways. Its role in protein degradation networks and disease relevance makes KLHL12 a compelling subject for both basic research and drug discovery. Purified recombinant forms are essential tools for crystallography, binding assays, and pathway validation studies.
×