美国Phoenix Secretomics是一个专业的蛋白质合成研究开发公司，目前有多种高纯度的重组蛋白推上市场，康肽生物科技特别介绍和代理这些产品。

目录	产品名称	包装	价格（元）	注明
PS001-06-RH	脂联素球状区人重组蛋白	100ug	4400	美国进口
PS001-06-RR	脂联素球状区大鼠重组蛋白	100ug	4400	美国进口
PB-ADI-01	人脂联素球状区（重组蛋白）	100UG	2500	国产
PS001-06-RM	脂联素球状区小鼠重组蛋白	100ug	4400	美国进口
EK-ADI-01	人脂联素酶联免疫三明治试剂盒	96T	4250	美国原装
EK-ADI-01	人脂联素酶联免疫三明治试剂盒	96T	2800	进口分装
EK-ADI-01	人脂联素酶联免疫三明治试剂盒	48T	1800	进口分装
EK-ADI-01-S	人脂联素样本检测技术服务（每样单孔检测）		2800起	曲线和数据处理
MAB-ADI-01-A	脂联素单克隆抗体（小鼠抗人脂联素球状区）	100 ug	2000	WB，IHC
MAB-ADI-01-B	脂联素单克隆抗体（小鼠抗人脂联素球状区）	200 ug	3800	WB，IHC
MAB-ADI-01-C	脂联素单克隆抗体（小鼠抗人脂联素球状区）	500 ug	6000	WB，IHC
MAB-ADI-01-D	脂联素单克隆抗体（小鼠抗人脂联素球状区）	1 mg	10000	WB，IHC
MAB-ADI-01-E	脂联素单克隆抗体（小鼠抗人脂联素球状区）	50 UL	1200	WB，IHC
MAB-ADI-01-E	脂联素单克隆抗体（小鼠抗人脂联素球状区）	100 UL	1900	WB，IHC
EK-ADI-02	脂联素(大鼠/小鼠）酶联免疫三明治试剂盒	96T	5500加税	美国原装
EK-ADI-03	脂联素(小鼠）酶联免疫三明治试剂盒	96T	5500加税	美国原装

A hypothetical model for the secretion and action of adiponectin.
The synthesis and secretion of adiponectin is increased by activation of the nuclear receptor PPAR-gamma, and reduced by caloric excess, presumably associated with leptin deficiency or resistance. Once released, adiponectin can directly increase fatty-acid transport, oxidation and dissipation in skeletal muscle, reducing the levels of intramyocellular lipids, thus improving insulin signaling. The protein can also increase the sensitivity of the hepatocyte to insulin, either through a direct action, or indirectly by lowering circulating lipids due to its action on muscle. Thus, administration of adiponectin can result in improved insulin sensitivity and glucose tolerance, and can correct hyperglycemia associated with obesity.
Saltiel AR. You are what you secrete. Nat Med. 2001 Aug.;7(8):887-8

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Data Sheet

Immunohistochemistry protocol of
Anti-Adiponectin Receptor 1 (41-65) (human) Purified IgG

Adiponectin (ADP) is an adipocyte hormone involved in glucose and lipid metabolism. We detected a rise in ADP in cerebrospinal fluid after intravenous (i.v.) injection, consistent with brain transport. In contrast to leptin, intracerebroventricular (i.c.v.) administration of ADP decreased body weight mainly by stimulating energy expenditure. Full-length ADP, mutant ADP with Cys39 replaced with serine, and globular ADP were effective, whereas the collagenous tail fragment was not. Lepob/ob mice were especially sensitive to i.c.v. and systemic ADP, which resulted in increased thermo genesis, weight loss and reduction in serum glucose and lipid levels. ADP also potentiated the effect of leptin on thermo genesis and lipid levels. While both hormones increased expression of hypothalamic corticotropin-releasing hormone (CRH), ADP had no substantial effect on other neuropeptide targets of leptin. In addition, ADP induced distinct Fos immuno-reactivity. Agouti (Ay/a) mice did not respond to ADP or leptin, indicating the melanocortin pathway may be a common target. These results show that ADP has unique central effects on energy homeostasis.

