首页 / 产品 / 蛋白 / 细胞因子、趋化因子与生长因子
| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RARRES2 |
| Uniprot No | Q99969 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 21-157aa |
| 氨基酸序列 | ELTEAQRRGLQVALEEFHKHPPVQWAFQETSVESAVDTPFPAGIFVRLEFKLQQTSCRKRDWKKPECKVRPNGRKRKCLACIKLGSEDKVLGRLVHCPIETQVLREAEEHQETQCLRVQRAGEDPHSFYFPGQFAFS |
| 预测分子量 | 31.9kDa |
| 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. |
1. **"Recombinant chemerin induces chemotaxis and adipogenesis in 3T3-L1 adipocytes"**
- 作者：Bondue B, et al.
- 摘要：研究利用重组RARRES2(Chemerin)蛋白探究其对脂肪细胞趋化性和分化的影响，发现其通过激活CMKLR1受体促进细胞迁移并调节脂肪生成。
2. **"Production and functional characterization of recombinant human chemerin"**
- 作者：Wittamer V, et al.
- 摘要：报道了重组人Chemerin蛋白在大肠杆菌中的表达与纯化方法，验证其生物活性，包括免疫细胞趋化及受体结合能力，为炎症研究提供工具。
3. **"Chemerin suppresses breast cancer growth via activation of natural killer cells"**
- 作者：Wang N, et al.
- 摘要：通过重组Chemerin蛋白处理乳腺癌模型，证明其通过增强NK细胞活性抑制肿瘤生长，提示RARRES2在癌症免疫治疗中的潜在应用。
4. **"RARRES2 regulates lipid metabolic reprogramming to control the survival of dormant tumor cells"**
- 作者：Pacheco-Fernández N, et al.
- 摘要：利用重组RARRES2蛋白研究肿瘤休眠机制，发现其通过调控脂代谢重编程抑制休眠肿瘤细胞的存活，揭示代谢干预治疗新靶点。
RARRES2 (Retinoic Acid Receptor Responder 2), also known as Chemerin, is a multifunctional adipokine initially identified as a chemoattractant protein involved in immune regulation and metabolic processes. Encoded by the RARRES2 gene, this secreted protein is synthesized as a precursor (pro-Chemerin, ~163 amino acids) and undergoes proteolytic cleavage by serine proteases to generate bioactive isoforms (e.g., Chem157. Chem156. Chem155). These isoforms exhibit differential receptor-binding affinities, primarily targeting the G protein-coupled receptor CMKLR1 (ChemR23), as well as CCRL2 and GPR1.
Chemerin plays dual roles in physiological and pathological contexts. In metabolism, it regulates adipocyte differentiation, lipid metabolism, and insulin sensitivity, linking obesity to metabolic syndrome. Its immunomodulatory functions include recruiting dendritic cells, macrophages, and NK cells to inflammation sites through chemotaxis, making it critical in autoimmune diseases and infection responses. Paradoxically, RARRES2 demonstrates both tumor-suppressive and tumor-promoting activities in cancer, influencing angiogenesis, metastasis, and tumor microenvironment interactions.
Recombinant RARRES2 proteins are typically produced in Escherichia coli or mammalian expression systems to ensure proper folding and post-translational modifications (e.g., glycosylation at Asn67). Researchers utilize these proteins to investigate Chemerin's signaling mechanisms, receptor interactions, and therapeutic potential. Recent studies explore its role as a biomarker in cardiovascular diseases, psoriasis, and cancer progression. Challenges remain in elucidating isoform-specific functions and context-dependent signaling, driving ongoing interest in RARRES2 as a multifaceted regulator of immunity and metabolism.
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