种属：本重组人脂联素的氨基酸序列与人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。

Human Adiponectin, Recombinant Protein

 Specificity: The amino acid sequence of recombinant human adiponectin is 100% homologous to the amino acid sequence of human 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.