| 纯度 | >90%SDS-PAGE. |
| 种属 | Luciola cruciata |
| 靶点 | . |
| Uniprot No | P13129 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-548aa |
| 氨基酸序列 | MENMENDENIVVGPKPFYPIEEGSAGTQLRKYMERYAKLGAIAFTNAVTGVDYSYAEYLEKSCCLGKALQNYGLVVDGRIALCSENCEEFFIPVIAGLFIGVGVAPTNEIYTLRELVHSLGISKPTIVFSSKKGLDKVITVQKTVTTIKTIVILDSKVDYRGYQCLDTFIKRNTPPGFQASSFKTVEVDRKEQVALIMNSSGSTGLPKGVQLTHENTVTRFSHARDPIYGNQVSPGTAVLTVVPFHHGFGMFTTLGYLICGFRVVMLTKFDEETFLKTLQDYKCTSVILVPTLFAILNKSELLNKYDLSNLVEIASGGAPLSKEVGEAVARRFNLPGVRQGYGLTETTSAIIITPEGDDKPGASGKVVPLFKAKVIDLDTKKSLGPNRRGEVCVKGPMLMKGYVNNPEATKELIDEEGWLHTGDIGYYDEEKHFFIVDRLKSLIKYKGYQVPPAELESVLLQHPSIFDAGVAGVPDPVAGELPGAVVVLESGKNMTEKEVMDYVASQVSNAKRLRGGVRFVDEVPKGLTGKIDGRAIREILKKPVAKM |
| 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. |
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**Background of Recombinant Proteins**
Recombinant proteins are artificially engineered proteins produced by introducing specific DNA sequences into host organisms, enabling them to express proteins that they would not naturally produce. This technology emerged in the 1970s with the advent of recombinant DNA techniques, pioneered by scientists like Stanley Cohen and Herbert Boyer. By combining DNA from different sources, researchers unlocked the ability to mass-produce proteins with tailored functions, revolutionizing biotechnology and medicine.
The production process typically involves isolating a target gene, inserting it into a plasmid vector, and introducing the vector into a host system (e.g., *E. coli*, yeast, or mammalian cells). The host’s cellular machinery then transcribes and translates the gene into the desired protein. Bacterial systems like *E. coli* are cost-effective for simple proteins, while eukaryotic systems (e.g., CHO cells) are preferred for complex proteins requiring post-translational modifications, such as antibodies or hormones.
Recombinant proteins have transformed healthcare. Insulin, the first recombinant therapeutic protein approved in 1982. replaced animal-derived insulin, improving safety and scalability. Today, they are pivotal in treating diseases (e.g., monoclonal antibodies for cancer, clotting factors for hemophilia), vaccines (e.g., hepatitis B, HPV), and diagnostic tools. Beyond medicine, they are used in industrial enzymes, agriculture, and research reagents.
Challenges persist, including optimizing expression yields, ensuring proper protein folding, and reducing production costs. Advances in synthetic biology, CRISPR, and AI-driven protein design are addressing these issues, enabling more efficient and customizable production.
In summary, recombinant protein technology bridges genetic engineering and practical applications, offering scalable solutions for global health, industry, and scientific discovery. Its continuous evolution underscores its critical role in addressing emerging biomedical and environmental challenges.
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