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           Search results for: Recombinant Mouse ADIPOQ, trimeric Proteins    

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#22449980   2012/03/27 Save this To Up

Crystal structure of a single-chain trimer of human adiponectin globular domain.

Adiponectin is increasingly recognized as a potential therapeutic agent for the treatment of diabetes and other metabolic diseases. It circulates in plasma as homotrimers and higher-order oliogomers of homotrimers. To facilitate the production of active recombinant adiponectin as a therapeutic tool, we designed a single-chain globular domain adiponectin (sc-gAd) in which three monomer sequences are linked together in tandem to form one contiguous polypeptide. Here, we present the crystal structure of human sc-gAd at 2.0√Ö resolution. The structure reveals a similar trimeric topology to that of mouse gAd protein. Trimer formation is further rigidified by three calcium ions.

1518 related Products with: Crystal structure of a single-chain trimer of human adiponectin globular domain.

Proteins and Antibodies H Human tissue plasminogen Human tissue plasminogen Human Dnak (HSP70) His ta Human, Adiponectin (Trime Human , Adiponectin (Glob Mouse Anti-Human Adiponec Mouse Anti-Human Ig Kappa Mouse Anti-Human Ig Kappa Mouse Anti-Human Ig Lambd Mouse Anti-Human Ig Lambd Sheep Anti-Human Kappa Li

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#20663797   2010/08/18 Save this To Up

Expression of adiponectin receptors and effects of adiponectin isoforms in mouse preimplantation embryos.

Adiponectin, a pleiotropic hormone secreted from adipose tissue, can mediate some negative effects of obesity on female health, and can participate in the impaired reproductive performance of obese women. Using a mouse model, we investigated expression of adiponectin receptors in ovulated oocytes and in vivo derived preimplantation embryos, and tested effects of different adiponectin isoforms on development of preimplantation embryos in vitro.

1327 related Products with: Expression of adiponectin receptors and effects of adiponectin isoforms in mouse preimplantation embryos.

Mouse Anti-Human Adiponec Adiponectin Antibody Sour Recombinant Mouse Adipone Recombinant Mouse Adipone Recombinant Mouse Adipone Mouse anti human Adiponec Mouse Adiponectin ELISA K Adiponectin (mouse) Elisa Rat monoclonal anti mouse Mouse , Adiponectin HEK29 Mouse, Adiponectin (Trime Rabbit Polyclonal Antibod

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#18628355   2008/09/08 Save this To Up

Adiponectin deficiency promotes endothelial activation and profoundly exacerbates sepsis-related mortality.

Sepsis is a multifactorial, and often fatal, disorder typically characterized by widespread inflammation and immune activation with resultant endothelial activation. In the present study, we postulated that the adipokine adiponectin serves as a critical modulator of survival and endothelial activation in sepsis. To this aim, we evaluated both loss-of-function (adiponectin gene-deficient mice) and subsequent gain-of-function (recombinant adiponectin reconstitution) strategies in two well-established inflammatory models, cecal ligation perforation (CLP) and thioglyocollate-induced peritonitis. Adipoq(-/-) mice, subjected to CLP, exhibited a profound ( approximately 8-fold) reduction in survival compared with their wild-type Adipoq(+/+) littermates after 48 h. Furthermore, compared with wild-type controls, thioglycollate challenge resulted in a markedly greater influx of peritoneal neutrophils in Adipoq(-/-) mice accompanied by an excess production of key chemoattractant cytokines (IL-12p70, TNFalpha, MCP-1, and IL-6) and upregulation of aortic endothelial adhesion molecule VCAM-1 and ICAM-1 expressions. Importantly, all of these effects were blunted by recombinant total adiponectin administration given 3 days prior to thioglycollate challenge. The protective effects of adiponectin were ascribed largely to higher-order adiponectin oligomers, since administration of recombinant C39A trimeric adiponectin did not attenuate endothelial adhesion molecule expression in thioglycollate-challenged Adipoq(-/-) mice. These data suggest a critical role of adiponectin as a modulator of survival and endothelial inflammation in experimental sepsis and a potential mechanistic link between adiposity and increased sepsis.

2563 related Products with: Adiponectin deficiency promotes endothelial activation and profoundly exacerbates sepsis-related mortality.

CD31, Endothelial Cell; CD31, Endothelial Cell; Factor VIII Related Anti Factor VIII Related Anti CD34, Endothelial Cell; CD34, Endothelial Cell; CD31, Endothelial Cell; Factor VIII Related Anti CD34, Endothelial Cell; Adiponectin Human Endocrine Gland Vas Human Vascular Endothelia

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#18202126   2008/04/22 Save this To Up

Plasma adiponectin complexes have distinct biochemical characteristics.

