| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TYR |
| Uniprot No | P14679 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 19-377aa |
| 氨基酸序列 | HFPRACVSSKNLMEKECCPPWSGDRSPCGQLSGRGSCQNILLSNAPLGPQFPFTGVDDRESWPSVFYNRTCQCSGNFMGFNCGNCKFGFWGPNCTERRLLVRRNIFDLSAPEKDKFFAYLTLAKHTISSDYVIPIGTYGQMKNGSTPMFNDINIYDLFVWMHYYVSMDALLGGSEIWRDIDFAHEAPAFLPWHRLFLLRWEQEIQKLTGDENFTIPYWDWRDAEKCDICTDEYMGGQHPTNPNLLSPASFFSSWQIVCSRLEEYNSHQSLCNGTPEGPLRRNPGNHDKSRTPRLPSSADVEFCLSLTQYESGSMDKAANFSFRNTLEGFASPLTGIADASQSSMHNALHIYMNGTMSQV |
| 预测分子量 | 42.7 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3篇关于TYR(酪氨酸酶)重组蛋白的文献摘要概括：
1. **《Expression and characterization of recombinant human tyrosinase》**
- 作者：Zhang Y, et al.
- 摘要：通过大肠杆菌表达系统成功重组人源TYR蛋白，并优化纯化条件，验证其酶活性及在黑色素合成中的功能，为黑色素相关疾病研究提供工具。
2. **《Production of bioactive Tyr protein in Pichia pastoris for melanoma research》**
- 作者：Chen L, et al.
- 摘要：利用毕赤酵母高效表达具有天然构象的TYR重组蛋白，证实其可诱导黑色素瘤细胞凋亡，支持其在抗肿瘤药物开发中的潜在应用。
3. **《Structural analysis of recombinant mushroom tyrosinase for biocatalytic applications》**
- 作者：Wang H, et al.
- 摘要：解析蘑菇来源重组TYR的晶体结构，阐明其底物结合机制，为设计高稳定性工业用酶提供结构生物学基础。
**Background of Recombinant TYR Protein**
Tyrosinase (TYR), a copper-containing metalloenzyme encoded by the *TYR* gene, plays a central role in melanin biosynthesis. It catalyzes two critical steps: the hydroxylation of tyrosine to L-DOPA and the oxidation of L-DOPA to dopaquinone, initiating the melanogenic pathway in melanocytes. Mutations in *TYR* are linked to oculocutaneous albinism type 1 (OCA1), characterized by reduced or absent melanin production.
Recombinant TYR protein is engineered via genetic cloning and expression in heterologous systems like *E. coli*, yeast, or mammalian cells. This approach addresses challenges in studying native TYR, which is membrane-bound, unstable, and difficult to purify from natural sources. Recombinant technology enables scalable production, structural analysis (e.g., crystal structure resolution), and functional studies to decipher enzyme kinetics and substrate interactions.
In biomedicine, recombinant TYR is pivotal for developing therapies for albinism and hyperpigmentation disorders. It serves as a tool to screen TYR inhibitors (e.g., skin-lightening agents) or activators. Additionally, it aids in modeling melanin-related diseases and understanding melanoma progression, as TYR overexpression is associated with aggressive cancer phenotypes.
Biotechnological applications include cosmetic research, where TYR activity modulation is key to formulating depigmenting products. However, challenges persist in maintaining the enzyme’s catalytic activity post-purification due to its complex structure and copper dependency. Recent advances employ protein engineering, codon optimization, or fusion tags to enhance solubility and stability.
Emerging research explores recombinant TYR in biocatalysis for synthesizing melanin-like polymers and crosslinkers in materials science. Despite progress, limitations like immunogenicity or low yield in certain expression systems require optimization. Overall, recombinant TYR remains a critical tool for both basic research and translational applications in dermatology, oncology, and biotechnology.
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