| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MAX |
| Uniprot No | P61244 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-160aa |
| 氨基酸序列 | MSDNDDIEVE SDEEQPRFQS AADKRAHHNA LERKRRDHIK DSFHSLRDSV PSLQGEKASR AQILDKATEY IQYMRRKNHT HQQDIDDLKR QNALLEQQVR ALEKARSSAQ LQTNYPSSDN SLYTNAKGST ISAFDGGSDS SSESEPEEPQ SRKKLRMEAS LEHHHHHH |
| 预测分子量 | 19 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. |
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**Background of MAX Recombinant Protein**
MAX (MYC-associated factor X) is a critical transcriptional regulator belonging to the basic helix-loop-helix leucine zipper (bHLH-Zip) protein family. It was initially identified as an obligate dimerization partner for the MYC oncoprotein, forming a heterodimer that binds to E-box DNA sequences (CACGTG) to regulate gene expression. Unlike MYC, which is tightly regulated and often dysregulated in cancers, MAX is constitutively expressed and serves as a universal interactor for multiple bHLH-Zip proteins, including MAD and MNT. These interactions create a dynamic network that fine-tunes cellular processes such as proliferation, differentiation, and apoptosis.
Recombinant MAX protein is engineered using biotechnological platforms, typically expressed in *E. coli* or mammalian systems (e.g., HEK293 cells) to ensure proper folding and post-translational modifications. The recombinant form retains the functional domains required for dimerization and DNA binding, enabling its use in *in vitro* studies to dissect MYC/MAX interaction mechanisms, screen inhibitors, or analyze DNA-binding kinetics. Its applications extend to structural biology (e.g., crystallography) and diagnostic assays targeting MYC-driven cancers.
The development of recombinant MAX has advanced research into MYC-dependent oncogenesis, a hallmark of numerous malignancies. By providing a purified, bioactive tool, scientists can explore therapeutic strategies to disrupt MYC/MAX complexes, potentially curbing uncontrolled cell growth. Additionally, MAX’s role in balancing transcriptional activation (via MYC) and repression (via MAD/MNT) underscores its importance in maintaining cellular homeostasis, making it a focal point in both cancer biology and regenerative medicine.
Quality-controlled batches of MAX recombinant protein are validated through techniques like SDS-PAGE, Western blot, and functional assays (e.g., electrophoretic mobility shift assays), ensuring reproducibility for experimental and preclinical use. Continued optimization of recombinant MAX production aims to enhance stability and scalability, supporting its expanding role in biomedical research and drug discovery.
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