纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | Cit |
Uniprot No | O14578 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-2027aa |
氨基酸序列 | MLKFKYGARNPLDAGAAEPIASRASRLNLFFQGKPPFMTQQQMSPLSREGILDALFVLFEECSQPALMKIKHVSNFVRKYSDTIAELQELQPSAKDFEVRSLVGCGHFAEVQVVREKATGDIYAMKVMKKKALLAQEQVSFFEEERNILSRSTSPWIPQLQYAFQDKNHLYLVMEYQPGGDLLSLLNRYEDQLDENLIQFYLAELILAVHSVHLMGYVHRDIKPENILVDRTGHIKLVDFGSAAKMNSNKMVNAKLPIGTPDYMAPEVLTVMNGDGKGTYGLDCDWWSVGVIAYEMIYGRSPFAEGTSARTFNNIMNFQRFLKFPDDPKVSSDFLDLIQSLLCGQKERLKFEGLCCHPFFSKIDWNNIRNSPPPFVPTLKSDDDTSNFDEPEKNSWVSSSPCQLSPSGFSGEELPFVGFSYSKALGILGRSESVVSGLDSPAKTSSMEKKLLIKSKELQDSQDKCHKMEQEMTRLHRRVSEVEAVLSQKEVELKASETQRSLLEQDLATYITECSSLKRSLEQARMEVSQEDDKALQLLHDIREQSRKLQEIKEQEYQAQVEEMRLMMNQLEEDLVSARRRSDLYESELRESRLAAEEFKRKATECQHKLLKAKDQGKPEVGEYAKLEKINAEQQLKIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLQNREDSSEGIRKKLVEAEELEEKHREAQVSAQHLEVHLKQKEQHYEEKIKVLDNQIKKDLADKETLENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIVELSEANKLAANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHSDKNRLLELETRLREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLTEDNAELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRREITEREMQLTSQKQTMEALKTTCTMLEEQVMDLEALNDELLEKERQWEAWRSVLGDEKSQFECRVRELQRMLDTEKQSRARADQRITESRQVVELAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETERELKQRLLEEQAKLQQQMDLQKNHIFRLTQGLQEALDRADLLKTERSDLEYQLENIQVLYSHEKVKMEGTISQQTKLIDFLQAKMDQPAKKKKGLFSRRKEDPALPTQVPLQYNELKLALEKEKARCAELEEALQKTRIELRSAREEAAHRKATDHPHPSTPATARQQIAMSAIVRSPEHQPSAMSLLAPPSSRRKESSTPEEFSRRLKERMHHNIPHRFNVGLNMRATKCAVCLDTVHFGRQASKCLECQVMCHPKCSTCLPATCGLPAEYATHFTEAFCRDKMNSPGLQTKEPSSSLHLEGWMKVPRNNKRGQQGWDRKYIVLEGSKVLIYDNEAREAGQRPVEEFELCLPDGDVSIHGAVGASELANTAKADVPYILKMESHPHTTCWPGRTLYLLAPSFPDKQRWVTALESVVAGGRVSREKAEADAKLLGNSLLKLEGDDRLDMNCTLPFSDQVVLVGTEEGLYALNVLKNSLTHVPGIGAVFQIYIIKDLEKLLMIAGEERALCLVDVKKVKQSLAQSHLPAQPDISPNIFEAVKGCHLFGAGKIENGLCICAAMPSKVVILRYNENLSKYCIRKEIETSEPCSCIHFTNYSILIGTNKFYEIDMKQYTLEEFLDKNDHSLAPAVFAASSNSFPVSIVQVNSAGQREEYLLCFHEFGVFVDSYGRRSRTDDLKWSRLPLAFAYREPYLFVTHFNSLEVIEIQARSSAGTPARAYLDIPNPRYLGPAISSGAIYLASSYQDKLRVICCKGNLVKESGTEHHRGPSTSRSSPNKRGPPTYNEHITKRVASSPAPPEGPSHPREPSTPHRYREGRTELRRDKSPGRPLEREKSPGRMLSTRRERSPGRLFEDSSRGRLPAGAVRTPLSQVNKVWDQSSV |
预测分子量 | 231,4 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条关于Cit重组蛋白的参考文献示例(内容基于学术文献常见主题,非真实文献):
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1. **文献名称**: *"Production and Characterization of Recombinant Citrullinated Fibrinogen for Autoantibody Detection in Rheumatoid Arthritis"*
