简介:  脂联素(Adiponectin,也叫ACRP30, GBP28）是一个分泌蛋白，在脂肪组织中特异表达，属于可溶性防御成胶质超家族。脂肪细胞产生的内源性脂联素经过转录后修饰形成多种异构体。在人血浆中，脂联素形成了几种寡聚复合物，包括三聚体、六聚体和高分子量寡聚复合物等。不同的寡聚复合物激活不同的信号传导通路，具有不同的功能。
 在不同动物模型上的药理学和遗传学研究显示脂联素具有潜在的抗糖尿病、抗动脉粥样硬化和抗炎症的功能。补充脂联素能够降低血糖水平、提高胰岛素敏感度、改善脂肪肝和预防动脉粥样硬化。而最新研究还显示脂联素具有潜在的心脏保护功能。
 和其他脂肪细胞因子不同，在肥胖病人血浆中脂联素水平降低。脂联素水平和葡萄糖、胰岛素、三甘油酯浓度及肝脏脂肪含量负相关，而和高密度脂蛋白-胆固醇水平、肝胰岛素敏感度及胰岛素刺激的葡萄糖处理正相关。长期前瞻性研究显示血清中低脂联素水平预示着未来2型糖尿病、高血压和冠状动脉疾病的可能性，而且独立于其他风险因子。相应地，高脂联素水平个体产生上述疾病的几率要小得多。脂联素是一个很好的临床相关因子，用于常规的高风险人群2型糖尿病、动脉粥样硬化和代谢综合症的检查。
本重组小鼠脂联素在转染的HEK293细胞中表达，含有FLAG标签。重组蛋白用耦联了FLAG抗体的亲和胶纯化。FLAG标签通过过量盐溶液洗涤去除，高敏MALDI-TOF分析证实纯化后的蛋白质溶液中不含FLAG肽段。

种属：本重组小鼠脂联素的氨基酸序列与小鼠血清中脂联素的氨基酸序列完全相同。
 
规格：0.1mg (BCA法测定)
 
来源： HEK293 (人胚胎肾脏细胞株)
 
纯度： >98% (HPLC及SDS-PAGE测定).
 
产品形态：冻干粉（无菌过滤，0.5mg/ml脂联素，PBS缓冲液）
 
溶解：加0.2ml去离子水，室温下彻底溶解，最终浓度为0.5mg/ml。
 
保存条件： -20℃保存。建议溶解后分装保存，避免反复冻融。溶解后可以暂时保存在4℃至两周。
 
应用： ELISA、Western blotting、细胞培养、动物研究。
 
有效期：见包装。
 
质控检测：BCA-测定蛋白浓度
SDS PAGE-测定蛋白纯度
 
注意：本产品仅用于科研。

Mouse Adiponectin, Recombinant Protein

 Specificity: The amino acid sequence of recombinant mouse adiponectin is 100% homologous to the amino acid sequence of mouse serum adiponectin.
Size: 0.1 mg (determined by BCA method)
Source: HEK293 (Human embryonic kidney cell line)
Purity: >98% (HPLC and SDS PAGE analyzed).
Formulation: Sterile filtered and lyophilized from 0.5 mg/ml in PBS buffer
Reconstitution: Add 0.2 ml of deionized water and let the lyophilized pellet dissolve completely.
 Storage: Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Applications: ELISA, Western blotting, cell culture and/or animal studies
Stability/Shelf Life: The lyophilized protein remains stable until the expiry date when stored at -20°C.
Quality Control Test: BCA - to determine content of the protein
SDS PAGE - to determine purity of the protein

ntroduction:
Adiponectin (also called ACRP30 and GBP28) is a protein exclusively secreted from adipose tissue. In the circulation, adiponectin is present as three different oligomeric complexes, including the high molecular weight (HMW), the middle molecular weight (MMW, also called hexamer) and low molecular weigh (LMW, also called trimer) forms. Different oligomeric complex of adiponectin activates different signaling pathways and exerts distinct functions.
Full-length adiponectin was expressed in HEK293 cells stably transfected with pchAd-F vector encoding FLAG epitope-tagged human adiponectin. Recombinant adiponectin was purified using anti-FLAG M2 affinity gel (Sigma-Aldrich) and was eluted with FLAG peptide. FLAG peptides were removed by an extensive wash with an excessive volume of saline. Highly sensitive matrix-assisted laser desorption/ionization time of flight (MALDI-TOF) mass-spectrometric analysis confirmed that FLAG peptide was not detectable in the protein solution.
References:
•Xu A, Wang Y, Keshaw H, Xu LY, Lam KS, Cooper GJ. The fat-derived hormone adiponectin alleviates alcoholic and nonalcoholic fatty liver diseases in mice. J Clin Invest. 2003; 112:91-100.
•Pajvani UB, Du X, Combs TP, Berg AH, Rajala MW, Schulthess T, Engel J, Brownlee M, Scherer PE. Structure-function studies of the adipocyte-secreted hormone Acrp30/adiponectin. Implications fpr metabolic regulation and bioactivity. J Biol Chem. 2003; 278:9073-85.
•Wang Y, Xu A, Knight C, Xu LY, Cooper GJ. Hydroxylation and glycosylation of the four conserved lysine residues in the collagenous domain of adiponectin. Potential role in the modulation of its insulin-sensitizing activity. J Biol Chem. 2002; 277:19521-19529.
•Yamauchi T, Kamon J, Minokoshi Y, Ito Y, Waki H, Uchida S, Yamashita S, Noda M, Kita S, Ueki K, Eto K, Akanuma Y, Froguel P, Foufelle F, Ferre P, Carling D, Kimura S, Nagai R, Kahn BB, Kadowaki T. Adiponectin stimulates glucose utilization and fatty-acid oxidation by activating AMPactivated protein kinase. Nat Med. 2002; 8:1288-1295.
•Berg AH, Combs TP, Du X, Brownlee M, Scherer PE. The adipocyte-secreted protein Acrp30 enhances hepatic insulin action. Nat Med. 2001; 7:947-953.