| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HPR |
| Uniprot No | P00739 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 20-348aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSLYSGNDV TDISDDRFPK PPEIANGYVE HLFRYQCKNY YRLRTEGDGV YTLNDKKQWI NKAVGDKLPECEAVCGKPKN PANPVQRILG GHLDAKGSFP WQAKMVSHHN LTTGATLINE QWLLTTAKNL FLNHSENATA KDIAPTLTLY VGKKQLVEIEKVVLHPNYHQ VDIGLIKLKQ KVLVNERVMP ICLPSKNYAE VGRVGYVSGW GQSDNFKLTD HLKYVMLPVA DQYDCITHYE GSTCPKWKAP KSPVGVQPIL NEHTFCVGMS KYQEDTCYGD AGSAFAVHDL EEDTWYAAGI LSFDKSCAVA EYGVYVKVTS IQHWVQKTIA EN |
| 预测分子量 | 39 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HPR(Haptoglobin-Related Protein)重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**：*Recombinant Haptoglobin-Related Protein as a Therapeutic Candidate for Hemoglobin Clearance*
**作者**：Smith A, et al.
**摘要**：研究利用重组HPR蛋白结合游离血红蛋白的能力，评估其在溶血性疾病中清除毒性游离血红蛋白的治疗潜力。实验显示重组HPR可有效抑制血红蛋白引发的氧化损伤。
2. **文献名称**：*Expression and Functional Characterization of HPR in Parasitic Infection Models*
**作者**：Zhang L, et al.
**摘要**：通过重组表达HPR蛋白，验证其在寄生虫感染(如血吸虫)中通过结合血红素抑制寄生虫生长的机制，为抗寄生虫药物开发提供依据。
3. **文献名称**：*Structural Analysis of Recombinant HPR Reveals Key Domains for Hemoglobin Binding*
**作者**：Brown K, et al.
**摘要**：通过X射线晶体学解析重组HPR蛋白结构，阐明其与血红蛋白结合的特定结构域，为设计靶向HPR的分子提供结构基础。
(注：以上文献为虚拟示例，实际研究中建议通过PubMed或Google Scholar检索具体论文。)
**Background of HPR Recombinant Protein**
HPR (Histidine-Proline-Rich glycoprotein) is a multifunctional plasma protein primarily synthesized in the liver and widely present in vertebrates. It is characterized by its unique amino acid composition, notably high levels of histidine and proline, and a molecular weight of approximately 70-75 kDa. Structurally, HPR contains distinct domains, including a cystatin-like region, a histidine-rich region, and a proline-rich region, which contribute to its diverse biological interactions.
Functionally, HPR exhibits binding affinities for various ligands, such as heparin, metal ions (e.g., Zn²⁺), and components of the fibrinolytic and complement systems. It plays regulatory roles in immune response modulation, angiogenesis, and coagulation. HPR’s ability to interact with cell surfaces and extracellular matrix components also links it to processes like wound healing and pathogen neutralization.
Recombinant HPR (rHPR) is produced using biotechnological platforms, such as *E. coli* or mammalian cell expression systems, enabling scalable and purified protein yields. Its recombinant form retains native binding properties and bioactivity, making it valuable for research and therapeutic development.
In biomedical research, rHPR is studied for its potential in drug delivery, anticoagulant therapies, and anti-tumor strategies, owing to its anti-angiogenic effects. It also serves as a tool to investigate molecular mechanisms in thrombosis, inflammation, and infectious diseases. Additionally, HPR’s role in modulating immune cell activity has spurred interest in autoimmune and cancer immunotherapy applications.
Despite its broad functional repertoire, HPR’s precise mechanisms remain under exploration, highlighting its significance as both a biological modulator and a therapeutic candidate. Advances in recombinant technology continue to expand its utility in understanding disease pathways and developing targeted therapies.
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