纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | PC |
Uniprot No | P11498 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-1178aa |
氨基酸序列 | MLKFRTVHGGLRLLGIRRTSTAPAASPNVRRLEYKPIKKVMVANRGEIAIRVFRACTELGIRTVAIYSEQDTGQMHRQKADEAYLIGRGLAPVQAYLHIPDIIKVAKENNVDAVHPGYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDAPITSLHEAHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVEIAPAAHLDPQLRTRLTSDSVKLAKQVGYENAGTVEFLVDRHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVAEGRSLPDLGLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNASAFQGAVISPHYDSLLVKVIAHGKDHPTAATKMSRALAEFRVRGVKTNIAFLQNVLNNQQFLAGTVDTQFIDENPELFQLRPAQNRAQKLLHYLGHVMVNGPTTPIPVKASPSPTDPVVPAVPIGPPPAGFRDILLREGPEGFARAVRNHPGLLLMDTTFRDAHQSLLATRVRTHDLKKIAPYVAHNFSKLFSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLRGANAVGYTNYPDNVVFKFCEVAKENGMDVFRVFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTGDVADPSRTKYSLQYYMGLAEELVRAGTHILCIKDMAGLLKPTACTMLVSSLRDRFPDLPLHIHTHDTSGAGVAAMLACAQAGADVVDVAADSMSGMTSQPSMGALVACTRGTPLDTEVPMERVFDYSEYWEGARGLYAAFDCTATMKSGNSDVYENEIPGGQYTNLHFQAHSMGLGSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGLSRAEAEAQAEELSFPRSVVEFLQGYIGVPHGGFPEPFRSKVLKDLPRVEGRPGASLPPLDLQALEKELVDRHGEEVTPEDVLSAAMYPDVFAHFKDFTATFGPLDSLNTRLFLQGPKIAEEFEVELERGKTLHIKALAVSDLNRAGQRQVFFELNGQLRSILVKDTQAMKEMHFHPKALKDVKGQIGAPMPGKVIDIKVVAGAKVAKGQPLCVLSAMKMETVVTSPMEGTVRKVHVTKDMTLEGDDLILEIE |
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. |
以下是关于重组蛋白C(Protein C)的参考文献示例,包含文献名称、作者及摘要概括:
1. **《Recombinant Human Protein C: Structure and Function》**
*作者:Johnson, R.B. et al.*
**摘要**:本研究解析了重组人蛋白C的晶体结构,揭示了其活化机制及与凝血因子相互作用的分子基础,为抗凝血疗法提供理论依据。
2. **《Expression and Purification of Recombinant Protein C in Mammalian Cells》**
*作者:Smith, L.M. et al.*
**摘要**:通过哺乳动物细胞表达系统高效制备重组蛋白C,优化纯化工艺,证实其具有与天然蛋白相似的抗凝血活性及稳定性。
3. **《Therapeutic Efficacy of Recombinant Protein C in Sepsis Models》**
*作者:Chen, H. et al.*
**摘要**:在败血症动物模型中,重组蛋白C显著降低炎症因子水平并改善凝血功能,验证了其在治疗脓毒症中的潜在应用价值。
4. **《Functional Characterization of a Novel Recombinant Protein C Variant》**
*作者:Wang, Y. et al.*
**摘要**:设计并制备了一种新型重组蛋白C变体,通过体外实验证明其增强的抗凝血活性及延长的半衰期,为优化临床制剂提供新策略。
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注:上述文献为示例,实际引用时需以真实发表的论文为准。若“PC”指其他特定蛋白(如前列腺癌相关蛋白),建议补充背景信息以调整检索方向。
**Background of Recombinant Protein C (PC)**
Recombinant Protein C (PC) is a biologically engineered version of the natural anticoagulant glycoprotein involved in regulating blood coagulation and inflammation. Native Protein C, synthesized in the liver, plays a critical role in the protein C anticoagulant pathway by inactivating clotting factors Va and VIIIa, thereby preventing excessive thrombus formation. It also exhibits anti-inflammatory and cytoprotective properties by modulating endothelial cell signaling. Deficiencies or mutations in Protein C are linked to thrombotic disorders, such as hereditary thrombophilia or severe sepsis-associated coagulopathy.
The development of recombinant Protein C (rPC) emerged to address limitations in plasma-derived Protein C, including supply constraints, risk of pathogen transmission, and batch variability. Using recombinant DNA technology, the *PROC* gene encoding human Protein C is inserted into expression systems (e.g., mammalian cells, *E. coli*, or yeast), enabling scalable and consistent production. Post-translational modifications, such as gamma-carboxylation for functional activity, are often achieved via engineered cell lines.
Recombinant PC has therapeutic applications in treating congenital Protein C deficiency, sepsis, and trauma-induced coagulopathy. It also serves as a research tool for studying thrombosis, inflammation, and endothelial dysfunction. Additionally, rPC is utilized in diagnostic assays to measure Protein C activity in clinical settings.
Despite advancements, challenges remain, including optimizing expression systems for cost-effective production, ensuring proper folding and post-translational modifications, and minimizing immunogenicity. Ongoing research focuses on bioengineering approaches, such as fusion proteins or PEGylation, to enhance stability and bioavailability. Recombinant Protein C exemplifies the intersection of biotechnology and hematology, offering tailored solutions for complex clotting disorders and advancing personalized medicine.
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