**作者**: Suzuki M, et al.
**摘要**: 本研究描述了通过大肠杆菌表达系统制备重组瓜氨酸化纤维蛋白原(Cit-Fib)的方法,并验证其在类风湿性关节炎(RA)患者血清中检测抗瓜氨酸化抗体的敏感性和特异性,为临床诊断提供新工具。
2. **文献名称**: *"Structural Insights into Citrullinated Vimentin by Recombinant Expression and X-ray Crystallography"*
**作者**: De Rycke L, et al.
**摘要**: 通过重组表达技术获得瓜氨酸化波形蛋白(Cit-Vimentin),结合X射线晶体学分析其三维结构,揭示瓜氨酸修饰对蛋白抗原表位的影响,为理解RA中自身免疫反应机制提供结构基础。
3. **文献名称**: *"Recombinant Citrullinated Histone H3 as a Novel Biomarker for Early-Stage Rheumatoid Arthritis"*
**作者**: Van Steendam K, et al.
**摘要**: 利用哺乳动物细胞系统表达重组瓜氨酸化组蛋白H3(Cit-H3),发现其在早期RA患者血清中的抗体水平显著升高,提示其作为早期诊断和疾病活动度监测的潜在标志物。
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**说明**:
- 以上文献围绕瓜氨酸化(Citrullinated, Cit)重组蛋白的制备、结构分析及临床应用展开,符合RA等自身免疫疾病的研究热点。
- 若需真实文献,建议在PubMed或Google Scholar中检索关键词:**recombinant citrullinated protein, rheumatoid arthritis, autoantibody**。
**Background of Cit Recombinant Protein**
Cit recombinant proteins, typically referring to citrullinated proteins produced via recombinant DNA technology, are engineered to study post-translational modifications (PTMs) involved in autoimmune diseases, particularly rheumatoid arthritis (RA). Citrullination, catalyzed by peptidylarginine deiminase (PAD) enzymes, converts arginine residues to citrulline, altering protein structure and function. This modification can trigger immune responses by generating neoepitopes, leading to the production of anti-citrullinated protein antibodies (ACPAs), a hallmark of RA.
Recombinant citrullinated proteins are synthesized by expressing target proteins (e.g., filaggrin, vimentin, or fibrinogen) in host systems (e.g., *E. coli*, mammalian cells), followed by *in vitro* citrullination using PAD enzymes. Alternatively, co-expression with PAD isoforms in eukaryotic systems enables site-specific citrullination during production. These proteins serve as critical tools to investigate antigen-antibody interactions, diagnose ACPAs, and explore therapeutic strategies targeting citrullination pathways.
Their recombinant nature ensures high purity, consistency, and scalability compared to isolating citrullinated proteins from biological tissues. Additionally, tagging systems (e.g., His-tag, FLAG-tag) simplify purification and detection. Research using Cit recombinant proteins has advanced understanding of RA pathogenesis, including HLA-DR4 epitope presentation, neutrophil extracellular trap (NET) involvement, and cross-reactivity mechanisms. Beyond autoimmunity, citrullination is implicated in cancer, neurodegeneration, and epigenetics, broadening the relevance of these proteins.
In summary, Cit recombinant proteins are indispensable for dissecting the biological and clinical implications of citrullination, bridging molecular insights to therapeutic innovations in autoimmune and inflammatory disorders.
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