Adipocytes release the secretory protein adiponectin in a number of different higher-order complexes. Once synthesized and assembled in the secretory pathway of the adipocyte, these complexes circulate as biochemically distinct and stable entities with little evidence of interchange between the different forms that include a high-molecular-weight (HMW) species, a hexamer (low-molecular-weight form), and a trimeric form of the complexes. Here, we validate a high-resolution gel filtration method that reproducibly separates the three complexes in recombinant adiponectin and adiponectin from human and murine samples. We demonstrate that the HMW form is prominently reduced in male vs. female subjects and in obese, insulin-resistant vs. lean, insulin-sensitive individuals. A direct comparison of human and mouse adiponectin demonstrates that the trimer is generally more abundant in human serum. Furthermore, when the production of adiponectin is reduced, either by obesity or in mice carrying only a single functional allele of the adiponectin locus, then the amount of the HMW form is selectively reduced in circulation. The complex distribution of adiponectin can be regulated in several ways. Both mouse and human HMW adiponectin are very stable under basic conditions but are exquisitely labile under acidic conditions below pH 7. Murine and human adiponectin HMW forms also display differential susceptibility to the presence of calcium in the buffer. A mutant form of adiponectin unable to bind calcium is less susceptible to changes in calcium concentrations. However, the lack of calcium binding results in a destabilization of the structure. Disulfide bond formation (at position C39) is also important for complex formation. A mutant form of adiponectin lacking C39 prominently forms HMW and trimer but not the low-molecular-weight form. Injection of adiponectin with a fluorescent label reveals that over time, the various complexes do not interconvert in vivo. The stability of adiponectin complexes highlights that the production and secretion of these forms from fat cells has a major influence on the circulating levels of each complex.

1275 related Products with: Plasma adiponectin complexes have distinct biochemical characteristics.

Non-sterile bovine plasm Non-sterile bovine plasm Non-sterile Cynomolgus m Non-sterile Cynomolgus m Non-sterile Cynomolgus m Non-sterile Cynomolgus m Non-sterile Cynomolgus m Non-sterile Cynomolgus m Non-sterile Cynomolgus m Non-sterile Cynomolgus m Non-sterile Cynomolgus m Adiponectin

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#16439533   2006/01/27 Save this To Up

Multimeric soluble CD40 ligand and GITR ligand as adjuvants for human immunodeficiency virus DNA vaccines.

For use in humans, human immunodeficiency virus (HIV) DNA vaccines may need to include immunostimulatory adjuvant molecules. CD40 ligand (CD40L), a member of the tumor necrosis factor (TNF) superfamily (TNFSF), is one candidate adjuvant, but it has been difficult to use because it is normally expressed as a trimeric membrane molecule. Soluble trimeric forms of CD40L have been produced, but in vitro data indicate that multimeric, many-trimer forms of soluble CD40L are more active. This multimerization requirement was evaluated in mice using plasmids that encoded either 1-trimer, 2-trimer, or 4-trimer soluble forms of CD40L. Fusion with the body of Acrp30 was used to produce the 2-trimer form, and fusion with the body of surfactant protein D was used to produce the 4-trimer form. Using plasmids for secreted HIV-1 antigens Gag and Env, soluble CD40L was active as an adjuvant in direct proportion to the valence of the trimers (1 < 2 < 4). These CD40L-augmented DNA vaccines elicited strong CD8(+) T-cell responses but did not elicit significant CD4(+) T-cell or antibody responses. To test the applicability of the multimeric fusion protein approach to other TNFSFs, a 4-trimer construct for the ligand of glucocorticoid-induced TNF family-related receptor (GITR) was also prepared. Multimeric soluble GITR ligand (GITRL) augmented the CD8(+) T-cell, CD4(+) T-cell, and antibody responses to DNA vaccination. In summary, multimeric CD40L and GITRL are new adjuvants for DNA vaccines. Plasmids for expressing multimeric TNFSF fusion proteins permit the rapid testing of TNFSF molecules in vivo.

1479 related Products with: Multimeric soluble CD40 ligand and GITR ligand as adjuvants for human immunodeficiency virus DNA vaccines.

Human soluble RANK Ligand Human CD40 Ligand CD40-Li RANK Ligand Soluble, Huma RANK Ligand Soluble, Huma RANK Ligand Soluble, Huma RANK Ligand Soluble, Huma RANK Ligand Soluble, Huma RANK Ligand Soluble, Huma RANK Ligand Soluble, Huma Recombinant Mouse soluble Recombinant Human CD40 Li Recombinant Human CD40 Li

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