Adiponectin (also known as 30-kDa adipocyte complement-related protein; Acrp30) is a hormone secreted by adipocyte's that acts as an anti diabetic and anti-atherogenic adipokine. Levels of adiponectin in the blood are decreased under conditions of obesity, insulin resistance and type 2 diabetes. Administration of adiponectin causes glucose-lowering effects and ameliorates insulin resistance in mice. Conversely, adiponectin-deficient mice exhibit insulin resistance and diabetes. This insulin-sensitizing effect of adiponectin seems to be mediated by an increase in fatty-acid oxidation through activation of AMP kinase and PPAR-alpha. Here we report the cloning of complementary DNAs encoding adiponectin receptors 1 and 2 (AdipoR1 and AdipoR2) by expression cloning. AdipoR1 is abundantly expressed in skeletal muscle, whereas AdipoR2 is predominantly expressed in the liver. These two adiponectin receptors are predicted to contain seven trans membrane domains, but to be structurally and functionally distinct from G-protein-coupled receptors. Expression of AdipoR1/R2 or suppression of AdipoR1/R2 expression by small-interfering RNA supports our conclusion that they serve as receptors for globular and full-length adiponectin, and that they mediate increased AMP kinase and PPAR-alpha ligand activities, as well as fatty-acid oxidation and glucose uptake by adiponectin.

OBJECTIVE: We investigated the acute responses of plasma adiponectin levels to a test meal in lean and obese subjects. RESEARCH METHODS AND PROCEDURES: We studied 13 lean and 11 obese subjects after a 10-hour overnight fast. Glucose, insulin, and adiponectin concentrations were measured at baseline and 15, 30, 60, 120, and 180 minutes after a fixed breakfast. RESULTS: At baseline, fasting adiponectin concentrations were lower in the obese group vs. the lean group [mean (95% confidence interval): 2.9 (2.1 to 4.1) micro g/mL vs. 8.6 (6.5 to 11.3) micro g/mL], but rose 4-fold postprandially in the obese group, reaching a peak at 60 minutes [baseline: 2.9 (2.1 to 4.1) micro g/mL vs. 60 minutes: 12.1 (8.5 to 17.4) micro g/mL; p< 0.0001] and remaining elevated for the remainder of the study. There were no postprandial changes in plasma adiponectin concentrations in lean subjects. DISCUSSION: This increase of adiponectin concentrations in obese individuals might have important beneficial effects on postprandial glucose and lipid metabolism and might be viewed as a mechanism for maintaining normal glucose tolerance in those who are obese and insulin resistant.

Presently surgery is the most effective way to obtain a controlled weight reduction in morbidly obese patients. Roux-en-Y gastric bypass (RYGBP) surgery is effective and used worldwide, but the exact mechanism of action is unknown. The effect of RYGBP on ghrelin, insulin, adiponectin, and leptin levels was investigated in 66 obese subjects; mean weight 127 kg (range, 96-195 kg) and mean body mass index (BMI) 45 kg/m(2) (range, 33-64) before and after surgery. Ghrelin levels were also compared in 10 non operated and 10 operated obese, BMI-matched women. RYGBP resulted in 22% and 30% weight loss at 6 and 12 months, respectively. Ghrelin increased by 44% and 62% and adiponectin by 36% and 98%, but insulin declined by 57% and 62% and leptin by 60% and 64%. The changes were all related to the reduction in BMI. In addition, ghrelin and insulin were inversely correlated at all time points as were changes of the peptides at 12 months (F = 4.9, P = 0.031), independent of the change in BMI. No evidence for RYGBP surgery per se having an effect on ghrelin levels, independent of weight loss, was obtained. The profound changes in the regulatory peptides are likely to reflect the new state of energy balance achieved. A close inverse association between ghrelin and insulin was observed, supporting an important role for ghrelin in glucose homeostasis.

Adiponectin has recently been shown to be a promising candidate for the treatment of obesity-associated metabolic syndromes. Replenishment of recombinant adiponectin in mice can decrease hyperglycemia, reverse insulin resistance, and cause sustained weight loss without affecting food intake. Here we report its potential roles in alcoholic and nonalcoholic fatty liver diseases in mice. Circulating concentrations of adiponectin decreased significantly following chronic consumption of high-fat ethanol-containing food. Delivery of recombinant adiponectin into these mice dramatically alleviated hepatomegaly and steatosis (fatty liver) and also significantly attenuated inflammation and the elevated levels of serum alanine aminotransferase. These therapeutic effects resulted partly from the ability of adiponectin to increase carnitine palmitoyltransferase I activity and enhance hepatic fatty acid oxidation, while it decreased the activities of two key enzymes involved in fatty acid synthesis, including acetyl-Co carboxylase and fatty acid synthase. Furthermore, adiponectin treatment could suppress the hepatic production of TNF-alpha and plasma concentrations of this pro inflammatory cytokine. Adiponectin was also effective in ameliorating hepatomegaly, steatosis, and alanine aminotransferase abnormality associated with nonalcoholic obese, ob/ob mice. These results demonstrate a novel mechanism of adiponectin action and suggest a potential clinical application of adiponectin and its agonists in the treatment of liver diseases.
Xu A, et al. J Clin. Invest. 2003 July;112(1):91-100